CN107109444A - 生产6‑碳单体的方法和材料 - Google Patents
生产6‑碳单体的方法和材料 Download PDFInfo
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- CN107109444A CN107109444A CN201580068117.6A CN201580068117A CN107109444A CN 107109444 A CN107109444 A CN 107109444A CN 201580068117 A CN201580068117 A CN 201580068117A CN 107109444 A CN107109444 A CN 107109444A
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Abstract
本文件描述了用于生产6‑羟基己酸的生物化学途径,其使用具有β‑酮硫解酶活性的多肽以形成3‑氧代‑6‑羟基己酰基CoA中间体进行。可以将6‑羟基己酸酶促转化为己二酸、己内酰胺、6‑氨基己酸、六亚甲基二胺或1,6‑己二醇。本文件还描述了生产6‑羟基己酸以及己二酸、己内酰胺、6‑氨基己酸、六亚甲基二胺和1,6‑己二醇的重组宿主。
Description
相关申请的交叉引用
本申请要求2014年11月14日提交的美国申请号62/079,903,和2015年11月13日提交的美国申请号62/255,276的权益,其公开内容通过提述以其整体并入本文。
发明领域
本发明提供了用于生产6碳单体的非天然存在的方法。本发明提供了使用具有β-酮硫解酶活性的多肽生物合成3-氧代-6-羟基己酰基CoA,并且使用一种或多种具有以下酶活性的多肽,或者使用一种或多种表达此类酶的重组宿主将3-氧代-6-羟基己酰基CoA酶促转化为6-羟基己酸:具有3-羟基酰基CoA脱氢酶活性的多肽、具有3-酮酰基CoA还原酶活性的多肽、具有烯酰CoA水合酶活性的多肽、具有反式-2-烯酰CoA还原酶活性的多肽,和具有硫酯酶活性的多肽。本发明还涉及使用一种或多种分离的酶或者使用表达一种或多种此类酶的重组宿主细胞将6-羟基己酸转化为己二酸、6-氨基己酸、六亚甲基二胺、己内酰胺,和1,6-己二醇的一种或多种的方法,所述分离的酶诸如具有脱氢酶活性的多肽、具有还原酶活性的多肽、具有水合酶活性的多肽、具有硫酯酶活性的多肽、具有单加氧酶活性的多肽、具有转氨酶活性的多肽。
发明背景
尼龙是聚酰胺,其一般通过二胺与二羧酸的缩合聚合(condensationpolymerization)合成。类似地,可以通过内酰胺的缩合聚合生成尼龙。一种普遍存在的尼龙是尼龙6,6,其通过六亚甲基二胺(HMD)和己二酸的缩合聚合生成。可以通过己内酰胺的开环聚合生成尼龙6。因此,己二酸,六亚甲基二胺和己内酰胺是尼龙生产中重要的中间体(Anton&Baird,Polyamides Fibers,Encyclopedia of Polymer Science andTechnology,2001)。
工业上,己二酸和己内酰胺通过环己烷的空气氧化产生。环己烷的空气氧化在一系列步骤中产生环己酮(K)和环己醇(A)和混合物,命名为KA油。KA油的硝酸氧化产生己二酸(Musser,Adipic acid,Ullmann's Encyclopedia of Industrial Chemistry,2000)。己内酰胺由环己酮经由其肟和随后的酸重排产生(Fuchs,Kieczka and Moran,Caprolactam,Ullmann's Encyclopedia oflndustrial Chemistry,2000)。
工业上,通过将C6构建快氢氰化成己二腈,然后氢化成HMD来制备六亚甲基二胺(HMD)(Herzog and Smiley,Hexamethylenediamine,Ullmann's Encyclopedia ofIndustrial Chemistry,2012)。
鉴于对石油化学原料的依赖;生物技术通过生物催化提供了一种替代方法。生物催化是使用生物催化剂(如酶)来进行有机化合物的生物化学转化。
生物来源的原料和石油化学原料都是用于生物催化过程的可行的原料。
发明概述
因此,针对这种背景,显然需要生产己二酸、己内酰胺、6-氨基己酸、六亚甲基二胺和1,6-己二醇(下文称为“C6构建快(C6 building block)”)的一种或多种的可持续方法,其中所述方法是基于生物催化剂的。
本文至少部分基于这样的发现,即可以构建生物化学途径,其(除其他外)使用β-酮硫解酶以生产6-羟基己酸,6-羟基己酸可以在一个或多个酶促步骤中转化为己二酸、6-氨基己酸、六亚甲基二胺、己内酰胺,或1,6-己二醇。己二酸(Adipic acid)和己二酸盐/酯、6-羟基己酸(6-hydroxyhexanoic acid)和6-羟基己酸盐/酯,以及6-氨基己酸(6-aminohexanoic acid)和6-氨基己酸盐/酯在本文中可互换使用,指任何其中性或离子化形式的化合物,包括其任何盐形式。本领域技术人员应当理解,具体形式将取决于pH。
令人惊奇地,在面对最优性原则下,已经发现可以组合适当的非天然途径、原料、宿主微生物、对宿主生物化学网络的弱化策略,和培养策略以有效地生产作为C6构建块的6-羟基己酸,或将6-羟基己酸转化为其他C6构建块,如己二酸、6-氨基己酸、六亚甲基二胺、己内酰胺,或1,6-己二醇。
在一些实施方案中,可以使用硫酯酶、醛脱氢酶、6-氧代己酸脱氢酶、7-氧代庚酸脱氢酶,或单加氧酶(例如与氧化还原酶和铁氧还蛋白组合)酶促形成末端羧基。参见图1和图2。
在一些实施方案中,可以使用ω-转氨酶或脱酰基酶酶促形成末端氨基。参见图4。ω-转氨酶可以与SEQ ID NOs.7-12中所列的任一个氨基酸序列具有至少70%序列同一性。
在一些实施方案中,可以使用醇脱氢酶酶促形成末端羟基。参见图1和图5。
一方面,本文件特征在于生产3-氧代-6-羟基己酰基CoA的方法。所述方法包括使用归类于EC.2.3.1.-(如EC 2.3.1.16或EC 2.3.1.174)下的具有β-酮硫解酶活性的多肽将4-羟基丁酰基CoA酶促转化为3-氧代-6-羟基己酰基CoA。所述具有β-酮硫解酶活性多肽可以与SEQ ID NO:1、SEQ ID NO:13或SEQ ID NO:14中所列的氨基酸序列具有至少70%序列同一性。所述方法可以包括使用以下的酶将3-氧代-6-羟基己酰基CoA酶促转化为6-羟基己酸:3-羟基酰基CoA脱氢酶或3-酮酰基CoA还原酶、烯酰CoA水合酶、反式-2-烯酰CoA还原酶,和硫酯酶或CoA转移酶。所述3-羟基酰基CoA脱氢酶或3-酮酰基CoA还原酶可以归类于EC1.1.1.35、EC 1.1.1.36、EC 1.1.1.100,或EC 1.1.1.157下。所述烯酰CoA水合酶可以被归类于EC 4.2.1.17或EC 4.2.1.119下。所述反式-2-烯酰CoA还原酶可以被归类于EC1.3.1.38、EC 1.3.1.44,或EC 1.3.1.8下。所述反式-烯酰CoA还原酶可以与SEQ ID NO:15或SEQ ID NO:16中所列的氨基酸序列具有至少70%序列同一性。
一方面,本文件特征在于生物合成6-羟基己酸的方法,所述方法包括使用归类于EC.2.3.1.-(例如EC 2.3.1.16或EC 2.3.1.174)下的β-酮硫解酶从4-羟基丁酰基CoA酶促合成3-氧代-6-羟基己酰基CoA,并且将3-氧代-6-羟基己酰基CoA酶促转化为6-羟基己酸。所述β-酮硫解酶可以与SEQ ID NO:1、SEQ ID NO:13或SEQ ID NO:14中所列的氨基酸序列具有至少70%序列同一性。可以使用3-羟基酰基CoA脱氢酶或3-酮酰基CoA还原酶将3-氧代-6-羟基己酰基CoA转化为3-羟基-6-羟基己酰基CoA,可以使用烯酰CoA水合酶将3-羟基-6-羟基己酰基CoA转化为2,3-脱氢-6-羟基己酰基CoA,可以使用反式-2-烯酰CoA还原酶将2,3-脱氢-6-羟基己酰基CoA转化为6-羟基己酰基CoA,以及可以使用硫酯酶或CoA转移酶将6-羟基己酰基CoA转化为6-羟基己酸。
任何方法还可以包括在一个或多个步骤中将6-羟基己酸酶促转化为己二酸、6-氨基己酸、己内酰胺,六亚甲基二胺,或1,6-己二醇。
例如,可以使用一种或多种以下的酶将6-羟基己酸转化为己二酸:单加氧酶、醇脱氢酶、4-羟基丁酸脱氢酶、5-羟基戊酸脱氢酶、6-羟基己酸脱氢酶、7-氧代庚酸脱氢酶、6-氧代己酸脱氢酶、5-氧代戊酸脱氢酶,或醛脱氢酶。
例如,可以使用一种或多种以下的酶将6-羟基己酸转化为6-氨基己酸:醇脱氢酶、6-羟基己酸脱氢酶、5-羟基戊酸脱氢酶、4-羟基丁酸脱氢酶,和ω-转氨酶。所述ω-转氨酶可以与SEQ ID NOs:7-12中所列的任一个氨基酸序列具有至少70%序列同一性。
例如,可以使用一种或多种以下的酶将6-羟基己酸转化为己内酰胺:醇脱氢酶、6-羟基己酸脱氢酶、5-羟基戊酸脱氢酶、4-羟基丁酸脱氢酶、ω-转氨酶,和酰胺水解酶。所述ω-转氨酶可以与SEQ ID NOs:7-12中所列的任一个氨基酸序列具有至少70%序列同一性。
例如,可以使用一种或多种以下的酶将6-羟基己酸转化为六亚甲基二胺:羧酸还原酶、ω-转氨酶、醇脱氢酶、N-乙酰基转移酶,和乙酰腐胺脱酰基酶。所述ω-转氨酶可以与SEQ ID NOs:7-12中所列的任一个氨基酸序列具有至少70%序列同一性。
例如,可以使用羧酸还原酶和醇脱氢酶将6-羟基己酸转化为1,6-己二醇。所述羧酸还原酶可以与SEQ ID NOs:2-6中所列的任一个氨基酸序列具有至少70%序列同一性。
在任何方法中,可以从2-酮戊二酸酶促生产4-羟基丁酰基CoA。例如,可以使用以下酶的一种或多种从2-酮戊二酸酶促生产4-羟基丁酰基CoA:谷氨酸合酶;2-酮戊二酸脱羧酶;支链脱羧酶;谷氨酸脱羧酶;ω-转氨酶、CoA转移酶、CoA连接酶,和醇脱氢酶。
在本文描述的任何方法中,可以使用以下的酶通过在己二酸半醛(也称为6-氧代己酸)中形成第二末端官能团来生产己二酸:(i)归类于EC 1.2.1.3下的醛脱氢酶,(ii)归类于EC 1.2.1.63下的6-氧代己酸脱氢酶如由ChnE编码,或归类于EC 1.2.1.-下的7-氧代庚酸脱氢酶(例如ThnG的基因产物)或者(iii)细胞色素P450家族中的单加氧酶。
在本文描述的任何方法中,可以使用归类于EC 2.61.18、EC 2.6.1.19、EC2.6.1.29、EC 2.6.1.48,或EC 2.6.1.82下的ω-转氨酶通过在己二酸半醛中形成第二末端官能团来生产6-氨基己酸。
在本文描述的任何方法中,可以使用归类于EC 3.5.2.-下的酰胺水解酶从6-氨基己酸生产己内酰胺。从6-氨基己酸的末端羧基和末端氨基生产与己内酰胺相关的酰胺键。
在本文描述的任何方法中,可以通过以下(i)或者(ii)在6-氨基己醛中形成第二末端官能团:(i)使用归类于EC 2.61.18、EC 2.6.1.19、EC 2.6.1.29、EC 2.6.1.48或EC2.6.1.82下的ω-转氨酶,或者(ii)使用例如归类于EC 3.5.1.17下的脱酰基酶。
在本文描述的任何方法中,可以使用归类于EC 1.1.1.-(例如EC 1.1.1.1、1.1.1.2、1.1.1.21,或1.1.1.184)下的醇脱氢酶,如由YMR318C、YqhD或CAA81612.1编码的醇脱氢酶,在6-羟基己醛中形成第二末端官能团来生产1,6己二醇。
在一些实施方案中,生物原料可以是或可以源自单糖、二糖、木质纤维素、半纤维素、纤维素、木质素、乙酰丙酸和甲酸、甘油三酯、甘油、脂肪酸、农业废物、浓缩酒糟(condensed distillers'solubles),或城市废物。
在一些实施方案中,非生物原料可以是或可以源自天然气、合成气、CO2/H2、甲醇、乙醇、苯甲酸盐、非挥发性残留物(NVR)或来自环己烷氧化过程的碱洗液(caustic wash)废物流、或对苯二甲酸/异酞酸混合物废物流。
在一些实施方案中,通过在选择的环境中连续培养来改善宿主对高浓度的一种或多种C6构件块的耐受。
在一些实施方案中,所述宿主微生物的生物化学网络是弱化的或增强的以(1)确保乙酰CoA和4-羟基丁酰基CoA的细胞内利用度,(2)创建NADH或NADPH不平衡,其仅可经由形成一种或多种C6构件块来平衡,(3)防止导致并包括C6构件块的中心代谢物、中心前体的降解和(4)确保从细胞有效的流出。
在一些实施方案中,培养策略用于实现厌氧、微需氧,或需氧培养条件。
在一些实施方案中,培养策略包括限制营养物,如限制氮、磷酸盐或氧。
在一些实施方案中,例如使用发酵策略,通过单一类型的微生物(例如含有一种或多种外源核酸的重组宿主)来生产一种或多种C6构建块。
另一方面,本文件特征在于包括至少一种编码以下酶的外源核酸的重组宿主:(i)β-酮硫解酶,(ii)硫酯酶或CoA转移酶,以及一种或多种(iii)3-羟基酰基CoA脱氢酶或3-酮酰基CoA还原酶,(iv)烯酰CoA水合酶,和(v)反式-2-烯酰CoA还原酶,所述宿主生产6-羟基己酸。
生产6-羟基己酸的宿主还可以包括一种或多种以下的外源酶:单加氧酶、醇脱氢酶、4-羟基丁酸脱氢酶、5-羟基戊酸脱氢酶、6-羟基己酸脱氢酶、7-氧代庚酸脱氢酶、6-氧代己酸脱氢酶、5-氧代戊酸脱氢酶,或醛脱氢酶,所述宿主进一步生产己二酸。
生产6-羟基己酸的宿主还可以包括一种或多种以下的外源酶:单加氧酶、转氨酶、6-羟基己酸脱氢酶、5-羟基戊酸脱氢酶、4-羟基丁酸脱氢酶,和醇脱氢酶,所述宿主进一步生产6-氨基己酸。此类宿主还可以包括外源酰胺水解酶,所述宿主进一步生产己内酰胺。
生产6-羟基己酸的宿主还可以包括一种或多种以下的外源酶:羧酸还原酶、ω-转氨酶、脱酰基酶、N-乙酰基转移酶,或醇脱氢酶,所述宿主进一步生产六亚甲基二胺。
生产6-羟基己酸的宿主还可以包括外源羧酸还原酶和外源醇脱氢酶,所述宿主进一步生产1,6-己二醇。
本文所述的任何重组宿主还可以包括一种或多种以下的外源酶:谷氨酸合酶、2-酮戊二酸脱羧酶、支链脱羧酶、谷氨酸脱羧酶、ω-转氨酶、CoA-连接酶、CoA-转移酶,和醇脱氢酶。
任何重组宿主可以是原核生物,如选自下组的原核生物:埃希氏菌属(Escherichia);梭菌属(Clostridia);棒状杆菌属(Corynebacteria);贪铜菌属(Cupriavidus);假单胞菌属(Pseudomonas);代尔夫特菌属(Delftia);芽孢杆菌属(Bacillus);乳杆菌属(Lactobacillus);乳球菌属(Lactococcus);和红球菌属(Rhodococcus)。例如,所述原核生物可以选自下组:大肠杆菌(Escherichia coli)、杨氏梭菌(Clostridium ljungdahlii)、自产乙醇梭菌(Clostridium autoethanogenum)、克鲁佛梭菌(Clostridium kluyveri)、谷氨酸棒状杆菌(Corynebacterium glutamicum)、钩虫贪铜菌(Cupriavidus necator)、耐金属贪铜菌(Cupriavidus metallidurans)、荧光假单胞菌(Pseudomonas fluorescens)、恶臭假单胞菌(Pseudomonas putida)、食油假单胞菌(Pseudomonas oleavorans)、食酸代尔夫特菌(Delftia acidovorans)、枯草芽胞杆菌(Bacillus subtillis)、德氏乳杆菌(Lactobacillus delbrueckii)、乳酸乳球菌(Lactococcus lactis),和马红球菌(Rhodococcus equi)。此类原核生物还可以是用于构建本文中所述的能够生产C6构件块的重组宿主细胞的基因的。
任何重组宿主可以是真核生物,如选自下组的真核生物:曲霉属(Aspergillus)、酵母属(Saccharomyces)、毕赤氏酵属(Pichia)、耶罗维亚酵母属(Yarrowia)、伊萨酵母属(Issatchenkia)、德巴利酵母属(Debaryomyces)、Arxula属和克鲁维酵母菌属(Kluyveromyces)。例如,所述真核生物可以选自下组:黑曲霉(Aspergillus niger)、酿酒酵母(Saccharomyces cerevisiae)、巴斯德毕赤酵母(Pichia pastoris)、解脂耶罗维亚酵母(Yarrowia lipolytica)、东方伊萨酵母(Issathenkia orientalis)、汉逊德巴利酵母(Debaryomyces hansenii)、Arxula adenoinivorans和乳酸克鲁维酵母(Kluyveromyceslactis)。此类真核生物还可以是用于构建本文中所述的能够生产C6构件块的重组宿主细胞的基因的来源。
本文所述的任何重组宿主还可以包括一种或多种以下酶的弱化:聚羟基烷酸酯(polyhydroxyalkanoate)合酶、乙酰CoA硫酯酶、形成乙酸的磷酸转乙酰酶、乙酸激酶、乳酸脱氢酶、menaquinol-富马酸氧化还原酶、形成乙醇的醇脱氢酶、丙糖磷酸异构酶、丙酮酸脱羧酶、葡萄糖-6-磷酸异构酶、消耗NADH的转氢酶、NADH特异性谷氨酸脱氢酶,和利用NADH/NADPH的谷氨酸脱氢酶、庚二酰-CoA脱氢酶;接受C6构件块和中心前体作为底物的的乙酰CoA脱氢酶;丁酰基CoA脱氢酶,或己二酰CoA合成酶。
本文所述的任何重组宿主还可以过表达一种或多种编码以下的基因:乙酰CoA合成酶;6-磷酸葡萄糖酸脱氢酶;转酮醇酶;嘌呤核苷酸转氢酶;甘油醛-3P-脱氢酶;苹果酸酶;葡萄糖-6-磷酸脱氢酶;葡萄糖脱氢酶;果糖1,6二磷酸酶;L-丙氨酸脱氢酶;L-谷氨酸脱氢酶;甲酸脱氢酶;L-谷氨酰胺合成酶;二胺转运蛋白;二羧酸转运蛋白,和/或多药转运蛋白。
本文所述的许多酶催化可逆反应,并且感兴趣的反应可以是所述反应的逆反应。示于图1至5的示意途径说明了每种中间体的感兴趣的反应。
在一些方面,本文件特征在于核酸构建体和/或表达载体,其包含(a)多核苷酸,其编码具有β-酮硫解酶活性的多肽,其中所述多核苷酸可操作地连接于一种或多种指导多肽生产的异源控制序列,并且其中所述具有β-酮硫解酶活性的多肽选自下组:(a)与SEQ IDNOs:1、13或14的多肽具有至少70%序列同一性的多肽;(b)多核苷酸,其编码具有ω-转氨酶活性的多肽,其中所述多核苷酸可操作地连接于一种或多种指导多肽生产的异源控制序列,并且其中所述具有ω-转氨酶活性的多肽选自下组:(a)与SEQ ID NOs:7-12的多肽具有至少70%序列同一性的多肽;多核苷酸,其编码具有羧酸还原酶活性的多肽,其中所述多核苷酸可操作地连接于一种或多种指导多肽生产的异源控制序列,并且其中所述具有羧酸还原酶活性的多肽选自下组:(a)与SEQ ID NOs:2-6的多肽具有至少70%序列同一性的多肽;或者(d)多核苷酸,其编码具有以下酶活性的多肽:3-羟基酰基CoA脱氢酶活性、3-酮酰基CoA还原酶活性、烯酰CoA水合酶活性、反式-2-烯酰CoA还原酶活性、硫酯酶CoA转移酶活性、单加氧酶活性、醇脱氢酶活性、4-羟基丁酸脱氢酶活性、5-羟基戊酸脱氢酶活性、6-羟基己酸脱氢酶活性、7-氧代庚酸脱氢酶活性、6-氧代己酸脱氢酶活性、5-氧代戊酸脱氢酶活性、醛脱氢酶活性、6-羟基己酸脱氢酶活性、5-羟基戊酸脱氢酶活性、ω-转氨酶活性、酰胺水解酶活性、谷氨酸合成酶活性;2-酮戊二酸脱羧酶活性;支链脱羧酶活性;谷氨酸脱羧酶活性;ω-转氨酶活性活性;CoA转移酶活性、CoA连接酶活性。在一些实施方案中,本公开提供了含有上述核酸构建体或表达载体的组合物。
一方面,本文件特征在于生产生物衍生的六碳化合物的方法。所述生产生物衍生的六碳化合物的方法可以包括在条件下培养或生长本文所述的宿主达足够的时间段以生产生物衍生的六碳化合物,其中,任选地,所述生物衍生的六碳化合物选自下组:己二酸、6-氨基己酸、六亚甲基二胺、己内酰胺,或1,6-己二醇,及它们的组合。
一方面,本文件特征在于组合物,其包含如本文所述的生物衍生的六碳化合物以及除生物衍生的六碳化合物以外的化合物,其中所述生物衍生的六碳化合物选自下组:己二酸、6-氨基己酸、六亚甲基二胺、己内酰胺,或1,6-己二醇,及它们的组合。例如,所述生物衍生的六碳化合物是宿主细胞或生物体的细胞部分。
本文件特征还在于生物基聚合物,其包含生物衍生的己二酸、6-氨基己酸、六亚甲基二胺、己内酰胺,或1,6-己二醇,及它们的组合。
本文件特征还在于生物基树脂,其包含生物衍生的己二酸、6-氨基己酸、六亚甲基二胺、己内酰胺,或1,6-己二醇,及它们的组合,以及通过模制生物基树脂获得的模制的产品。
另一方面,本文件特征在于生产生物基聚合物的方法,其包括在聚合物生产反应中将生物衍生的己二酸、6-氨基己酸、六亚甲基二胺、己内酰胺,或1,6-己二醇与其自身或另一化合物发生化学反应。
另一方面,本文件特征在于生产生物基树脂的方法,其包括在树脂生产反应中将生物衍生的己二酸、6-氨基己酸、六亚甲基二胺、己内酰胺,或1,6-己二醇与其自身或另一化合物发生化学反应。
此外,描述的是包含具有β-酮硫解酶活性的多肽的生物化学网络,其中所述具有β-酮硫解酶活性的多肽将4-羟基丁酰基CoA酶促转化为3-氧代-6-羟基己酰基CoA。
所述生物化学网络还可以包括具有3-羟基酰基CoA脱氢酶活性的多肽或具有3-酮酰基CoA还原酶活性的多肽、具有烯酰CoA水合酶活性的多肽、具有反式-2-烯酰CoA还原酶活性的多肽、具有硫酯酶或CoA转移酶活性的多肽,用于将3-氧代-6-羟基己酰基CoA酶促转化为6-羟基己酸。
生物化学网络还可以包括一种或多种具有以下酶活性的多肽将6-羟基己酸酶促转化为己二酸:单加氧酶活性、醇脱氢酶活性、4-羟基丁酸脱氢酶活性、5-羟基戊酸脱氢酶活性、6-羟基己酸脱氢酶活性、7-氧代庚酸脱氢酶活性、6-氧代己酸脱氢酶活性、5-氧代戊酸脱氢酶活性,或醛脱氢酶活性。
生物化学网络还可以包括具有ω-转氨酶活性的多肽将6-羟基己酸酶促转化为6-氨基己酸。
生物化学网络还可以包括具有酰胺水解酶活性的多肽将6-氨基己酸转化为己内酰胺。
生物化学网络还可以包括一种或多种具有ω-转氨酶或脱酰基酶活性的多肽将6-羟基己酸酶促转化为六亚甲基二胺。
生物化学网络还可以包括一种或多种具有醇脱氢酶活性的多肽,通过在6-羟基己烷中形成第二末端官能团1,6己二醇。
一方面,生物化学网络是非天然存在的生物化学网络,其包含至少一种图1至图5的底物、至少一种编码具有至少一种图1至图5的活性的多肽的外源核酸,以及至少一种图1至图5的产物。
本发明的一方面,描述的是用于形成至少一种图1至图5化合物的步骤。本发明的一方面,描述的是用于形成至少一种图1至图5化合物的手段。还描述的是使用一种或多种具有以下酶活性的多肽获得己二酸、6-氨基己酸、六亚甲基二胺、己内酰胺,或1,6-己二醇的手段:β-酮硫解酶活性、3-羟基酰基CoA脱氢酶活性、3-酮酰基CoA还原酶活性、烯酰CoA水合酶活性、反式-2-烯酰CoA还原酶活性、硫酯酶或CoA转移酶活性、单加氧酶活性、醇脱氢酶活性、4-羟基丁酸脱氢酶活性、5-羟基戊酸脱氢酶活性、6-羟基己酸脱氢酶活性、7-氧代庚酸脱氢酶活性、6-氧代己酸脱氢酶活性、5-氧代戊酸脱氢酶活性、醛脱氢酶活性、ω-转氨酶活性、酰胺水解酶活性、ω-转氨酶或脱酰基酶活性。
另一方面,本文件特征在于组合物,其包含一种或多种具有以下酶活性的多肽以及己二酸、6-氨基己酸、六亚甲基二胺、己内酰胺,或1,6-己二醇的至少一种:β-酮硫解酶活性、3-羟基酰基CoA脱氢酶活性、3-酮酰基CoA还原酶活性、烯酰CoA水合酶活性、反式-2-烯酰CoA还原酶活性、硫酯酶或CoA转移酶活性、单加氧酶活性、醇脱氢酶活性、4-羟基丁酸脱氢酶活性、5-羟基戊酸脱氢酶活性、6-羟基己酸脱氢酶活性、7-氧代庚酸脱氢酶活性、6-氧代己酸脱氢酶活性、5-氧代戊酸脱氢酶活性、醛脱氢酶活性、ω-转氨酶活性、酰胺水解酶活性、ω-转氨酶或脱酰基酶活性。所述组合物可以是细胞的。
本领域技术人员理解,当存在于亲本化合物中的酸性质子被金属离子,例如碱金属离子,碱土金属离子或铝离子替代;或与有机碱配位时,含有羧酸基团的化合物(包括但不限于有机一元酸,羟基酸,氨基酸和二羧酸)得以形成或被转化成其离子盐形式。可接受的有机碱包括但不限于乙醇胺,二乙醇胺,三乙醇胺,氨丁三醇,N-甲基葡糖胺等。可接受的无机碱包括但不限于氢氧化铝,氢氧化钙,氢氧化钾,碳酸钠,氢氧化钠等。将本发明的盐分离为盐或通过经由添加酸或用酸性离子交换树脂处理将pH降至pKa以下而转化成游离酸。
本领域技术人员理解,含有胺基团的化合物(包括但不限于有机胺,氨基酸和二胺)得以形成或被转化为它们的离子盐形式,例如通过向胺中加入酸性质子形成铵盐,与无机酸如盐酸,氢溴酸,硫酸,硝酸,磷酸等形成;或与有机酸形成,包括但不限于乙酸,丙酸,己酸,环戊烷丙酸,乙醇酸,丙酮酸,乳酸,丙二酸,琥珀酸,苹果酸,马来酸,富马酸,酒石酸,柠檬酸,苯甲酸,3-(4-羟基苯甲酰基)苯甲酸,肉桂酸,扁桃酸,甲磺酸,乙磺酸,1,2-乙二磺酸,2-羟基乙磺酸,苯磺酸,2-萘磺酸,4-甲基双环-[2.2.2]辛-2-烯-1-羧酸,葡庚糖酸,4,4'-亚甲基双-(3-羟基-2-烯-1-羧酸),3-苯基丙酸,三甲基乙酸,叔丁基乙酸,月桂基硫酸,葡糖酸,谷氨酸,羟基萘甲酸,水杨酸,硬脂酸,粘康酸等。可接受的无机碱包括但不限于氢氧化铝,氢氧化钙,氢氧化钾,碳酸钠,氢氧化钠等。本发明的盐以盐的形式分离或通过经由添加碱或用碱性离子交换树脂处理将pH至高于pKb转化成游离胺。
本领域技术人员理解,含有胺基团和羧酸基团两者的化合物(包括但不限于氨基酸)通过以下形成或转化成它们的离子盐形式:通过1)与无机酸形成的酸加成盐,所述无机酸包括但不限于盐酸,氢溴酸,硫酸,硝酸,磷酸等;或与有机酸形成的酸加成盐,所述有机酸包括但不限于乙酸,丙酸,己酸,环戊烷丙酸,乙醇酸,丙酮酸,乳酸,丙二酸,琥珀酸,苹果酸,马来酸,富马酸,酒石酸,柠檬酸,苯甲酸,3-(4-羟基苯甲酰基)苯甲酸,肉桂酸,扁桃酸,甲磺酸,乙磺酸,1,2-乙二磺酸,2-羟基乙磺酸,苯磺酸,2-萘磺酸,4-甲基双环-[2.2.2]辛-2-烯-1-羧酸,葡庚糖酸,4,4'-亚甲基双-(3-羟基-2-烯-1-羧酸),3-苯基丙酸,三甲基乙酸酸,叔丁基乙酸,月桂基硫酸,葡糖酸,谷氨酸,羟基萘甲酸,水杨酸,硬脂酸,粘康酸等。可接受的无机碱包括但不限于氢氧化铝,氢氧化钙,氢氧化钾,碳酸钠,氢氧化钠等,或2)当存在于亲本化合物中的酸性质子被金属离子,例如碱金属离子,碱土金属离子或铝离子置换时;或与有机碱配位。可接受的有机碱包括但不限于乙醇胺,二乙醇胺,三乙醇胺,氨丁三醇,N-甲基葡糖胺等。可接受的无机碱包括但不限于氢氧化铝,氢氧化钙,氢氧化钾,碳酸钠,氢氧化钠等。本发明的盐可以作为盐分离或通过经由添加酸或用酸性离子交换树脂处理将pH降至pKa以下而转化为游离酸。
除非另有定义,本文中使用的所有技术和科学术语与本发明所属领域的普通技术人员的通常理解具有相同的含义。尽管与本文中所述的方法和材料类似或等同的方法和材料可用于实施本发明,但下文描述了合适的方法和材料。本文中提及的所有出版物,专利申请,专利和其它参考文献,包括具有登录号的GenBank和NCBI提交物通过引用整体并入。在冲突的情况下,以本说明书(包括定义)为准。此外,材料,该方法和实施例仅仅是说明性的,而不是限制性的。
在下面的附图和描述中阐述了本发明的一个或多个实施例的细节。本发明的其它特征,目的和优点将从说明书和附图以及权利要求书中显而易见。根据专利法中的标准实践,权利要求书中的词语“包括”可以被“基本上由...组成”或由“由...组成”替代。
附图简述
图1是使用2-酮戊二酸作为中心代谢物导致6-羟基己酸的示例性生物化学途径的示意图。
图2是使用6-羟基己酸作为中心前体导致己二酸的示例性生物化学途径的示意图。
图3是使用6-羟基己酸作为中心前体导致6-氨基己酸的示例性生物化学途径的示意图,以及从6-氨基己酸导致己内酰胺的示例性生物化学途径的示意图。
图4是使用6-氨基己酸、6-羟基己酸、己二酸半醛,或1,6-己二醇作为中心前体导致六亚甲基二胺的示例性生物化学途径的示意图。
图5是使用6-羟基己酸作为中心前体导致1,6-己二醇的示例性生物化学途径的示意图。
图6包含以下酶的氨基酸序列:钩虫贪铜菌(Cupriavidus necator)β-酮硫解酶(参见GenBank登录号AAC38322.1,SEQ ID NO:1)、海分枝杆菌(Mycobacterium marinum)羧酸还原酶(参见GenBank登录号ACC40567.1,SEQ ID NO:2)、耻垢分枝杆菌(Mycobacteriumsmegmatis)羧酸还原酶(参见GenBank登录号ABK71854.1,SEQ ID NO:3)、Segniliparusrugosus羧酸还原酶(参见GenBank登录号EFV11917.1,SEQ ID NO:4)、马赛分枝杆菌(Mycobacterium massiliense)羧酸还原酶(参见GenBank登录号EIVl 1 143.1,SEQ IDNO:5)、Segniliparus rotundus羧酸还原酶(参见GenBank登录号ADG98140.1,SEQ ID NO:6)、紫色色杆菌(Chromobacterium violaceum)ω-转氨酶(参见GenBank登录号AAQ59697.1,SEQ ID NO:7)、铜绿假单胞菌(Pseudomonas aeruginosa)ω-转氨酶(参见GenBank登录号AAG08191.1,SEQ ID NO:8)、丁香假单胞菌(Pseudomonas syringae)ω-转氨酶(参见Genbank登录号AAY39893.1,SEQ ID NO:9)、球形红杆菌(Rhodobactersphaeroides)ω-转氨酶(参见GenBank登录号ABA81135.1,SEQ ID NO:10)、大肠杆菌ω-转氨酶(参见GenBank登录号AAA57874.1,SEQ ID NO:11)、河流弧菌(Vibriofluvialis)ω-转氨酶(参见GenBank登录号AEA39183.1,SEQ ID NO:12)、大肠杆菌β-酮硫解酶(参见GenBank登录号AAC74479.1,SEQ ID NO:13)、氨基丁酸羧菌(Clostridium aminobutyricum)CoA转移酶(参见GenBank登录号CAB60036.2,SEQ ID NO:14)、齿垢密螺旋体(Treponemadenticola)烯酰CoA还原酶(参见GenBank登录号AAS11092.1,SEQ ID NO:15)、Euglenagracilis烯酰CoA还原酶(参见GenBank登录号AAW66853.1,SEQ ID NO:16)以及鼠伤寒沙门氏菌(Salmonella typhimurium)脱羧酶(参见GenBank登录号CAC48239.1,SEQ ID NO:17)。
图7是总结了20分钟后在340nm处吸光度变化的柱状图,其是仅酶对照(无底物)的NADPH消耗和羧酸还原酶活性的量度。
图8是20分钟后在340nm处吸光度变化的柱状图,其是相对于空载体对照的NADPH消耗和将6-羟基己酸转化为6-羟基己醛的羧酸还原酶活性的量度。
图9是20分钟后在340nm处吸光度变化的柱状图,其是相对于空载体对照的NADPH消耗和将N6-乙酰基-6-氨基己酸转化为N6-乙酰基-6-氨基己醛的羧酸还原酶活性的量度。
图10是20分钟后在340nm处吸光度变化的柱状图,其是相对于空载体对照的NADPH消耗和将己二酸半醛转化为己二醛的羧酸还原酶活性的量度。
图11是总结了4小时后丙酮酸至L-丙氨酸的转化百分比(mol/mol)的柱状图,其作为仅酶的对照(无底物)的ω-转氨酶活性的量度。
图12是24小时后丙酮酸至L-丙氨酸的转化百分比(mol/mol)的柱状图,其作为相对于空载体对照的将6-氨基己酸转化为己二酸半醛的ω-转氨酶活性的量度。
图13是4小时后L-丙氨酸至丙酮酸的转化百分比(mol/mol)的柱状图,其作为相对于空载体对照的将己二酸半醛转化为6-氨基己酸的ω-转氨酶活性的量度。
图14是4小时后丙酮酸至L-丙氨酸的转化百分比(mol/mol)的柱状图,其作为相对于空载体对照的将六亚甲基二胺转化为6-氨基己醛的ω-转氨酶活性的量度。
图15是4小时后丙酮酸至L-丙氨酸的转化百分比(mol/mol)的柱状图,其作为相对于空载体对照的将N6-乙酰基-1,6-二氨基己烷转化为N6-乙酰基-6-氨基己醛的ω-转氨酶活性的量度。
图16是4小时后丙酮酸至L-丙氨酸的转化百分比(mol/mol)的柱状图,其作为相对于空载体对照的将6-氨基己醇转化为6-氧代己醇的ω-转氨酶活性的量度。
发明详述
一般而言,本文件提供了用于生产6-羟基己酸或己二酸、己内酰胺、6-氨基己酸、六亚甲基二胺,或1,6-己二醇的一种或多种(所有这些都被称为C6构件块)的酶、非天然途径、培养策略、原料、宿主微生物和宿主生物化学网络的弱化(attenuation)。如本文所用,术语“中心前体”用于表示本文所示的任何代谢途径中的任何代谢物,其导致C6构件块的合成。术语“中心代谢物”在本文中用于表示在所有微生物中产生以支持生长的代谢物。
本文所述的宿主微生物可以包括能够被操作,使得可以产生6-羟基己酸或者一种或多种其它C6构件块的内源途径。在内源途径中,宿主微生物天然表达催化途径中的反应的所有酶。包含工程化途径的宿主微生物不天然表达催化途径中的反应的所有酶,但已经被工程化改造,从而在宿主中表达途径中所有的酶。
如本文中提及核酸(或蛋白质)和宿主使用的,术语“外源”指不像其在自然界中被发现一样存在于特定类型细胞中(并且不能从特定类型细胞获得)的核酸或由所述核酸编码的蛋白质。如此,非天然存在的核酸一旦在宿主中即视为对于宿主而言外源的。重要的是注意非天然存在的核酸可含有在自然界中发现的核酸序列的核酸亚序列或片段,只要该核酸作为整体不存在于自然界中。例如,表达载体内含有基因组DNA序列的核酸分子是非天然存在的核酸,如此一旦导入宿主中对于宿主细胞而言是外源的,因为该核酸分子作为整体(基因组DNA加载体DNA)不存在于自然界中。如此,作为整体不存在于自然界中的任何载体、自主复制的质粒或病毒(例如逆转录病毒、腺病毒、或疱疹病毒)视为非天然存在的核酸。由此得出结论通过PCR或限制内切性核酸酶处理产生的基因组DNA片段以及cDNA也视为非天然存在的核酸,因为它们作为未见于自然界的分开的分子存在。由此还得出结论任何以未见于自然界中的排布含有启动子序列和多肽编码序列(例如cDNA或基因组DNA)的任何核酸也是非天然存在的核酸。天然存在的核酸可以是对于特定宿主微生物而言外源的。例如,从酵母x的细胞分离的完整染色体一旦将该染色体导入酵母y的细胞中就酵母y细胞而言是外源核酸。
比较而言,如本文中提及核酸(例如基因)(或蛋白质)和宿主使用的,术语“内源的”指就像其在自然界中被发现一样的确存在于特定宿主中(并且可以从特定宿主获得)的核酸(或蛋白质)。此外,“内源表达”核酸(或蛋白质)的细胞就像其在自然界中被发现时相同特定类型的宿主那样表达所述核酸(或蛋白质)。此外,“内源生成”核酸、蛋白质、或其它化合物的宿主就像其在自然界中被发现时相同特定类型的宿主那样生成所述核酸、蛋白质、或化合物。
例如,根据宿主和宿主产生的化合物,除了β-酮硫解酶外,还可以在宿主中表达以下酶的一种或多种:3-羟基酰基CoA脱氢酶、3-酮酰基CoA还原酶、烯酰CoA水合酶、反式-2-烯酰CoA还原酶、硫酯酶、CoA转移酶、醛脱氢酶、单加氧酶、醇脱氢酶、6-氧代己酸脱氢酶、7-氧代庚酸脱氢酶、ω-转氨酶、6-羟基己酸脱氢酶、5-羟基戊酸脱氢酶、4-羟基丁酸脱氢酶、羧酸还原酶、脱酰基酶、N-乙酰基转移酶、ω-转氨酶,或酰胺水解酶。在表达羧酸还原酶的重组宿主中,也可以表达磷酸泛酰巯基乙胺基转移酶,因为它增强羧酸还原酶的活性。在表达单加氧酶的重组宿主中,也可以表达电子转移链蛋白,如氧化还原酶或铁氧还蛋白多肽。
例如,重组宿主可以包括外源β-酮硫解酶并生产可以被转化为6-羟基己酸的3-氧代-6-羟基己酰基CoA。
例如,重组宿主可以包括外源β-酮硫解酶和外源硫酯酶或CoA转移酶,以及以下外源酶的一种或多种:3-羟基酰基CoA脱氢酶或3-酮酰基CoA还原酶、烯酰CoA水合酶,和反式-2-烯酰CoA还原酶,并生产6-羟基己酸。例如,重组宿主可以包括外源β-酮硫解酶、外源硫酯酶或CoA转移酶、烯酰CoA水合酶、外源反式-2-烯酰CoA还原酶,和外源3-羟基酰基CoA脱氢酶或外源3-酮酰基CoA还原酶,并生产6-羟基己酸。
例如,生产6-羟基己酸的重组宿主可以包括以下外源酶的一种或多种:单加氧酶、醇脱氢酶、4-羟基丁酸脱氢酶、5-羟基戊酸脱氢酶、6-羟基己酸脱氢酶、7-氧代庚酸脱氢酶、5-氧代戊酸脱氢酶、6-氧代己酸脱氢酶,或醛脱氢酶,并进一步生产己二酸。例如生产6-羟基己酸的重组宿主可以包括外源单加氧酶并生产己二酸。例如,生产6-羟基己酸的重组宿主可以包括外源6-羟基己酸脱氢酶和醛脱氢酶并生产己二酸。例如,生产6-羟基己酸的重组宿主可以包括外源醇脱氢酶和以下外源酶之一:5-氧代戊酸脱氢酶、6-氧代己酸脱氢酶,或7-氧代庚酸脱氢酶,并生产己二酸。
例如,生产6-羟基己酸的重组宿主可以包括以下外源酶的一种或多种:醇脱氢酶、6-羟基己酸脱氢酶,或转氨酶,并进一步生产6-氨基己酸。例如,生产6-羟基己酸的重组宿主可以包括外源醇脱氢酶和外源转氨酶并生产6-氨基己酸。例如,生产6-羟基己酸的重组宿主可以包括外源6-羟基己酸脱氢酶和外源转氨酶并生产6-氨基己酸。任何此类宿主还可以包括外源酰胺水解酶并进一步生产己内酰胺。
例如,生产6-羟基己酸的重组宿主可以包括以下外源酶的一种或多种:羧酸还原酶、ω-转氨酶、脱酰基酶、N-乙酰基转移酶,或醇脱氢酶,并生产六亚甲基二胺。例如,生产6-羟基己酸的重组宿主可以包括外源羧酸还原酶、外源醇脱氢酶,以及一种或多种外源转氨酶(例如一种转氨酶或两种不同的转氨酶),并生产六亚甲基二胺。例如,生产6-羟基己酸的重组宿主可以包括外源羧酸还原酶和一种或多种外源转氨酶(例如一种转氨酶或两种不同的转氨酶),并生产六亚甲基二胺。例如,生产6-羟基己酸的重组宿主可以包括外源醇脱氢酶、外源羧酸还原酶,以及一种或多种外源转氨酶(例如一种转氨酶或两种不同的转氨酶),并生产六亚甲基二胺。例如,生产6-羟基己酸的重组宿主可以包括外源醇脱氢酶、外源N-乙酰基转移酶、羧酸还原酶、脱酰基酶,以及一种或多种外源转氨酶(例如一种转氨酶或两种不同的转氨酶),并生产六亚甲基二胺。
例如,生产6-羟基己酸的重组宿主可以包括一种或多种以下的外源酶:羧酸还原酶以及外源醇脱氢酶,并进一步生产1,6-己二醇。
在任何重组宿主中,重组宿主还可以包括一种或多种(例如,一种、两种、三种,或四种)用于将2-酮戊二酸转化为4-羟基丁酰基CoA的以下的外源酶:谷氨酸合酶;2-酮戊二酸脱羧酶;支链脱羧酶;谷氨酸脱羧酶;CoA连接酶;CoA-转移酶;ω-转氨酶;和醇脱氢酶。例如,重组宿主可以包括外源谷氨酸合酶,谷氨酸脱羧酶;CoA连接酶或CoA-转移酶;ω-转氨酶;和醇脱氢酶。例如,重组宿主可以包括外源2-酮戊二酸脱羧酶或支链脱羧酶;CoA连接酶;CoA-转移酶;和醇脱氢酶。
在工程化途径中,酶可以来自单一来源,即来自一个物种或属,或可来自多个来源,即不同的物种或属。已经从各种生物体鉴定了编码本文所述酶的核酸,并且可容易地在公众可获得的数据库,如GenBank或EMBL中获得。
如本文所用,提及特定的酶(例如β-酮硫解酶)意指具有特定酶活性的多肽(例如具有β-酮硫解酶活性的多肽)。
本文描述的可用于生产一种或多种C6构建块的任何酶可与相应的野生型酶的氨基酸序列具有至少70%序列同一性(同源性)(例如,至少75%、80%、85%、90%、91%、92%、93%、94%、95%、96%、97%、98%、99%或100%)。应当理解,可以基于成熟酶(例如,除去任何信号序列)或基于未成熟酶(例如,包括任何信号序列)确定序列同一性。还应当理解,起始甲硫氨酸残基可以存在于或可以不存在于本文所述的任何酶序列上。
例如,本文所述的具有β-酮硫解酶活性的多肽可以与钩虫贪铜菌β-酮硫解酶(参见Genbank登录号AAC38322.1,SEQ ID NO:1)、大肠杆菌β-酮硫解酶(参见Genbank登录号AAC74479.1,SEQ ID NO:13)或氨基丁酸羧菌(参见Genbank登录号No.CAB60036.2,SEQ IDNO:14)的氨基酸序列具有至少70%序列同一性(同源性)(例如,至少75%、80%、85%、90%、95%、97%、98%、99%或100%)。参见图6。
例如,本文所述的羧酸还原酶可以与海分枝杆菌(参见GenBank登录号ACC40567.1,SEQ ID NO:2)、耻垢分枝杆菌(参见GenBank登录号ABK71854.1,SEQ ID NO:3)、Segniliparus rugosus(参见GenBank登录号EFV11917.1,SEQ ID NO:4)、马赛分枝杆菌(参见GenBank登录号EIV11143.1,SEQ ID NO:5),或Segniliparus rotundus(参见GenBank登录号ADG98140.1,SEQ ID NO:6)羧酸还原酶的氨基酸序列具有至少70%序列同一性(同源性)(例如,至少75%、80%、85%、90%、95%、97%、98%、99%或100%)。参见图6。
例如,本文所述的ω-转氨酶可以与紫色色杆菌(参见GenBank登录号AAQ59697.1,SEQ ID NO:7)、铜绿假单胞菌(参见GenBank登录号AAG08191.1,SEQ ID NO:8)、丁香假单胞菌(参见GenBank登录号AAY39893.1,SEQ ID NO:9)、球形红杆菌(参见GenBank登录号ABA81135.1,SEQ ID NO:10)、大肠杆菌(参见GenBank登录号AAA57874.1,SEQ ID NO:11),或河流弧菌(参见GenBank登录号AEA39183.1,SEQ ID NO:12)ω-转氨酶的氨基酸序列具有至少70%序列同一性(同源性)(例如,至少75%、80%、85%、90%、95%、97%、98%、99%或100%)。这些ω-转氨酶中的一些是二胺ω-转氨酶。参见图6。
例如,本文所述的烯酰CoA还原酶可以与齿垢密螺旋体(参见GenBank登录号AAS11092.1,SEQ ID NO:15)或Euglena gracilis(参见GenBank登录号AAW66853.1,SEQ IDNO:16)的氨基酸序列具有至少70%序列同一性(同源性)(例如,至少75%、80%、85%、90%、95%、97%、98%、99%或100%)。参见图6。
例如,本文所述的脱羧酶可以与鼠伤寒沙门氏菌的氨基酸序列(参见GenbankAccession No.CAC48239.1,SEQ ID NO:17)具有至少70%序列同一性(同源性)(例如,至少75%、80%、85%、90%、95%、97%、98%、99%或100%)。参见图6。
可以如下测定两种氨基酸序列间的百分比同一性(同源性)。首先,使用来自含有BLASTP第2.0.14版的单机版BLASTZ的BLAST 2 Sequences(Bl2seq)程序比对氨基酸序列。此单机版BLASTZ可以获自Fish&Richardson的网站(例如www.fr.com/blast/)或美国政府国立生物技术信息中心网站(www.ncbi.nlm.nih.gov)。解释如何使用Bl2seq程序的用法说明可以参见伴随BLASTZ的自述文件。Bl2seq使用BLASTP算法实施两种氨基酸序列之间的比较。为了比较两种氨基酸序列,如下设置Bl2seq的选项:-i设置为含有要比较的第一氨基酸序列的文件(例如C:\seq1.txt);-j设置为含有要比较的第二氨基酸序列的文件(例如C:\seq2.txt);-p设置为blastp;-o设置为任何期望的文件名称(例如C:\output.txt);并且所有其它选项保持为其缺省设置。例如,可以使用以下命令来产生含有两种氨基酸序列间的比较的输出文件:C:\Bl2seq–i c:\seq1.txt–j c:\seq2.txt–p blastp–o c:\output.txt。如果两种比较序列共享同源性(同一性),那么指定的输出文件会呈现那些同源性区作为比对序列。如果两种比较序列不共享同源性(同一性),那么指定的输出文件不会呈现比对序列。可以对核酸序列遵循相似的规程,只是使用blastn。
一旦比对,通过计算相同氨基酸残基在这两种序列中呈现的位置的数目确定匹配数目。通过用匹配数目除以全长多肽氨基酸序列的长度,接着将所得的数值乘以100来确定百分比同一性(同源性)。注意到百分比同一性(同源性)值被四舍五入到最近的十分位。例如,78.11、78.12、78.13、和78.14被向下四舍五入到78.1,而78.15、78.16、78.17、78.18、和78.19被向上四舍五入到78.2。还注意到长度值会总是整数。
应当领会,许多核酸可以编码具有特定氨基酸序列的多肽。遗传密码的简并性是本领域中公知的;即对于许多氨基酸,存在有超过一种充当氨基酸密码子的核苷酸三联体。例如,可以修饰给定酶的编码序列中的密码子,从而获得特定物种(例如细菌或真菌)中的最佳表达,这使用适合于所述物种的密码子偏爱表进行。
也可以在本文件的方法中使用本文中描述的任何酶的功能性片段。如本文中使用的,术语“功能性片段”指与相应的成熟、全长、野生型蛋白质的活性具有至少25%(例如至少30%;40%;50%;60%;70%;75%;80%;85%;90%;95%;98%;99%;100%;或甚至大于100%)的蛋白质的肽片段。功能性片段一般但不总是可以由蛋白质的连续区构成,其中该区具有功能性活性。
此文件还提供了(i)本文件的方法中使用的酶的功能性变体和(ii)上文描述的功能性片段的功能性变体。相对于相应的野生型序列,酶和功能性片段的功能性变体可以含有添加、缺失、或取代。具有取代的酶一般会具有不超过50(例如不超过1、2、3、4、5、6、7、8、9、10、12、15、20、25、30、35、40、或50)处氨基酸取代(例如保守取代)。这适用于本文中描述的任何酶和功能性片段。保守取代是用一种氨基酸取代具有相似特征的另一种。保守取代包括下列组内的取代:缬氨酸、丙氨酸和甘氨酸;亮氨酸、缬氨酸、和异亮氨酸;天冬氨酸和谷氨酸;天冬酰胺和谷氨酰胺;丝氨酸、半胱氨酸、和苏氨酸;赖氨酸和精氨酸;和苯丙氨酸和酪氨酸。非极性疏水性氨基酸包括丙氨酸、亮氨酸、异亮氨酸、缬氨酸、脯氨酸、苯丙氨酸、色氨酸和甲硫氨酸。极性中性氨基酸包括甘氨酸、丝氨酸、苏氨酸、半胱氨酸、酪氨酸、天冬酰胺和谷氨酰胺。带正电荷的(碱性)氨基酸包括精氨酸、赖氨酸和组氨酸。带负电荷的(酸性)氨基酸包括天冬氨酸和谷氨酸。用上文提及的极性、碱性或酸性组的一种成员被相同组的另一种成员的任何取代可以视为保守取代。比较而言,非保守取代是用一种氨基酸取代具有不同特征的另一种。
缺失变体可以缺乏1、2、3、4、5、6、7、8、9、10、11、12、13、14、15、16、17、18、19、或20个氨基酸的区段(具有两个或更多个氨基酸)或非连续的单一氨基酸。添加(添加变体)包括融合蛋白,其含有:(a)本文中描述的任何酶或其片段;和(b)内部或末端(C或N)无关或外源氨基酸序列。在此类融合蛋白的背景中,术语“外源氨基酸序列”指与(a)不同的氨基酸序列。外源序列可以是例如用于纯化重组蛋白的序列(例如FLAG、多组氨酸(例如六组氨酸)、凝集素(HA)、谷胱甘肽-S-转移酶(GST)、或麦芽糖结合蛋白(MBP))。外源序列也可以是可用作可检测标志物的蛋白质,例如萤光素酶、绿色荧光蛋白(GFP)、或氯霉素乙酰基转移酶(CAT)。在一些实施方案中,融合蛋白含有来自另一种蛋白质的信号序列。在某些宿主细胞(例如酵母宿主细胞)中,可以经由使用外源信号序列提高靶蛋白的表达和/或分泌。在一些实施方案中,融合蛋白可以含有可用于例如引发免疫应答以生成抗体的载体(例如KLH)或ER或高尔基体保留信号。外源序列可以是不同长度的,并且在一些情况中可以是比与外源序列附接的全长靶蛋白质更长的序列。
工程化宿主可天然表达本文所述途径的酶的无一(none)或一些(例如,一种或多种、两种或多种、三种或多种、四种或多种、五种或多种,或六种或多种)。因此,工程化宿主内的途径可以包括所有外源酶,或者可以包括内源和外源酶两者。工程化宿主的内源基因也可以被破坏以防止不期望的代谢物的形成或防止通过作用于此类中间体的其他酶导致途径中的中间体的损失。工程化宿主可以称为重组宿主或重组宿主细胞。如本文所述,重组宿主可以包括编码如下的一种或多种的核酸:如本文所述的β-酮硫解酶、脱氢酶、合酶、脱羧酶、还原酶、水合酶、硫酯酶、单加氧酶、硫酯酶、酰胺水解酶,和转氨酶。
此外,可以使用本文所述的分离的酶,使用来自宿主微生物的裂解物(例如,细胞裂解物)作为酶的来源,或使用多种来自不同宿主微生物的裂解物作为酶的来源,体外进行C6构件块的生产。
本文中所述的途径的反应可以在一种或多种宿主菌株中进行,所述宿主菌株(a)天然表达一种或多种的相关酶,(b)经遗传工程化以表达一种或多种相关的酶,或(c)天然表达一种或多种相关的酶并经遗传工程化以表达一种或多种相关的酶。或者,可以从上述类型的宿主细胞中提取相关的酶,并以纯化或半纯化形式使用。此外,此类提取物包括可用作相关酶来源的裂解物(例如细胞裂解物)。在由本文件所提供的方法中,所有步骤可以在宿主细胞中进行,所有步骤可以使用提取的酶进行,或者一些步骤可以在细胞中进行,而其它步骤可以使用提取的酶进行。
产生6-羟基己酸的酶
如图1所示,可以从2-酮戊二酸通过中间体3-氧代-6-羟基己酰基CoA(其可以使用β-酮硫解酶从4-羟基丁酰基CoA生产)生物合成6-羟基己酸。可以使用以下的酶将3-氧代-6-羟基己酰基CoA转化为6-羟基己酸:3-羟基酰基CoA脱氢酶或3-酮酰基CoA脱氢酶、烯酰CoA水合酶、反式-2-烯酰CoA还原酶,和硫酯酶或CoA转移酶。
在一些实施方案中β-酮硫解酶可以被归类于EC 2.3.1.16下,如bktB的基因产物,或者可以被归类于EC 2.3.1.174下,如paaJ的基因产物。来自钩虫贪铜菌由bktB编码的β-酮硫解酶接受乙酰CoA和丙酰CoA作为底物,形成CoA活化的脂肪族骨架(参见例如Haywoodet al.,FEMS Microbiology Letters,1988,52:91-96;Slater et al.,J.Bacteriol.,1998,180(8):1979-1987)。来自大肠杆菌由paaJ编码的β-酮硫解酶接受琥珀酰CoA和乙酰CoA作为底物,形成CoA活化的骨架(Nogales et al.,Microbiology,2007,153,357-365)。参见,例如图6中的SEQ ID NO:1和SEQ ID NO:13。
在一些实施方案中,3-羟基酰基CoA脱氢酶或3-酮酰基CoA脱氢酶可以被归类于EC1.1.1.-下。例如,3-羟基酰基CoA脱氢酶可以被归类于EC 1.1.1.35下,如fadB的基因产物;归类于EC 1.1.1.157下,如hbd的基因产物(也可称为3-羟基丁酰基CoA脱氢酶);或归类于EC 1.1.1.36下,如phaB的乙酰乙酰基CoA还原酶基因产物(Liu&Chen,Appl.Microbiol.Biotechnol,2007,76(5):1153-1159;Shen et al,Appl.Environ.Microbiol,201 1,77(9):2905-2915;Budde et al,J.Bacteriol,2010,192(20):5319-5328)。
在一些实施方案中,3-酮酰基CoA还原酶可以被归类于EC 1.1.1.100下,如fabG的基因产物(Budde et al,J.Bacteriol,2010,192(20):5319-5328;Nomura et al,Appl.Environ.Microbiol,2005,71(8):4297-4306)。
在一些实施方案中,烯酰CoA水合酶可以被归类于EC 4.2.1.17下,如crt的基因产物,或归类于EC 4.2.1.1 19下,如phaJ的基因产物(Shen et al,2011,同上;Fukui et al,J.Bacteriol,1998,180(3):667-673)。
在一些实施方案中,反式-2-烯酰CoA还原酶可以被归类于EC 1.3.1.38或EC1.3.1.44下,如Egter的基因产物(Nishimaki et al,J.Biochem.,1984,95:1315-1321;Shen et al,2011,同上),或者tdter的基因产物(Bond-Watts et al,Biochemistry,2012,51:6827-6837),或者被归类于EC 1.3.1.8下(Inui et al,Eur.J.Biochem.,1984,142,121-126)。
在一些实施方案中,通过归类于EC 3.1.2.-下的硫酯酶,在6-羟基己酰基CoA中酶促形成导致合成6-羟基己酸的末端羧基,导致6-羟基己酸的产生。硫酯酶可以是YciA或Acot13的基因产物(Cantu et al,Protein Science,2010,19,1281-1295;Zhuang et al,Biochemistry,2008,47(9):2789-2796;Naggert et al.,J Biol.Chem.,1991,266(17):11044-1 1050)。
在一些实施方案中,通过CoA转移酶在6-羟基己酰基CoA中酶促形成导致合成6-羟基己酸的末端羧基,所述CoA转移酶例如归类于EC 2.8.3-下,如来自克鲁佛梭菌cat2的基因产物,来自氨基丁酸羧菌abfT的基因产物,或来自Clostridium viride的5-羟基戊酸CoA转移酶。
在己二酸的生物合成中产生末端羧基的酶
如描绘于图2中,可以使用醛脱氢酶、5-氧代戊酸脱氢酶、6-氧代己酸脱氢酶、7-氧代庚酸脱氢酶,或单加氧酶来酶促形成导致己二酸生产的末端羧基。
在一些实施方案中,可以通过归类于EC 1.2.1.3下的醛脱氢酶,在己二酸半醛中酶促形成导致己二酸合成的第二末端羧基(Guerrillot&Vandecasteele,Eur.J.Biochem.,1977,81,185-192)。参见图2。
在一些实施方案中,通过以下的酶,在己二酸半醛中酶促形成导致己二酸合成的第二末端羧基:EC 1.2.1.-如5-氧代戊酸脱氢酶(例如归类于EC 1.2.1.20下,如CpnE的基因产物),6-氧代己酸脱氢酶(例如归类于EC 1.2.1.63下,如来自不动杆菌属(Acinetobacter sp.)ChnE的基因产物),或7-氧代庚酸脱氢酶(如来自鞘氨醇单胞菌(Sphingomonas macrogolitabida)ThnG的基因产物)(Iwaki et al,Appl.Environ.Microbiol,1999,65(11),5158-5162;Lopez-Sanchez et al.,Αppl.Environ.Microbiol,2010,76(1),110-118))。参见图2。
在一些实施方案中,通过细胞色素P450家族中的单加氧酶(如CYP4F3B),在己二酸半醛中酶促形成导致己二酸合成的第二末端羧基(参见例如,Sanders et al,J.LipidResearch,2005,46(5):1001-1008;Sanders et al,The FASEB Journal,2008,22(6):2064-2071)。参见图2。
在六亚甲基二胺或6-氨基己酸的生物合成中产生末端胺基的酶
如描绘与图3和图4中,可以使用ω-转氨酶或脱酰基酶酶促形成末端胺基。
在一些实施方案中,通过ω-转氨酶,在己二酸半醛中酶促形成导致6-氨基己酸合成的末端胺基,所述ω-转氨酶例如归类于EC 2.6.1.-下,如EC 2.6.1.18,EC 2.6.1.19、EC2.6.1.29、EC 2.6.1.48,或EC 2.6.1.82下,诸如获得自紫色色杆菌(参见GenBank登录号AAQ59697.1,SEQ ID NO:7)、铜绿假单胞菌(参见GenBank登录号AAG08191.1,SEQ ID NO:8)、丁香假单胞菌(参见GenBank登录号AAY39893.1,SEQ ID NO:9)、球形红杆菌(参见GenBank登录号ABA81135.1,SEQ ID NO:10)、河流弧菌(参见GenBank登录号AEA39183.1,SEQ ID NO:12)、灰色链霉菌(Streptomyces griseus)或Clostridium viride。参见图3。
可被用于本文所述方法和宿主中的另外的ω-转氨酶来自大肠杆菌(参见GenBank登录号AAA57874.1,SEQ ID NO:11)。一些例如归类于EC 2.6.1.29或EC 2.6.1.82下的ω-转氨酶是二胺ω-转氨酶(例如SEQ ID NO:11)。
来自紫色色杆菌的可逆的ω-转氨酶(GenBank登录号AAQ59697.1,SEQ ID NO:13)已经证明接受6-氨基己酸作为氨基供体的类似的活性,从而在己二酸半醛中形成第一末端氨基(Kaulmann et al.,Enzyme and Microbial Technology,2007,41,628-637)。
来自灰色链霉菌的可逆的4-氨基丁酸:2-酮戊二酸转氨酶已经证明对于6-氨基己酸到己二酸半醛的转化的类似的活性(Yonaha et al.,Eur.J.Biochem.,1985,146,101-106)。
来自Clostridium viride的可逆的5-氨基戊酸转氨酶已经证明对于6-氨基己酸到己二酸半醛的转化的类似的活性(Barker et al,J.Biol.Chem.,1987,262(19),8994-9003)。
在一些实施方案中,通过二胺转氨酶,在6-氨基己醛中酶促形成导致六亚甲基二胺合成的第二末端胺基,所述二胺转氨酶例如归类于EC 2.6.1.29下或例如归类于EC2.6.1.82下,如来自大肠杆菌的YgjG的基因产物(GenBank登录号AAA57874.1,SEQ ID NO:12)。还可以使用SEQ ID NOs:7-10和11中所列的转氨酶来生产六亚甲基二胺。参见图4。
ygjG的基因产物接受宽范围的二胺碳链长度底物,如腐胺,尸胺和亚精胺(Samsonova et al,BMC Microbiology,2003,3:2)。
来自大肠杆菌菌株B的二胺ω-转氨酶已经证明针对1,7二氨基庚烷的活性(Kim,The Journal of Chemistry,1964,239(3),783-786)。
在一些实施方案中,通过脱酰基酶,在N6-乙酰基-1,6-二氨基己烷中酶促形成导致六亚甲基二胺合成的第二末端胺基,所述脱酰基酶例如归类于EC 3.5.1.17下,如酰基赖氨酸脱羧酶。
在1,6己二醇的生物合成中产生末端羟基的酶
如描绘于图5,可以使用醇脱氢酶来酶促形成末端羟基。例如,通过醇脱氢酶,在6-羟基己烷中酶促形成导致1,6己二醇合成的末端羟基,所述醇脱氢酶归类于EC 1.1.1.-(例如EC 1.1.1.1、1.1.1.2、1.1.1.21,或1.1.1.184)下,如YMR318C或YqhD的基因产物(Liu etal,Microbiology,2009,155,2078-2085;Larroy et ah,2002,Biochem J.,361(Pt 1),163-172;Jarboe,2011,Appl.Microbiol.Biotechnol,89(2),249-257)或者具有GenBank序列号CAA81612.1的蛋白质。
生物化学途径
导致6-羟基己酸的途径
在一些实施方案中,如下从中心代谢物2-酮戊二酸合成6-羟基己酸:通过谷氨酸合酶(例如归类于EC 1.4.1.13下)或者α-氨基转移酶(例如归类于EC 2.6.1.-,如EC2.6.1.39下)将2-酮戊二酸转化为L-谷氨酸;然后通过谷氨酸脱羧酶(例如归类于EC4.1.1.15或EC 4.1.1.18下)将L-谷氨酸转化为4-氨基丁酸;然后通过ω-转氨酶(例如归类于EC 2.6.1.18,EC 2.6.1.19,EC 2.6.1.48,或EC 2.6.1.96下),如来自大肠杆菌gabT的基因产物,将4-氨基丁酸转化为琥珀酸半醛(Bartsch et al,J.Bacteriol,1990,172(12),7035);然后通过醇脱氢酶(例如归类于EC 1.1.1.61下),如gbd(例如来自纤维素堆囊菌(Sorangium cellulosu))、gabD(Bartsch et al,J.Bacteriol,1990,172(12),7035)或者YihU(Saito et al,J.Biol.Chem.,2009,284(24),16442-16452)的基因产物,或者通过5-羟基戊酸脱氢酶(如cpnD的基因产物(例如参见,Iwaki et al,2002,Appl.Environ.Microbiol,68(11):5671-5684))将琥珀酸半醛转化为4-羟基丁酸;然后通过使用CoA连接酶(例如归类于EC 6.2.1-(例如EC 6.2.1.40))或CoA转移酶(例如归类于EC2.8.3-)如来自克鲁佛梭菌cat2的基因产物、来自氨基丁酸羧菌abfT的基因产物或者来自Clostridium viride 5-羟基戊酸CoA转移酶,将4-羟基丁酸转化为4-羟基丁酰基CoA;然后通过使用β-酮硫解酶(例如归类于EC 2.3.1.16或EC 2.3.1.174下)如bktB或paaJ的基因产物(例如SEQ ID NO:1或13),或者由CAB60036.2编码的β-酮硫解酶活性(例如SEQ ID NO:14)将4-羟基丁酰基CoA转化为3-氧代-6-羟基己酰基CoA;然后使用3-羟基酰基CoA脱氢酶(例如归类于EC 1.1.1.-下)如EC 1.1.1.35(例如fadB的基因产物),EC 1.1.1.36(例如phaB的基因产物),或EC 1.1.1.157(例如hbd的基因产物),或者通过3-酮酰基CoA还原酶(例如归类于EC 1.1.1.100下)如fabG的基因产物,转化为3-羟基-6-羟基己酰基CoA;然后使用烯酰CoA水合酶(例如归类于EC 4.2.1.17下如crt的基因产物,或者归类于EC4.2.1.119下,如phaJ的基因产物)将3-羟基-6-羟基己酰基CoA转化为2,3-脱氢-6-羟基己酰基CoA;然后通过反式-2-烯酰CoA还原酶(例如归类于EC 1.3.1.38、EC 1.3.1.44,或EC1.3.1.8下)如Egter或tdter的基因产物,将2,3-脱氢-6-羟基己酰基CoA转化为6-羟基己酰基CoA;然后通过硫酯酶(例如归类于EC 3.1.2.-下)如YciA或Acot13的基因产物,或者CoA转移酶(例如归类于EC 2.8.3.-下)将6-羟基己酰基CoA转化为6-羟基己酸。参见图1。
在一些实施方案中,如下将2-酮戊二酸转化为琥珀酸半醛:使用羧基裂解酶(例如归类于EC.4.1.1.-下)像是2-酮戊二酸脱羧酶(例如归类于EC 4.1.1.71下)或支链脱羧酶(例如归类于EC 4.1.1.72下)如kdcA或kivD的基因产物,或者吲哚丙酮酸脱羧酶(例如归类于EC 4.1.1.74下)或者苯基丙酮酸脱羧酶(例如归类于EC 4.1.1.43下)。以这种方式生产的琥珀酸半醛可以如上所述转化为6-羟基己酸。参见图1。
使用6-羟基己酸作为中心前体至己二酸的途径
在一些实施方案中,如下从6-羟基己酸合成己二酸:通过醇脱氢酶(例如归类于EC1.1.1.-下)如YMR318C的基因产物(例如归类于EC 1.1.1.2下,参见Genbank登录号CAA90836.1)(Larroy et al,2002,Biochem J.,361(Pt 1),163-172),cpnD的基因产物(Iwaki et al,2002,Appl.Environ.Microbiol,68(11):5671-5684)或gabD的基因产物(Lutke-Eversloh&Steinbüchel,1999,F EMS Microbiology Letters,181(1):63-71),或者通过6-羟基己酸脱氢酶(例如归类于EC 1.1.1.258下)如ChnD的基因产物(Iwaki et al,ΑρρΙ.Environ.Microbiol.,1999,65(1 1):5158-5162)将6-羟基己酸转化为己二酸半醛;然后通过脱氢酶(例如归类于EC 1.2.1.-下)如7-氧代庚酸脱氢酶(例如,ThnG的基因产物)、6-氧代己酸脱氢酶(例如,ChnE的基因产物),通过谷氨酸半醛脱氢酶(例如归类于EC1.2.1.20下),通过5-氧代戊酸脱氢酶(如CpnE的基因产物),或醛脱氢酶(归类于EC1.2.1.3下),将己二酸半醛转化为己二酸。参见图2。由YMR318C编码的醇脱氢酶具有广泛的底物特异性,包括C6醇的氧化。
在一些实施方案中,如下从中心前体6-羟基己酸合成己二酸:通过细胞色素P450将6-羟基己酸转化为己二酸半醛(Sanders et al,J.Lipid Research,2005,46(5),1001-1008;Sanders et al,The FASEB Journal,2008,22(6),2064-2071);然后通过细胞色素P450家族中的单加氧酶(如CYP4F3B)将己二酸半醛转化为己二酸。参见图2。
使用6-羟基己酸作为中心前体至6-氨基己酸和ε-己内酰胺的途径
在一些实施方案中,如下从中心前体6-羟基己酸合成6-氨基己酸:通过醇脱氢酶(例如归类于EC 1.1.1.2下)如YMR318C的基因产物,6-羟基己酸脱氢酶(例如归类于EC1.1.1.258下),5-羟基戊酸脱氢酶(例如归类于EC 1.1.1.-下)如cpnD的基因产物,或4-羟基丁酸脱氢酶(例如归类于EC 1.1.1.-)如gabD的基因产物,将6-羟基己酸转化为己二酸半醛;然后通过ω-转氨酶(EC 2.6.1.18、EC 2.6.1.19、EC 2.6.1.29、EC 2.6.1.48,或EC2.6.1.82如SEQ ID NOs:7-10或12中的一个,见上)将己二酸半醛转化为6-氨基己酸。参见图3。
在一些实施方案中,如下从中心前体6-羟基己酸合成ε-己内酰胺:通过醇脱氢酶(例如归类于EC 1.1.1.2下)如YMR318C的基因产物,6-羟基己酸脱氢酶(例如归类于EC1.1.1.258下),5-羟基戊酸脱氢酶(例如归类于EC 1.1.1.-)如cpnD的基因产物,或者4-羟基丁酸脱氢酶(例如归类于EC 1.1.1.-)如gabD的基因产物,将6-羟基己酸转化为己二酸半醛;然后通过ω-转氨酶(EC 2.6.1.18、EC 2.6.1.19、EC 2.6.1.29、EC 2.6.1.48,或EC2.6.1.82)将己二酸半醛转化为6-氨基己酸;然后通过酰胺水解酶(EC 3.5.2.-)将6-氨基己酸转化为ε-己内酰胺。参见图3。
在一些实施方案中,通过上述最后一步(即通过使用酰胺水解酶如EC.3.5.2.-中的一个酶转化)从中心前体6-氨基己酸合成ε-己内酰胺。参见图3。
使用6-氨基己酸、6-羟基己酸、己二酸半醛,或1,6-己二醇作为中心前体至六亚甲基二胺的途径
在一些实施方案中,如下从中心前体6-氨基己酸合成六亚甲基二胺:通过羧酸还原酶(例如归类于EC 1.2.99.6下)如car的基因产物与磷酸泛酰巯基乙胺转移酶增强剂(enhancer)(例如由来自枯草芽孢杆菌的sfp基因编码或来自诺卡氏菌的npt基因编码)或来自灰色链霉菌的GriC和GriD的基因产物(Suzuki et al.,J.Antibiot.,2007,60(6),380-387)组合,将6-氨基己酸转化为6-氨基己醛;然后通过ω-转氨酶(例如归类于EC2.6.1.-下(如EC 2.6.1.18、EC 2.6.1.19、EC 2.6.1.29、EC 2.6.1.48,或EC 2.6.1.82,如SEQ ID NOs:7-12))将6-氨基己醛转化为六亚甲基二胺。例如,所述羧酸还原酶可以获得自海分枝杆菌(Genbank Accession No.ACC40567.1,SEQ ID NO:2)、耻垢分枝杆菌(Genbank登录号ABK71854.1,SEQ ID NO:3)、Segniliparus rugosus(Genbank登录号EFV11917.1,SEQ ID NO:4)、马赛分枝杆菌(Genbank登录号EIV11143.1,SEQ ID NO:5),或者Segniliparus rugosus(Genbank登录号ADG98140.1,SEQ ID NO:6)。参见图4。
由car的基因产物编码的羧酸还原酶和磷酸泛酰巯基乙胺转移酶增强剂npt或sfp具有广泛的底物特异性,其包括末端双官能的C4和C5羧酸(Venkitasubramanian et al.,Enzyme and Microbial Technology,2008,42,130-137)。
在一些实施方案中,如下从中心前体6-羟基己酸(其可以如图1中描述的产生)合成六亚甲基二胺:通过羧酸还原酶(例如归类于EC 1.2.99.6下)如car的基因产物(见上)与磷酸泛酰巯基乙胺转移酶增强剂(例如由来自枯草芽孢杆菌的sfp基因编码或来自诺卡氏菌的npt基因编码)或GriC和GriD的基因产物(Suzuki et al,2001,见上)组合,将6-羟基己酸转化为6-羟基己醛;然后通过ω-转氨酶(例如归类于EC 2.6.1.18、EC 2.6.1.19、EC2.6.1.29、EC 2.6.1.48,或EC 2.6.1.82下)如SEQ ID NOs:7-12(见上),将6-氨基己醛转化为6-氨基己醇;然后通过醇脱氢酶或者具有GenBank登录号CAA81612.1的蛋白质转化为7-氨基己醛,所述醇脱氢酶例如归类于EC 1.1.1.-(如EC 1.1.1.1,EC 1.1.1.2,EC1.1.1.21,或EC 1.1.1.184)下,如YMR318C或YqhD的基因产物(Liu et al,Microbiology,2009,155,2078-2085;Larroy et al,2002,Biochem J.,361(Pt 1),163-172;Jarboe,2011,Appl.Microbiol.Biotechnol,89(2),249-257);然后通过ω-转氨酶转化为六亚甲基二胺,所述ω-转氨酶例如归类于EC 2.6.1.18、EC 2.6.1.19、EC 2.6.1.29、EC 2.6.1.48,或EC 2.6.1.82下,如SEQ ID NOs:7-12,见上。参见图4。
在一些实施方案中,如下从中心前体6-氨基己酸合成六亚甲基二胺:通过N-乙酰基转移酶(如例如归类于EC 2.3.1.32下的赖氨酸N-乙酰基转移酶)将6-氨基己酸转化为N6-乙酰基-6-氨基己酸;然后通过羧酸还原酶(例如归类于EC 1.2.99.6下)如car的基因产物(见上,例如SEQ ID NO:4、5,或6)与磷酸泛酰巯基乙胺转移酶增强剂(例如由来自枯草芽孢杆菌的sfp基因编码或来自诺卡氏菌的npt基因编码)或GriC和GriD的基因产物组合,转化为N6-乙酰基-6-氨基己醛;然后通过ω-转氨酶转化为为N6-乙酰基-1,6-氨基己烷,所述ω-转氨酶例如归类于EC 2.6.1.18、EC 2.6.1.19、EC 2.6.1.29、EC 2.6.1.48,或EC2.6.1.82下,如SEQ ID NOs:7-12,见上;然后通过酰基赖氨酸脱酰基,酶(例如归类于EC3.5.1.17下)转化为六亚甲基二胺。参见图4。
在一些实施方案中,如下从中心前体己二酸半醛合成六亚甲基二胺:通过羧酸还原酶(例如归类于EC 1.2.99.6下)如car的基因产物(见上,例如SEQ ID NO:6)与磷酸泛酰巯基乙胺转移酶增强剂(例如由来自枯草芽孢杆菌的sfp基因编码或来自诺卡氏菌的npt基因编码)或GriC和GriD的基因产物组合,将己二酸半醛转化为己二醛;然后通过ω-转氨酶转化为6-氨基己醛,所述ω-转氨酶例如归类于EC 2.6.1.18、EC 2.6.1.19、EC 2.6.1.29、EC 2.6.1.48,或EC 2.6.1.82下;然后通过ω-转氨酶转化为六亚甲基二胺,所述ω-转氨酶例如归类于EC 2.6.1.18、EC 2.6.1.19、EC 2.6.1.29、EC 2.6.1.48,或EC 2.6.1.82下,如SEQ ID NOs:7-12。参见图4。
在一些实施方案中,如下从1,6-己二醇合成六亚甲基二胺:使用醇脱氢酶将1,6-己二酮转化为6-羟基己烷,所述醇脱氢酶例如归类于EC 1.1.1.-(例如EC 1.1.1.1、EC1.1.1.2、EC 1.1.1.21,或EC 1.1.1.184)下,如YMR318C或YqhD的基因产物或者具有GenBank登录号CAA81612.1的蛋白质;然后通过ω-转氨酶转化为6-氨基己醇,所述ω-转氨酶例如归类于EC 2.6.1.18、EC 2.6.1.19、EC 2.6.1.29、EC 2.6.1.48,或EC 2.6.1.82下,如SEQ ID NOs:7-12;然后通过醇脱氢酶转化为6-氨基己醛,所述醇脱氢酶例如归类于EC1.1.1.-(例如EC 1.1.1.1、EC 1.1.1.2、EC 1.1.1.21,或EC 1.1.1.184)下,如YMR318C或YqhD的基因产物或者具有GenBank登录号CAA81612.1的蛋白质;然后通过ω-转氨酶转化为六亚甲基二胺,所述ω-转氨酶例如归类于EC 2.6.1.18、EC 2.6.1.19、EC 2.6.1.29、EC2.6.1.48,或EC 2.6.1.82下,如SEQ ID NOs:7-12。参见图4。
使用6-羟基己酸作为中心前体至1,6-己二醇的途径
在一些实施方案中,如下从中心前体6-羟基己酸合成1,6己二醇:通过羧酸还原酶(例如归类于EC 1.2.99.6下)如car的基因产物(见上,例如SEQ ID NO:2,3,4,5,或6)与磷酸泛酰巯基乙胺转移酶增强剂(例如由来自枯草芽孢杆菌的sfp基因编码或来自诺卡氏菌的npt基因编码)或来自灰色链霉菌的GriC和GriD的基因产物组合(Suzuki et ah,J.Antibiot,2007,60(6),380-387),将6-羟基己酸转化为6-羟基己醛;然后通过醇脱氢酶将6-羟基己醛转化为1,6-己二醇,所述醇脱氢酶例如归类于EC 1.1.1.-(例如EC 1.1.1.1、EC 1.1.1.2、EC 1.1.1.21,或EC 1.1.1.184)下,如YMR318C或YqhD的基因产物(来自大肠杆菌,GenBank登录号AAA69178.1)(参见例如Liu et ah,Microbiology,2009,155,2078-2085;Larroy et al,2002,Biochem J.,361(Pt 1),163-172;或者Jarboe,2011,Appl.Microbiol.Biotechnol.,89(2),249-257)或者具有GenBank登录号CAA81612.1(来自嗜热脂肪地芽孢杆菌(Geobacillus stearothermophilus))的蛋白质。参见图5。
培养策略
在一些实施方案中,在重组宿主中使用厌氧、需氧或微需氧培养条件生物合成一种或多种C6构建块。在一些实施方案中,培养策略需要营养限制,如氮、磷酸盐或氧限制。
在一些实施方案中,可以采用使用例如陶瓷膜的细胞保留策略来实现并维持补料分批或连续发酵期间的高细胞密度。
在一些实施方案中,在一种或多种C6构件块的合成中对发酵补料的主要碳源可以源自生物或非生物原料。
在一些实施方案中,生物原料可以是或可以源自单糖,二糖,木质纤维素,半纤维素,纤维素,木质素,乙酰丙酸和甲酸,甘油三酯,甘油,脂肪酸,农业废物,浓缩的酒糟可溶物(condensed distillers'solubles),或城市废物。
已经在几种微生物(诸如大肠杆菌、钩虫贪铜菌、食油假单胞菌、恶臭假单胞菌和解脂耶罗维亚酵母)中证明了源自生物柴油产生的粗制甘油的有效分解代谢(Lee et al,Appl.Biochem.Biotechnol.,2012,166:1801-1813;Yang et al,Biotechnology forBiofuels,2012,5:13;Meijnen et al,Appl.Microbiol.Biotechnol,2011,90:885-893)。
已经在几种生物体(诸如钩虫贪铜菌和恶臭假单胞菌)中在经由前体丙酰基-CoA合成3-羟基戊酸中证明了木质纤维素衍生的乙酰丙酸的有效分解代谢(Jaremko and Yu,2011,同上;Martin and Prather,J.Biotechnol,2009,139:61-67)。
已经在几种微生物(诸如恶臭假单胞菌、钩虫贪铜菌)中证明了木质素衍生的芳香族化合物诸如苯甲酸类似物的有效分解代谢(Bugg et al.,Current Opinion inBiotechnology,2011,22,394-400;Pérez-Pantoja et al,FEMS Microbiol.Rev.,2008,32,736-794)。
已经在几种微生物(包括解脂耶罗维亚酵母)中证明了农业废物(诸如橄榄磨坊废水)的有效利用(Papanikolaou et al,Bioresour.Technol,2008,99(7):2419-2428)。
已经对几种微生物(诸如大肠杆菌、谷氨酸棒状杆菌和德氏乳杆菌和乳酸乳球菌)证明了可发酵糖类(诸如源自纤维素、半纤维素、甘蔗和甜菜糖蜜、木薯、玉米和其它农业来源的单糖和二糖)的有效利用(参见例如Hermann et al,J.Biotechnol,2003,104:155-172;Wee et al,Food Technol.Biotechnol,2006,44(2):163-172;Ohashi et al,J.Bioscience and Bioengineering,1999,87(5):647-654)。
已经针对钩虫贪铜菌证明了源自多种农业木质纤维素来源的糠醛的有效利用(Liet al,Biodegradation,2011,22:1215-1225)。
在一些实施方案中,非生物原料可以是或者可以源自天然气,合成气,CO2/H2,甲醇,乙醇,苯甲酸酯,非挥发性残留物(NVR),或来自环己烷氧化过程的碱洗液(causticwash)废物流,或对苯二甲酸/间苯二甲酸混合物废物流。
已经对甲基营养型酵母巴斯德毕赤酵母证明了甲醇的有效分解代谢。
已经对克鲁佛梭菌证明了乙醇的有效分解代谢(Seedorf et al,Proc.NatlAcad.Sci.USA,2008,105(6)2128-2133)。
已经对钩虫贪铜菌证明了CO2和H2(其可以源自天然气和其它化学和石油化学来源)的有效分解代谢(Prybylski et al,Energy,Sustainability and Society,2012,2:11)。
已经对多种微生物(诸如杨氏梭菌和自产乙醇梭菌)证明了合成气的有效分解代谢( et al,Applied and Environmental Microbiology,2011,77(15):5467-5475)。
已经对多种微生物(诸如食酸代尔夫特菌和钩虫贪铜菌)证明了来自环己烷过程的非挥发性残留物废物流的有效分解代谢(Ramsay et al,Applied and EnvironmentalMicrobiology,1986,52(1):152-156)。
在一些实施方案中,宿主微生物可以是原核生物。例如,原核生物可以是来自以下的细菌:埃希氏菌属如大肠杆菌;梭菌属如杨氏梭菌、自产乙醇梭菌或者克鲁佛梭菌;棒状杆菌属如谷氨酸棒状杆菌;贪铜菌属如钩虫贪铜菌或者耐金属贪铜菌;假单胞菌属如荧光假单胞菌、恶臭假单胞菌或者食油假单胞菌;代尔夫特菌属如食酸代尔夫特菌;芽孢杆菌属如枯草芽胞杆菌;乳杆菌属如德氏乳杆菌;或者乳球菌属如乳酸乳球菌。此类原核生物也可以是构建能够生成一种或多种C6构件块的本文中描述的重组宿主细胞的基因来源。
在一些实施方案中,宿主微生物可以是真核生物。例如,真核生物可以是丝状真菌,例如来自曲霉属如黑曲霉的。另外,真核生物可以是酵母,例如来自酵母属如酿酒酵母;来自毕赤氏酵属如巴斯德毕赤酵母;来自耶罗维亚酵母属如解脂耶罗维亚酵母;来自伊萨酵母属如东方伊萨酵母;来自德巴利酵母属如汉逊德巴利酵母;来自Arxula属如Arxulaadenoinivorans;或者来自克鲁维酵母菌属如乳酸克鲁维酵母菌的酵母。此类真核生物也可以是构建能够生成一种或多种C6构件块的本文中描述的重组宿主细胞的基因来源。
代谢工程
本文件提供方法,所述方法牵涉对所有上述途径描述的少于所有的步骤。此类方法可牵涉例如此类步骤中的1,2,3,4,5,6,7,8,9,10,11,12或者更多个。在此类方法包含少于所有步骤的情况下,第一个步骤(且仅在一些实施方案中)可为所列步骤中的任一个。
此外,本文所述的重组宿主可以包括以上酶的任何组合,使得可以在重组宿主中进行一个或多个步骤,例如此类步骤中的1,2,3,4,5,6,7,8,9,10或者更多个。本文件提供了列出的任何属和种的宿主细胞,并遗传工程化以表达一种或多种(例如,2,3,4,5,6,7,8,9,10,11,12或者更多种)本文件所述的任何酶的重组形式。因此,例如,宿主细胞可以含有编码催化本文所述的任意途径的一个或多个步骤的酶的核酸。
另外,本文件认识到,在酶已经被描述为接受CoA活化的底物的情况下,存在与[acp]结合底物相关的相似的酶活性,其不一定为相同的酶种类。
此外,本文件认识到,在酶已经被描述为接受底物的(R)-对映异构体的情况下,存在与底物的(S)-对映异构体相关的相似的酶活性,其不一定为相同的酶种类。
本文件还认识到,在已经显示酶接受特定辅因子如NADPH或者共底物如乙酰CoA的情况下,许多酶在催化特定酶活性中在接受大量不同辅因子或者共底物方面是泛宿主性的(promiscuous)。此外,本文件认识到,在酶对例如特定辅因子如NADH具有高特异性的情况下,对辅助因子NADPH具有高特异性的具有相似或者相同活性的酶可为不同的酶种类。
在一些实施方案中,概述于本文的途径中的酶是经由非直接或者合理酶设计方法的酶工程的结果,目的在于改善活性、改善特异性、降低反馈抑制、降低阻抑、改善酶溶解度、改变立体特异性,或者改变辅因子特异性。
在一些实施方案中,将概述于本文的途径中的酶经由附加型或者染色体整合方法基因投入(gene dose)(即,通过在宿主生物中具有多个拷贝的基因的过表达)至所得的经遗传修饰的生物体中。
在一些实施方案中,可以使用基因组级别(genome-scale)系统生物学技术如通量平衡分析(Flux Balance Analysis)来设计用于将碳流量引导至C6构件块的基因组级别的弱化或者敲除策略。
弱化策略包括但不限于使用转座子,同源重组(双交叉方法),诱变,酶抑制剂和RNAi干扰。
在一些实施方案中,可以利用通量组(fluxomic)、代谢物组(metabolomic)和转录物组(transcriptomal)数据来告知或者支持基因组级别的系统生物学技术,由此在将碳流量导向C6构件块中设计基因组级别的弱化或者敲除策略。
在一些实施方案中,可以通过在选择性环境中连续培养,改善宿主微生物对高浓度C6构件块的耐受性。
在一些实施方案中,弱化或增强宿主微生物的生物化学网络以(1)确保乙酰CoA和4-羟基丁酰基CoA的细胞内利用度,(2)创建NADH或NADPH不平衡,其仅可通过形成C6构件块来平衡,(3)防止导致并包括C6构件块的中心代谢物、中心前体的降解和(4)确保从细胞有效的流出。
在需要用于C6构建块合成的乙酰CoA细胞内利用度的一些实施方案中,可以在宿主生物体中弱化催化乙酰CoA水解的内源性酶,如短链长度的硫酯酶。
在需要用于C6构建块合成的乙酰CoA细胞内利用度的一些实施方案中,可以弱化产生乙酸的内源磷酸转乙酰化酶,如pta(Shen et al,Αppl.Environ.Microbiol,2011,77(9):2905-2915)。
在需要用于C6构建块合成的乙酰CoA细胞内利用度的一些实施方案中,可以弱化乙酸合成途径中编码乙酸激酶的内源基因,如ack。
在需要用于C6构建块合成的乙酰CoA和NADH细胞内利用度的一些实施方案中,可以弱化编码催化丙酮酸降解为乳酸的酶(如由ldhA编码的乳酸脱氢酶)的内源基因(Shenet al.,2011,同上)。
在一些实施方案中,可以在宿主中过表达催化添补反应(anapleroticreactions)的酶,如PEP羧化酶和/或丙酮酸羧化酶。
在需要用于C6构建块合成的乙酰CoA和NADH细胞内利用度的一些实施方案中,可以弱化例如编码催化磷酸烯醇式丙酮酸降解至琥珀酸的酶(如menaquinol-富马酸氧化还原酶)的内源基因,如frdBC(参见例如Shen et al.,2011,同上)。
在需要用于C6构建块合成的乙酰CoA和NADH细胞内利用度的一些实施方案中,可以弱化编码催化乙酰CoA降解至乙醇的酶(如由adhE编码的醇脱氢酶)的内源基因(Shen etal.,2011,同上)。
在一些实施方案中,其中途径需要过量的NADH辅因子用于C6构件块合成,可以在宿主生物体中过表达重组甲酸脱氢酶基因(Shen et al.,2011,同上)。
在一些实施方案中,其中途径需要过量的NADH辅因子用于C6构件块合成,可以弱化消耗NADH的重组转氢酶。
在一些实施方案中,可以弱化编码催化丙酮酸降解至乙醇的酶(如丙酮酸脱羧酶)的内源基因。
在需要用于C6构建块合成的乙酰CoA细胞内利用度的一些实施方案中,可以在微生物中过表达重组乙酰CoA合成酶如acs的基因产物(Satoh et al,J.Bioscience andBioengineering,2003,95(4):335-341)。
在一些实施方案中,可以通过弱化内源葡萄糖-6-磷酸异构酶(EC 5.3.1.9)将碳流引导入戊糖磷酸循环来增加NADPH的供应。
在一些实施方案中,可以通过过表达6-磷酸葡糖酸脱氢酶和/或转酮醇酶将碳流重新引导入戊糖磷酸循环来增加NADPH的供应(Lee et al.,2003,BiotechnologyProgress,19(5),1444-1449)。
在一些实施方案中,其中途径在C6构件块的合成中需要过量的NADPH辅因子,可以在宿主生物体中过表达编码吡啶(puridine)核苷酸转氢酶的基因,如UdhA(Brigham etal.,Advanced Biofuels and Bioproducts,2012,Chapter39,1065-1090)。
在一些实施方案中,其中途径在C6构件块的合成中需要过量的NADPH辅因子,可以在宿主生物体中过表达重组甘油醛-3-磷酸脱氢酶基因如GapN(Brigham et al,2012,同上)。
在一些实施方案中,其中途径在C6构件块的合成中需要过量的NADPH辅因子,可以在宿主生物体中过表达重组苹果酸酶基因如maeA或maeB(Brigham et al,2012,同上)。
在一些实施方案中,其中途径在C6构件块的合成中需要过量的NADPH辅因子,可以在宿主生物体中过表达重组葡萄糖-6-磷酸脱氢酶基因如zwf(Lim et al.,J.Bioscienceand Bioengineering,2002,93(6),543-549)。
在一些实施方案中,其中途径在C6构件块的合成中需要过量的NADPH辅因子,可以在宿主生物体中过表达重组果糖1,6二磷酸酶基因如fbp(Becker et al.,J.Biotechnol,2007,132:99-109)。
在一些实施方案中,其中途径在C6构件块的合成中需要过量的NADPH辅因子,可以弱化内源性丙糖磷酸异构酶(EC 5.3.1.1)。
在一些实施方案中,其中途径在C7构件块的合成中需要过量的NADPH辅因子,可以在宿主生物体中过表达重组葡萄糖脱氢酶如gdh的基因产物(Satoh et al,J.Bioscienceand Bioengineering,2003,95(4):335-341)。
在一些实施方案中,可以弱化促进将NADPH转化为NADH的内源性酶,如可经由EC1.4.1.2(NADH-特异的)和EC 1.4.1.4(NADPH-特异的)下分类的谷氨酸脱氢酶的相互转换产生的NADH产生循环。
在一些实施方案中,可以弱化利用NADH和NADPH两者作为辅因子的内源谷氨酸脱氢酶(EC 1.4.1.3)。
在一些实施方案中,可以通过仅表达胞质域而不是锚定P450到内质网的N端区域溶解膜结合的细胞色素P450如CYP4F3B(Scheller et al,J.Biol.Chem.,1994,269(17):12779-12783)。
在一些实施方案中,可以通过表达作为与小的可溶性蛋白(例如麦芽糖结合蛋白)的融合蛋白来溶解烯酰CoA还原酶(Gloerich et al,FEBS Letters,2006,580,2092-2096)。
在使用天然累积聚羟基链烷酸的宿主的一些实施方案中,可以在宿主菌株中弱化内源聚合物合酶。
在一些实施方案中,可以在宿主中过表达L-丙氨酸脱氢酶以从丙酮酸再生L-丙氨酸作为氨基供体用于ω-转氨酶反应。
在一些实施方案中,可以在宿主中过表达L-谷氨酸脱氢酶、L-谷氨酰胺合成酶,或谷氨酸合成酶以从2-酮戊二酸再生L-谷氨酸作为氨基供体用于ω-转氨酶反应。
在一些实施方案中,可以弱化酶如分类于EC 1.3.1.62下的庚二酰CoA脱氢酶;例如归类于EC 1.3.8.7、EC 1.3.8.1,或EC 1.3.99.-下的酰基CoA脱氢酶;和/或归类于例如EC 1.3.8.6下的丁酰CoA脱氢酶,其降解导致并包括C6构件块的中心代谢物和中心前体。
在一些实施方案中,可以弱化经由辅酶A酯化活化C6构件块的内源性酶,诸如例如归类于EC 6.2.1.14下的CoA连接酶(例如己二酰CoA合成酶)。
在一些实施方案中,可以通过对细胞膜的基因工程结构修饰或增加任何与C6构件块相关的转运蛋白活性来增强或放大跨越细胞膜至细胞外培养基的C6构件块流出。
可以通过过表达宽底物范围多药物转运蛋白,诸如来自枯草芽孢杆菌的Blt(Woolridge et al,1997,J.Biol.Chem.,272(14):8864-8866);来自大肠杆菌的AcrB和AcrD(Elkins&Nikaido,2002,J.Bacteriol.,184(23),6490–6499),来自金黄色葡萄球菌(Staphylococcus aereus)的NorA(Ng et al,1994,Antimicrob Agents Chemother,38(6),1345-1355),或来自枯草芽孢杆菌的Bmr(Neyfakh,1992,Antimicrob AgentsChemother,36(2),484-485)增强或放大六亚甲基二胺的流出。
可以通过过表达溶质转运蛋白诸如来自谷氨酸棒杆菌(Corynebacteriumglutamicum)的lysE转运蛋白增强或放大6-氨基己酸和七亚甲基二胺的流出(Bellmann etal,2001,Microbiology,147,1765-1774)。
通过过表达二羧酸转运蛋白诸如来自谷氨酸棒杆菌的SucE转运蛋白增强或放大己二酸的流出(Huhn et al.,Appl.Microbiol&Biotech.,89(2),327-335)。
使用重组宿主生产C6构件块
通常,可以通过提供宿主微生物,并且用含有如上文描述的合适的碳源的培养基培养提供的微生物生成一种或多种C7构件块。一般地,培养基和/或培养可以使得微生物生长到足够的密度并且有效产生C7构件块。对于大规模生产过程,可以使用任何方法,诸如别处描述的(Manual of Industrial Microbiology and Biotechnology,2nd Edition,Editors:A.L.Demain and J.E.Davies,ASM Press;和Principles of FermentationTechnology,P.F.Stanbury and A.Whitaker,Pergamon)。简言之,用特定微生物接种含有合适的培养基的大罐(例如,100加仑、200加仑、500加仑、或更多的罐)。在接种后,培养微生物以容许产生生物量。一旦达到期望的生物量,可以将含有微生物的培养基转移到第二个罐。此第二个罐可以是任何大小。例如,第二个罐可以是较大的,较小的,或者与第一个罐相同大小的。通常,第二个罐大于第一个,使得可以对来自第一个罐的培养基添加额外的培养基。另外,此第二个罐内的培养基可以与第一个罐中使用的培养基相同或不同。
一旦转移,可以温育微生物以容许生成C6构件块。一旦生成,可以使用任何方法来分离C6构件块。例如,可以经由吸附方法从发酵液选择性回收C6构件块。在己二酸和6-氨基己酸的情况下,可以经由蒸发进一步浓缩所得的洗脱液,经由蒸发和/或冷却结晶来结晶,并且经由离心回收晶体。在六亚甲基二胺和1,6-己二醇的情况下,可以采用蒸馏实现期望的产物纯度。
将在以下实施例中进一步描述本发明,其并不限制权利要求中描述的发明的范围。
实施例
实施例1
使用己二酸半醛作为底物并形成6-氨基己酸的ω-转氨酶的酶活性
将编码N末端His-标签的核苷酸序列添加到分别编码SEQ ID NO:7、8、9、10和12的ω-转氨酶的来自紫色色杆菌、铜绿假单胞菌、丁香假单胞菌、球形红杆菌和河流弧菌的核酸序列(参见图6),使得可以产生N末端加HIS标签的ω-转氨酶。将得到的每个修饰的基因在T7启动子控制下克隆到pET21a表达载体中,并将每个表达载体转化到BL21[DE3]大肠杆菌宿主中。所得的重组大肠杆菌菌株在含有50mL LB培养基和抗生素选择压力的250mL摇瓶培养物中于37℃在以230rpm振荡下培养。使用1mM IPTG在16℃诱导每种培养物过夜。
通过离心收获来自每个诱导的摇瓶培养物的团粒。重悬每个团粒并通过超声处理裂解。通过离心从上清液中分离细胞碎片,并将无细胞提取物立即用于酶活性测定。
在由最终浓度为50mM HEPES缓冲液(pH=7.5),10mM 6-氨基己酸,10mM丙酮酸和100μΜ吡哆5’磷酸盐(pyridoxyl 5’phosphate)组成的缓冲液中进行反向(reversedirection)(即6-氨基己酸至己二酸半醛)酶活性测定。通过将ω-转氨酶基因产物或空载体对照的无细胞提取物加入到含有6-氨基己酸的测定缓冲液中来开始每个酶活性测定反应,并在25℃在250rpm振荡的情况下温育24h。通过RP-HPLC对由丙酮酸形成的L-丙氨酸定量。
不含6-氨基己酸的每个仅酶的对照表明丙酮酸向L-丙氨酸的低基线转化。参见图11。如针对空载体对照所证实的,SEQ ID NO 7、SEQ ID NO 9、SEQ ID NO 10和SEQ ID NO12的基因产物接受6-氨基己酸作为底物。参见图12。
对于SEQ ID NO 7、SEQ ID NO 8、SEQ ID NO 9、SEQ ID NO 10和SEQ ID NO 12的转氨酶,证实了正向(forward direction)(即己二酸半醛至6-氨基己酸)酶活性。酶活性测定在由最终浓度为50mM HEPES缓冲液(pH=7.5),10mM己二酸半醛,10mM L-丙氨酸和100μM吡哆醇5'磷酸盐组成的缓冲液中进行。通过将ω-转氨酶基因产物或空载体对照的无细胞提取物加入到含有己二酸半醛的测定缓冲液中来开始每个酶活性测定反应,并在25℃在250rpm振荡的情况下温育4h。通过RP-HPLC定量丙酮酸的形成。
如针对空载体对照所证实的,SEQ ID NO 7、SEQ ID NO 8、SEQ ID NO 9、SEQ IDNO 10和SEQ ID NO 12的基因产物接受己二酸半醛作为底物。参见图13。证实了ω-转氨酶活性的可逆性,这表明SEQ ID NO 7、SEQ ID NO 8、SEQ ID NO 9、SEQ ID NO 10和SEQ IDNO 12的ω-转氨基酶接受己二酸半醛作为底物,并合成6-氨基己酸作为反应产物。
实施例2
使用6-羟基己酸作为底物并形成6-羟基己醛的羧酸还原酶活性
将编码N末端His-标签的核苷酸序列添加到分别编码SEQ ID NO:2-6的羧酸还原酶的来自海分枝杆菌、耻垢分枝杆菌、Segniliparus rugosus、马赛分枝杆菌和Segniliparus rotundus的核酸序列(参见图6),使得可以产生N末端加HIS标签的羧酸还原酶。将每个修饰的基因与编码加His标签的来自枯草芽孢杆菌的磷酸泛酰巯基乙胺转移酶的sfp基因一同克隆到pET Duet表达载体中,均在T7启动子下。将每个表达载体与来自实施例3的表达载体一同转化入BL21[DE3]大肠杆菌宿主中。在含有50mL LB培养基和抗生素选择压力的250mL摇瓶培养物中于37℃在230rpm振荡的情况下培养每个所得的重组大肠杆菌菌株。使用自诱导培养基在37℃诱导每种培养物过夜。
通过离心收获来自每个诱导的摇瓶培养物的团粒。重悬每个团粒并通过超声处理裂解。通过离心从上清液中分离细胞碎片。使用Ni亲和层析从上清液纯化羧酸还原酶和磷酸泛酰巯基乙胺转移酶,以10倍稀释到50mM HEPES缓冲液(pH=7.5)中,并通过超滤浓缩。
在由最终浓度为50mM HEPES缓冲液(pH=7.5),2mM 6-羟基己烷,10mM MgCl2,1mMATP和1mM NADPH组成的缓冲液中一式三份进行酶活性测定(即从6-羟基己酸到6-羟基己醛)。通过将纯化的羧酸还原酶和磷酸泛酰巯基乙胺转移酶或空载体对照加入到含有6-羟基己酸的测定缓冲液中,开始每个酶活性测定反应,然后在室温温育20分钟。通过在340nm处的吸光度监测NADPH的消耗。不含6-羟基己酸的每个仅酶的对照表明NADPH的低基线消耗。参见图7。
如针对空载体对照所证实的,通过sfp的基因产物增强的SEQ ID NO:2-6的基因产物接受6-羟基己酸作为底物(参见图13),并合成6-羟基己醛。
实施例3
用于7-氨基己醇,形成7-氧代己醇的ω-转氨酶活性
将编码N-末端His-标签的核苷酸序列添加到分别编码SEQ ID NO:7-12的ω-转氨酶的紫色色杆菌、铜绿假单胞菌、丁香假单胞菌、球形红杆菌、大肠杆菌和河流弧菌的核酸序列(参见图6),使得可以产生N末端加HIS标签的ω-转氨酶。将修饰的基因在T7启动子下克隆到pET21a表达载体中。将每个表达载体转化到BL21[DE3]大肠杆菌宿主中。将每个所得的重组大肠杆菌菌株在含有50mL LB培养基和抗生素选择压力的250mL摇瓶中于37℃在230rpm振荡情况下培养。使用1mM IPTG在16℃诱导每种培养物过夜。
通过离心收获来自每个诱导的摇瓶培养物的团粒。重悬每个团粒并通过超声处理裂解。通过离心从上清液中分离细胞碎片,并将无细胞提取物立即用于酶活性测定。
在由最终浓度为50mM HEPES缓冲液(pH=7.5),10mM 6-氨基己醇,10mM丙酮酸和100μM吡哆5’磷酸盐组成的缓冲液中进行反向(即6-氨基己醇至6-氧代己醇)酶活性测定。通过将ω-转氨酶基因产物或空载体对照的无细胞提取物加入到含有6-氨基己醇的测定缓冲液中来开始每个酶活性测定反应,并在25℃在250rpm振荡的情况下温育4小时。通过RP-HPLC定量L-丙氨酸的形成。
不含7-氨基己醇的每个仅酶的对照具有丙酮酸向L-丙氨酸的低基线转化。参见图11。
如针对空载体对照所证实的,SEQ ID NO 7-12的基因产物接受6-氨基己醇作为底物(参见图16)并合成6-氧代己醇作为反应产物。鉴于ω-转氨酶活性的可逆性(参见实施例1),可以得出结论,SEQ ID NO7-12的基因产物接受6-氨基己醇作为底物并形成6-氧代己醇。
实施例4
使用六亚甲基二胺作为底物并形成6-氨基己醛的ω-转氨酶的酶活性
将编码N末端His-标签的核苷酸序列添加到分别编码SEQ ID NO:7-12的ω-转氨酶的来自紫色色杆菌、铜绿假单胞菌、丁香假单胞菌、球形红杆菌、大肠杆菌和河流弧菌的核酸序列(参见图6),使得可以产生N末端加HIS标签的ω-转氨酶。将修饰的基因在T7启动子下克隆到pET21a表达载体中。将每个表达载体转化到BL21[DE3]大肠杆菌宿主中。所得的重组大肠杆菌菌株在含有50mL LB培养基和抗生素选择压力的250mL摇瓶培养物中于37℃在以230rpm振荡下培养。使用1mM IPTG在16℃诱导每种培养物过夜。
通过离心收获来自每个诱导的摇瓶培养物的团粒。重悬每个团粒并通过超声处理裂解。通过离心从上清液中分离细胞碎片,并将无细胞提取物立即用于酶活性测定。
在由最终浓度为50mM HEPES缓冲液(pH=7.5),10mM六亚甲基二胺,10mM丙酮酸和100μΜ吡哆5’磷酸盐(pyridoxyl 5’phosphate)组成的缓冲液中进行反向(reversedirection)(即六亚甲基二胺至6-氨基己醛)酶活性测定。通过将ω-转氨酶基因产物或空载体对照的无细胞提取物加入到含有六亚甲基二胺的测定缓冲液中来开始每个酶活性测定反应,并在25℃在250rpm振荡的情况下温育4h。通过RP-HPLC定量L-丙氨酸的形成。
不含六亚甲基二胺的每个仅酶的对照具有丙酮酸向L-丙氨酸的低基线转化。参见图11。
如针对空载体对照所证实的,SEQ ID NO 7-12的基因产物接受六亚甲基二胺作为底物并合成6-氨基己醛作为反应产物。鉴于ω-转氨酶活性的可逆性(参见实施例1),可以得出结论,SEQ ID Nos:7-12的基因产物接受6-氨基己醛作为底物并形成六亚甲基二胺。
实施例5
用于N6-乙酰基-6-氨基己酸,形成N6-乙酰基-6-氨基己醛的羧酸还原酶活性
在由最终浓度为50mM HEPES缓冲液(pH=7.5),2mM N6-乙酰基-6-氨基己酸,10mMMgCl2,1mM ATP和1mM NADPH组成的缓冲液中一式三份测定用于将N6-乙酰基-6-氨基己酸转化为N6-乙酰基-6-氨基己醛的每个N末端加His标签的SEQ ID Nos:4-6的羧酸还原酶的活性(参见实施例2,和图6)。通过将纯化的羧酸还原酶和磷酸泛酰巯基乙胺转移酶或空载体对照加入到含有N6-乙酰基-6-氨基己酸的测定缓冲液中来开始测定,然后在室温温育20min。通过340nm处的吸光度监测NADPH的消耗。不含N6-乙酰基-6-氨基己酸的每个仅酶的对照表明NADPH的低基线消耗。参见图7。
如针对空载体对照所证实的,通过sfp的基因产物增强的SEQ ID NO 4-6的基因产物接受N6-乙酰基-6-氨基己酸作为底物(参见图9),并合成N6-乙酰基-6-氨基己醛。
实施例6
使用N6-乙酰基-1,6-二氨基己烷,并形成N6-乙酰基-6-氨基己醛的ω-转氨酶的酶活性
使用由最终浓度为50mM HEPES缓冲液(pH=7.5),10mM N6-乙酰基-1,6-二氨基己烷,10mM丙酮酸和100μM吡哆5’磷酸盐组成的缓冲液测定用于将N6-乙酰基-1,6-二氨基己烷转化为N6-乙酰基-6-氨基己醛的N末端加His标签的SEQ ID NO:7-12的ω-转氨酶(参见实施例4,和图6)的活性。通过将ω-转氨酶的无细胞提取物或空载体对照加入到含有N6-乙酰基-1,6-二氨基己酸的测定缓冲液中来开始每个酶活性测定反应,然后在25℃在250rpm振荡的情况下温育4h。通过RP-HPLC定量L-丙氨酸的形成。
不含N6-乙酰基-1,6-二氨基己酸的每个仅酶的对照表明丙酮酸到L-丙氨酸的低基线转化。参见图11。
如针对空载体对照所证实的,SEQ ID NO 7-12的基因产物接受N6-乙酰基-1,6-二氨基己烷作为底物(参见图15)并合成N6-乙酰基-6-氨基己醛作为反应产物。
鉴于ω-转氨酶活性的可逆性(参见实施例1),SEQ ID NOs:7-12的基因产物接受N6-乙酰基-6-氨基己醛作为底物,形成N6-乙酰基-1,6-二氨基己烷。
实施例7
使用己二酸半醛作为底物并形成己二醛的羧酸还原酶的酶活性
使用己二酸半醛作为底物测定N-末端加His标签的SEQ ID NO 6的羧酸还原酶(参见实施例2和图6)。在由最终浓度为50mM HEPES缓冲液(pH=7.5),2mM己二酸半醛,10mMMgCl2,1mM ATP和1mM NADPH组成的缓冲液中一式三份进行酶活性测定。通过将纯化的羧酸还原酶和磷酸泛酰巯基乙胺转移酶或空载体对照加入到含有己二酸半醛的测定缓冲液中来开始酶活性测定反应,并然后在室温温育20min。通过340nm处的吸光度监测NADPH的消耗。不含己二酸半醛的每个仅酶的对照表明NADPH的低基线消耗。参见图7。
如针对空载体对照所证实的,通过sfp的基因产物增强的SEQ ID NO:6的基因产物接受己二酸半醛作为底物(参见图10),并合成己二醛。
实施例8
使用4-羟基丁酰基CoA和乙酰CoA作为底物并形成3-氧代-6-羟基己酰基CoA的β-酮硫解酶活性
将编码N末端His-标签的核苷酸序列添加到来自氨基丁酸羧菌的编码SEQ ID NO:14的β-酮硫解酶活性的基因(参见图6),使得可以产生N末端加HIS标签的酶。将所得的修饰的基因在T7启动子控制下克隆到pET15b表达载体中并将该表达载体转化到BL21[DE3]大肠杆菌宿主中。将所得的重组大肠杆菌菌株在含有350mL LB培养基和抗生素选择压力的1L摇瓶培养物中于37℃在以230rpm振荡下培养。使用1mM IPTG在25℃诱导每个培养物过夜。
通过离心收获来自每个诱导的摇瓶培养物的团粒。重悬每个团粒并通过超声处理裂解。通过离心从上清液中分离细胞碎片。使用Ni亲和层析从上清液纯化酶,交换缓冲液并通过超滤浓缩至50mM磷酸钾缓冲液(pH=6.8)中。
在由最终浓度为50mM磷酸钾缓冲液(pH=6.8),75μΜZnCl2,10mMγ-丁内酯和5mM乙酰CoA组成的缓冲液中一式三份进行将4-羟基丁酰基CoA和乙酰CoA转化为3-氧代-6-羟基己酰基CoA的酶活性测定。通过将分别至5[μΜ]的终浓度的SEQ ID NO:14和由来自不动杆菌属ChnC编码的内酯酶加入到含有10mMγ-丁内酯和5mM乙酰CoA组成的测定缓冲液中,并在30℃在180rpm震荡下温育3小时。通过LC-MS确定3-氧代-6-羟基己酰基-CoA的形成。
省略一种底物或一种酶的阴性对照表明没有转化为3-氧代-6-羟基己酰基CoA。通过LC-MS,确认了SEQ ID NO:14接受4-羟基丁酰基CoA和乙酰CoA作为底物并合成3-氧代-6-羟基己酰基CoA作为产物。
其它实施方案
应理解的是,尽管本发明已经结合其详细说明进行描述,但是前面描述意图说明并且不限制发明的范围,本发明的范围由所附权利要求书的范围限定。其它方面、优点和修改也在权利要求书的范围内。
序列表
<110> 英威达技术有限责任公司
<120> 使用Beta-酮硫酯酶生产6-碳单体的方法
<130> 35643-0078WO1
<150> US 62/079,903
<151> 2014-11-14
<160> 17
<170> FastSEQ for Windows Version 4.0
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Val Gly His Val Val Phe Gly Asn Val Ile Gln Thr Glu Pro Arg Asp
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Met Tyr Leu Gly Arg Val Ala Ala Val Asn Gly Gly Val Thr Ile Asn
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Ala Pro Ala Leu Thr Val Asn Arg Leu Cys Gly Ser Gly Leu Gln Ala
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Ile Val Ser Ala Ala Gln Thr Ile Leu Leu Gly Asp Thr Asp Val Ala
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Ile Gly Gly Gly Ala Glu Ser Met Ser Arg Ala Pro Tyr Leu Ala Pro
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Ala Ala Arg Trp Gly Ala Arg Met Gly Asp Ala Gly Leu Val Asp Met
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Met Leu Gly Ala Leu His Asp Pro Phe His Arg Ile His Met Gly Val
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Thr Ala Glu Asn Val Ala Lys Glu Tyr Asp Ile Ser Arg Ala Gln Gln
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Asp Glu Ala Ala Leu Glu Ser His Arg Arg Ala Ser Ala Ala Ile Lys
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Ala Gly Tyr Phe Lys Asp Gln Ile Val Pro Val Val Ser Lys Gly Arg
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Lys Gly Asp Val Thr Phe Asp Thr Asp Glu His Val Arg His Asp Ala
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Thr Ile Asp Asp Met Thr Lys Leu Arg Pro Val Phe Val Lys Glu Asn
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Gly Thr Val Thr Ala Gly Asn Ala Ser Gly Leu Asn Asp Ala Ala Ala
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Ala Val Val Met Met Glu Arg Ala Glu Ala Glu Arg Arg Gly Leu Lys
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Pro Leu Ala Arg Leu Val Ser Tyr Gly His Ala Gly Val Asp Pro Lys
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Ala Met Gly Ile Gly Pro Val Pro Ala Thr Lys Ile Ala Leu Glu Arg
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Ala Gly Leu Gln Val Ser Asp Leu Asp Val Ile Glu Ala Asn Glu Ala
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Ala Lys Val Asn Pro Asn Gly Ser Gly Ile Ser Leu Gly His Pro Ile
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Gly Ala Thr Gly Ala Leu Ile Thr Val Lys Ala Leu His Glu Leu Asn
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Arg Val Gln Gly Arg Tyr Ala Leu Val Thr Met Cys Ile Gly Gly Gly
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Phe Trp Arg Lys Arg Thr Trp Phe Glu Gly Gly Tyr Glu Pro Ser Ile
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Thr Leu Asn Phe Met Pro Met Ser His Val Met Gly Arg Gln Ile Leu
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Ala Val Leu Asp Tyr Lys Leu Val Asp Val Pro Asp Leu Gly Tyr Phe
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Leu Thr Asp Arg Pro His Pro Arg Gly Glu Leu Leu Val Lys Thr Asp
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Ser Leu Phe Pro Gly Tyr Tyr Gln Arg Ala Glu Val Thr Ala Asp Val
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Phe Asp Ala Asp Gly Phe Tyr Arg Thr Gly Asp Ile Met Ala Glu Val
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Gly Pro Glu Gln Phe Val Tyr Leu Asp Arg Arg Asn Asn Val Leu Lys
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Ala Val Pro Val Glu Glu Leu Lys Ala Arg Leu Gly Asp Ser Leu Gln
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Glu Val Ala Lys Ala Ala Gly Leu Gln Ser Tyr Glu Ile Pro Arg Asp
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Phe Ile Ile Glu Thr Thr Pro Trp Thr Leu Glu Asn Gly Leu Leu Thr
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Gly Ile Arg Lys Leu Ala Arg Pro Gln Leu Lys Lys His Tyr Gly Glu
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Leu Arg Ser Leu Arg Gln Ser Gly Ala Asp Ala Pro Val Leu Val Thr
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Val Cys Arg Ala Ala Ala Ala Leu Leu Gly Gly Ser Ala Ser Asp Val
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Gln Pro Asp Ala His Phe Thr Asp Leu Gly Gly Asp Ser Leu Ser Ala
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Leu Ser Phe Thr Asn Leu Leu His Glu Ile Phe Asp Ile Glu Val Pro
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Val Gly Val Ile Val Ser Pro Ala Asn Asp Leu Gln Ala Leu Ala Asp
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Tyr Val Glu Ala Ala Arg Lys Pro Gly Ser Ser Arg Pro Thr Phe Ala
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Ser Val His Gly Ala Ser Asn Gly Gln Val Thr Glu Val His Ala Gly
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Asp Pro Glu Leu Leu Ala His Tyr Arg Ala Leu Ala Gly Asp His Leu
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Glu Val Leu Ala Gly Asp Lys Gly Glu Ala Asp Leu Gly Leu Asp Arg
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Gln Thr Trp Gln Arg Leu Ala Asp Thr Val Asp Leu Ile Val Asp Pro
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Ala Ala Leu Val Asn His Val Leu Pro Tyr Ser Gln Leu Phe Gly Pro
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Asn Ala Leu Gly Thr Ala Glu Leu Leu Arg Leu Ala Leu Thr Ser Lys
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Ile Lys Pro Tyr Ser Tyr Thr Ser Thr Ile Gly Val Ala Asp Gln Ile
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Pro Pro Ser Ala Phe Thr Glu Asp Ala Asp Ile Arg Val Ile Ser Ala
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His Thr Tyr His Val Met Asn Pro Tyr Asp Asp Gly Ile Gly Leu Asp
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Tyr Arg Gln Pro Glu Arg Pro Val Arg Gly Ser Ile Ala Pro Thr Asp
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Arg Phe Arg Ala Ala Val Gln Glu Ala Lys Ile Gly Pro Asp Lys Asp
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Ile Pro His Val Gly Ala Pro Ile Ile Val Lys Tyr Val Ser Asp Leu
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Asn His Leu Gly Gly Arg Ile Pro Ile Ser Thr Ala Val Gln Asn Gly
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Asp Leu Ala Leu Val Arg Pro Thr Glu Leu Gly Leu Val Pro Arg Val
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Ala Asp Met Leu Tyr Gln His His Leu Ala Thr Val Asp Arg Leu Val
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Thr Gln Gly Ala Asp Glu Leu Thr Ala Glu Lys Gln Ala Gly Ala Glu
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Val Val Pro Thr Pro Glu Ala Leu Glu Gln Tyr Asp Pro Ala Ala Leu
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Leu Gln Ser Tyr Glu Val Pro Ala Asp Phe Ile Val Glu Thr Glu Pro
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Pro Asn Leu Lys Asp Arg Tyr Gly Gln Arg Leu Glu Gln Met Tyr Ala
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Ala Ala Thr Gln Pro Val Ile Asp Thr Leu Thr Gln Ala Ala Ala Thr
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Ile Leu Gly Thr Gly Ser Glu Val Ala Ser Asp Ala His Phe Thr Asp
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Asp Phe Phe Gly Phe Glu Val Pro Val Gly Thr Ile Val Asn Pro Ala
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Gly Asp Arg Arg Pro Ser Phe Thr Thr Val His Gly Ala Asp Ala Thr
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Glu Ile Arg Ala Ser Glu Leu Thr Leu Asp Lys Phe Ile Asp Ala Glu
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Thr Leu Arg Ala Ala Pro Gly Leu Pro Lys Val Thr Thr Glu Pro Arg
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Thr Val Leu Leu Ser Gly Ala Asn Gly Trp Leu Gly Arg Phe Leu Thr
785 790 795 800
Leu Gln Trp Leu Glu Arg Leu Ala Pro Val Gly Gly Thr Leu Ile Thr
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Ile Val Arg Gly Arg Asp Asp Ala Ala Ala Arg Ala Arg Leu Thr Gln
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Ala Tyr Asp Thr Asp Pro Glu Leu Ser Arg Arg Phe Ala Glu Leu Ala
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Asp Arg His Leu Arg Val Val Ala Gly Asp Ile Gly Asp Pro Asn Leu
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Gly Leu Thr Pro Glu Ile Trp His Arg Leu Ala Ala Glu Val Asp Leu
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Val Val His Pro Ala Ala Leu Val Asn His Val Leu Pro Tyr Arg Gln
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Leu Phe Gly Pro Asn Val Val Gly Thr Ala Glu Val Ile Lys Leu Ala
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Leu Thr Glu Arg Ile Lys Pro Val Thr Tyr Leu Ser Thr Val Ser Val
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Ala Met Gly Ile Pro Asp Phe Glu Glu Asp Gly Asp Ile Arg Thr Val
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Ser Pro Val Arg Pro Leu Asp Gly Gly Tyr Ala Asn Gly Tyr Gly Asn
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Ser Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His Asp Leu Cys
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Gly Leu Pro Val Ala Thr Phe Arg Ser Asp Met Ile Leu Ala His Pro
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Arg Tyr Arg Gly Gln Val Asn Val Pro Asp Met Phe Thr Arg Leu Leu
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Leu Ser Leu Leu Ile Thr Gly Val Ala Pro Arg Ser Phe Tyr Ile Gly
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Asp Gly Glu Arg Pro Arg Ala His Tyr Pro Gly Leu Thr Val Asp Phe
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Val Ala Glu Ala Val Thr Thr Leu Gly Ala Gln Gln Arg Glu Gly Tyr
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Val Ser Tyr Asp Val Met Asn Pro His Asp Asp Gly Ile Ser Leu Asp
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Val Phe Val Asp Trp Leu Ile Arg Ala Gly His Pro Ile Asp Arg Val
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Asp Asp Tyr Asp Asp Trp Val Arg Arg Phe Glu Thr Ala Leu Thr Ala
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Leu Pro Glu Lys Arg Arg Ala Gln Thr Val Leu Pro Leu Leu His Ala
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Phe Arg Ala Pro Gln Ala Pro Leu Arg Gly Ala Pro Glu Pro Thr Glu
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Val Phe His Ala Ala Val Arg Thr Ala Lys Val Gly Pro Gly Asp Ile
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Pro His Leu Asp Glu Ala Leu Ile Asp Lys Tyr Ile Arg Asp Leu Arg
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Glu Phe Gly Leu Ile
1170
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Met Gly Asp Gly Glu Glu Arg Ala Lys Arg Phe Phe Gln Arg Ile Gly
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Glu Leu Ser Ala Thr Asp Pro Gln Phe Ala Ala Ala Ala Pro Asp Pro
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Ala Val Val Glu Ala Val Ser Asp Pro Ser Leu Ser Phe Thr Arg Tyr
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Arg Val Gly Ala Gly Tyr Glu Thr Ile Ser Tyr Gly Glu Leu Trp Ala
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Arg Val Gly Ala Ile Ala Ala Ala Trp Gln Ala Asp Gly Leu Ala Pro
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Gly Asp Phe Val Ala Thr Val Gly Phe Thr Ser Pro Asp Tyr Val Ala
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Val Asp Leu Ala Ala Ala Arg Ser Gly Leu Val Ser Val Pro Leu Gln
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Ala Gly Ala Ser Leu Ala Gln Leu Val Gly Ile Leu Glu Glu Thr Glu
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Pro Lys Val Leu Ala Ala Ser Ala Ser Ser Leu Glu Gly Ala Val Ala
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Cys Ala Leu Ala Ala Pro Ser Val Gln Arg Leu Val Val Phe Asp Leu
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Arg Gly Pro Asp Ala Ser Glu Ser Ala Ala Asp Glu Arg Arg Gly Ala
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Val Glu Thr Leu Ala Asp Leu Ala Ala Arg Gly Glu Ala Leu Pro Glu
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Ala Pro Leu Phe Glu Pro Ala Glu Gly Glu Asp Pro Leu Ala Leu Leu
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Ile Tyr Thr Ser Gly Ser Thr Gly Ala Pro Lys Gly Ala Met Tyr Ser
245 250 255
Gln Arg Leu Val Ser Gln Leu Trp Gly Arg Thr Pro Val Val Pro Gly
260 265 270
Met Pro Asn Ile Ser Leu His Tyr Met Pro Leu Ser His Ser Tyr Gly
275 280 285
Arg Ala Val Leu Ala Gly Ala Leu Ser Ala Gly Gly Thr Ala His Phe
290 295 300
Thr Ala Asn Ser Asp Leu Ser Thr Leu Phe Glu Asp Ile Ala Leu Ala
305 310 315 320
Arg Pro Thr Phe Leu Ala Leu Val Pro Arg Val Cys Glu Met Leu Phe
325 330 335
Gln Glu Ser Gln Arg Gly Gln Asp Val Ala Glu Leu Arg Glu Arg Val
340 345 350
Leu Gly Gly Arg Leu Leu Val Ala Val Cys Gly Ser Ala Pro Leu Ser
355 360 365
Pro Glu Met Arg Ala Phe Met Glu Glu Val Leu Gly Phe Pro Leu Leu
370 375 380
Asp Gly Tyr Gly Ser Thr Glu Ala Leu Gly Val Met Arg Asn Gly Ile
385 390 395 400
Ile Gln Arg Pro Pro Val Ile Asp Tyr Lys Leu Val Asp Val Pro Glu
405 410 415
Leu Gly Tyr Arg Thr Thr Asp Lys Pro Tyr Pro Arg Gly Glu Leu Cys
420 425 430
Ile Arg Ser Thr Ser Leu Ile Ser Gly Tyr Tyr Lys Arg Pro Glu Ile
435 440 445
Thr Ala Glu Val Phe Asp Ala Gln Gly Tyr Tyr Lys Thr Gly Asp Val
450 455 460
Met Ala Glu Ile Ala Pro Asp His Leu Val Tyr Val Asp Arg Ser Lys
465 470 475 480
Asn Val Leu Lys Leu Ser Gln Gly Glu Phe Val Ala Val Ala Lys Leu
485 490 495
Glu Ala Ala Tyr Gly Thr Ser Pro Tyr Val Lys Gln Ile Phe Val Tyr
500 505 510
Gly Asn Ser Glu Arg Ser Phe Leu Leu Ala Val Val Val Pro Asn Ala
515 520 525
Glu Val Leu Gly Ala Arg Asp Gln Glu Glu Ala Lys Pro Leu Ile Ala
530 535 540
Ala Ser Leu Gln Lys Ile Ala Lys Glu Ala Gly Leu Gln Ser Tyr Glu
545 550 555 560
Val Pro Arg Asp Phe Leu Ile Glu Thr Glu Pro Phe Thr Thr Gln Asn
565 570 575
Gly Leu Leu Ser Glu Val Gly Lys Leu Leu Arg Pro Lys Leu Lys Ala
580 585 590
Arg Tyr Gly Glu Ala Leu Glu Ala Arg Tyr Asp Glu Ile Ala His Gly
595 600 605
Gln Ala Asp Glu Leu Arg Ala Leu Arg Asp Gly Ala Gly Gln Arg Pro
610 615 620
Val Val Glu Thr Val Val Arg Ala Ala Val Ala Ile Ser Gly Ser Glu
625 630 635 640
Gly Ala Glu Val Gly Pro Glu Ala Asn Phe Ala Asp Leu Gly Gly Asp
645 650 655
Ser Leu Ser Ala Leu Ser Leu Ala Asn Leu Leu His Asp Val Phe Glu
660 665 670
Val Glu Val Pro Val Arg Ile Ile Ile Gly Pro Thr Ala Ser Leu Ala
675 680 685
Gly Ile Ala Lys His Ile Glu Ala Glu Arg Ala Gly Ala Ser Ala Pro
690 695 700
Thr Ala Ala Ser Val His Gly Ala Gly Ala Thr Arg Ile Arg Ala Ser
705 710 715 720
Glu Leu Thr Leu Glu Lys Phe Leu Pro Glu Asp Leu Leu Ala Ala Ala
725 730 735
Lys Gly Leu Pro Ala Ala Asp Gln Val Arg Thr Val Leu Leu Thr Gly
740 745 750
Ala Asn Gly Trp Leu Gly Arg Phe Leu Ala Leu Glu Gln Leu Glu Arg
755 760 765
Leu Ala Arg Ser Gly Gln Asp Gly Gly Lys Leu Ile Cys Leu Val Arg
770 775 780
Gly Lys Asp Ala Ala Ala Ala Arg Arg Arg Ile Glu Glu Thr Leu Gly
785 790 795 800
Thr Asp Pro Ala Leu Ala Ala Arg Phe Ala Glu Leu Ala Glu Gly Arg
805 810 815
Leu Glu Val Val Pro Gly Asp Val Gly Glu Pro Lys Phe Gly Leu Asp
820 825 830
Asp Ala Ala Trp Asp Arg Leu Ala Glu Glu Val Asp Val Ile Val His
835 840 845
Pro Ala Ala Leu Val Asn His Val Leu Pro Tyr His Gln Leu Phe Gly
850 855 860
Pro Asn Val Val Gly Thr Ala Glu Ile Ile Arg Leu Ala Ile Thr Ala
865 870 875 880
Lys Arg Lys Pro Val Thr Tyr Leu Ser Thr Val Ala Val Ala Ala Gly
885 890 895
Val Glu Pro Ser Ser Phe Glu Glu Asp Gly Asp Ile Arg Ala Val Val
900 905 910
Pro Glu Arg Pro Leu Gly Asp Gly Tyr Ala Asn Gly Tyr Gly Asn Ser
915 920 925
Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His Glu Leu Val Gly
930 935 940
Leu Pro Val Ala Val Phe Arg Ser Asp Met Ile Leu Ala His Thr Arg
945 950 955 960
Tyr Thr Gly Gln Leu Asn Val Pro Asp Gln Phe Thr Arg Leu Val Leu
965 970 975
Ser Leu Leu Ala Thr Gly Ile Ala Pro Lys Ser Phe Tyr Gln Gln Gly
980 985 990
Ala Ala Gly Glu Arg Gln Arg Ala His Tyr Asp Gly Ile Pro Val Asp
995 1000 1005
Phe Thr Ala Glu Ala Ile Thr Thr Leu Gly Ala Glu Pro Ser Trp Phe
1010 1015 1020
Asp Gly Gly Ala Gly Phe Arg Ser Phe Asp Val Phe Asn Pro His His
1025 1030 1035 1040
Asp Gly Val Gly Leu Asp Glu Phe Val Asp Trp Leu Ile Glu Ala Gly
1045 1050 1055
His Pro Ile Ser Arg Ile Asp Asp His Lys Glu Trp Phe Ala Arg Phe
1060 1065 1070
Glu Thr Ala Val Arg Gly Leu Pro Glu Ala Gln Arg Gln His Ser Leu
1075 1080 1085
Leu Pro Leu Leu Arg Ala Tyr Ser Phe Pro His Pro Pro Val Asp Gly
1090 1095 1100
Ser Val Tyr Pro Thr Gly Lys Phe Gln Gly Ala Val Lys Ala Ala Gln
1105 1110 1115 1120
Val Gly Ser Asp His Asp Val Pro His Leu Gly Lys Ala Leu Ile Val
1125 1130 1135
Lys Tyr Ala Asp Asp Leu Lys Ala Leu Gly Leu Leu
1140 1145
<210> 5
<211> 1185
<212> PRT
<213> 马赛分枝杆菌
<400> 5
Met Thr Asn Glu Thr Asn Pro Gln Gln Glu Gln Leu Ser Arg Arg Ile
1 5 10 15
Glu Ser Leu Arg Glu Ser Asp Pro Gln Phe Arg Ala Ala Gln Pro Asp
20 25 30
Pro Ala Val Ala Glu Gln Val Leu Arg Pro Gly Leu His Leu Ser Glu
35 40 45
Ala Ile Ala Ala Leu Met Thr Gly Tyr Ala Glu Arg Pro Ala Leu Gly
50 55 60
Glu Arg Ala Arg Glu Leu Val Ile Asp Gln Asp Gly Arg Thr Thr Leu
65 70 75 80
Arg Leu Leu Pro Arg Phe Asp Thr Thr Thr Tyr Gly Glu Leu Trp Ser
85 90 95
Arg Thr Thr Ser Val Ala Ala Ala Trp His His Asp Ala Thr His Pro
100 105 110
Val Lys Ala Gly Asp Leu Val Ala Thr Leu Gly Phe Thr Ser Ile Asp
115 120 125
Tyr Thr Val Leu Asp Leu Ala Ile Met Ile Leu Gly Gly Val Ala Val
130 135 140
Pro Leu Gln Thr Ser Ala Pro Ala Ser Gln Trp Thr Thr Ile Leu Ala
145 150 155 160
Glu Ala Glu Pro Asn Thr Leu Ala Val Ser Ile Glu Leu Ile Gly Ala
165 170 175
Ala Met Glu Ser Val Arg Ala Thr Pro Ser Ile Lys Gln Val Val Val
180 185 190
Phe Asp Tyr Thr Pro Glu Val Asp Asp Gln Arg Glu Ala Phe Glu Ala
195 200 205
Ala Ser Thr Gln Leu Ala Gly Thr Gly Ile Ala Leu Glu Thr Leu Asp
210 215 220
Ala Val Ile Ala Arg Gly Ala Ala Leu Pro Ala Ala Pro Leu Tyr Ala
225 230 235 240
Pro Ser Ala Gly Asp Asp Pro Leu Ala Leu Leu Ile Tyr Thr Ser Gly
245 250 255
Ser Thr Gly Ala Pro Lys Gly Ala Met His Ser Glu Asn Ile Val Arg
260 265 270
Arg Trp Trp Ile Arg Glu Asp Val Met Ala Gly Thr Glu Asn Leu Pro
275 280 285
Met Ile Gly Leu Asn Phe Met Pro Met Ser His Ile Met Gly Arg Gly
290 295 300
Thr Leu Thr Ser Thr Leu Ser Thr Gly Gly Thr Gly Tyr Phe Ala Ala
305 310 315 320
Ser Ser Asp Met Ser Thr Leu Phe Glu Asp Met Glu Leu Ile Arg Pro
325 330 335
Thr Ala Leu Ala Leu Val Pro Arg Val Cys Asp Met Val Phe Gln Arg
340 345 350
Phe Gln Thr Glu Val Asp Arg Arg Leu Ala Ser Gly Asp Thr Ala Ser
355 360 365
Ala Glu Ala Val Ala Ala Glu Val Lys Ala Asp Ile Arg Asp Asn Leu
370 375 380
Phe Gly Gly Arg Val Ser Ala Val Met Val Gly Ser Ala Pro Leu Ser
385 390 395 400
Glu Glu Leu Gly Glu Phe Ile Glu Ser Cys Phe Glu Leu Asn Leu Thr
405 410 415
Asp Gly Tyr Gly Ser Thr Glu Ala Gly Met Val Phe Arg Asp Gly Ile
420 425 430
Val Gln Arg Pro Pro Val Ile Asp Tyr Lys Leu Val Asp Val Pro Glu
435 440 445
Leu Gly Tyr Phe Ser Thr Asp Lys Pro His Pro Arg Gly Glu Leu Leu
450 455 460
Leu Lys Thr Asp Gly Met Phe Leu Gly Tyr Tyr Lys Arg Pro Glu Val
465 470 475 480
Thr Ala Ser Val Phe Asp Ala Asp Gly Phe Tyr Met Thr Gly Asp Ile
485 490 495
Val Ala Glu Leu Ala His Asp Asn Ile Glu Ile Ile Asp Arg Arg Asn
500 505 510
Asn Val Leu Lys Leu Ser Gln Gly Glu Phe Val Ala Val Ala Thr Leu
515 520 525
Glu Ala Glu Tyr Ala Asn Ser Pro Val Val His Gln Ile Tyr Val Tyr
530 535 540
Gly Ser Ser Glu Arg Ser Tyr Leu Leu Ala Val Val Val Pro Thr Pro
545 550 555 560
Glu Ala Val Ala Ala Ala Lys Gly Asp Ala Ala Ala Leu Lys Thr Thr
565 570 575
Ile Ala Asp Ser Leu Gln Asp Ile Ala Lys Glu Ile Gln Leu Gln Ser
580 585 590
Tyr Glu Val Pro Arg Asp Phe Ile Ile Glu Pro Gln Pro Phe Thr Gln
595 600 605
Gly Asn Gly Leu Leu Thr Gly Ile Ala Lys Leu Ala Arg Pro Asn Leu
610 615 620
Lys Ala His Tyr Gly Pro Arg Leu Glu Gln Met Tyr Ala Glu Ile Ala
625 630 635 640
Glu Gln Gln Ala Ala Glu Leu Arg Ala Leu His Gly Val Asp Pro Asp
645 650 655
Lys Pro Ala Leu Glu Thr Val Leu Lys Ala Ala Gln Ala Leu Leu Gly
660 665 670
Val Ser Ser Ala Glu Leu Ala Ala Asp Ala His Phe Thr Asp Leu Gly
675 680 685
Gly Asp Ser Leu Ser Ala Leu Ser Phe Ser Asp Leu Leu Arg Asp Ile
690 695 700
Phe Ala Val Glu Val Pro Val Gly Val Ile Val Ser Ala Ala Asn Asp
705 710 715 720
Leu Gly Gly Val Ala Lys Phe Val Asp Glu Gln Arg His Ser Gly Gly
725 730 735
Thr Arg Pro Thr Ala Glu Thr Val His Gly Ala Gly His Thr Glu Ile
740 745 750
Arg Ala Ala Asp Leu Thr Leu Asp Lys Phe Ile Asp Glu Ala Thr Leu
755 760 765
His Ala Ala Pro Ser Leu Pro Lys Ala Ala Gly Ile Pro His Thr Val
770 775 780
Leu Leu Thr Gly Ser Asn Gly Tyr Leu Gly His Tyr Leu Ala Leu Glu
785 790 795 800
Trp Leu Glu Arg Leu Asp Lys Thr Asp Gly Lys Leu Ile Val Ile Val
805 810 815
Arg Gly Lys Asn Ala Glu Ala Ala Tyr Gly Arg Leu Glu Glu Ala Phe
820 825 830
Asp Thr Gly Asp Thr Glu Leu Leu Ala His Phe Arg Ser Leu Ala Asp
835 840 845
Lys His Leu Glu Val Leu Ala Gly Asp Ile Gly Asp Pro Asn Leu Gly
850 855 860
Leu Asp Ala Asp Thr Trp Gln Arg Leu Ala Asp Thr Val Asp Val Ile
865 870 875 880
Val His Pro Ala Ala Leu Val Asn His Val Leu Pro Tyr Asn Gln Leu
885 890 895
Phe Gly Pro Asn Val Val Gly Thr Ala Glu Ile Ile Lys Leu Ala Ile
900 905 910
Thr Thr Lys Ile Lys Pro Val Thr Tyr Leu Ser Thr Val Ala Val Ala
915 920 925
Ala Tyr Val Asp Pro Thr Thr Phe Asp Glu Glu Ser Asp Ile Arg Leu
930 935 940
Ile Ser Ala Val Arg Pro Ile Asp Asp Gly Tyr Ala Asn Gly Tyr Gly
945 950 955 960
Asn Ala Lys Trp Ala Gly Glu Val Leu Leu Arg Glu Ala His Asp Leu
965 970 975
Cys Gly Leu Pro Val Ala Val Phe Arg Ser Asp Met Ile Leu Ala His
980 985 990
Ser Arg Tyr Thr Gly Gln Leu Asn Val Pro Asp Gln Phe Thr Arg Leu
995 1000 1005
Ile Leu Ser Leu Ile Ala Thr Gly Ile Ala Pro Gly Ser Phe Tyr Gln
1010 1015 1020
Ala Gln Thr Thr Gly Glu Arg Pro Leu Ala His Tyr Asp Gly Leu Pro
1025 1030 1035 1040
Gly Asp Phe Thr Ala Glu Ala Ile Thr Thr Leu Gly Thr Gln Val Pro
1045 1050 1055
Glu Gly Ser Glu Gly Phe Val Thr Tyr Asp Cys Val Asn Pro His Ala
1060 1065 1070
Asp Gly Ile Ser Leu Asp Asn Phe Val Asp Trp Leu Ile Glu Ala Gly
1075 1080 1085
Tyr Pro Ile Ala Arg Ile Asp Asn Tyr Thr Glu Trp Phe Thr Arg Phe
1090 1095 1100
Asp Thr Ala Ile Arg Gly Leu Ser Glu Lys Gln Lys Gln His Ser Leu
1105 1110 1115 1120
Leu Pro Leu Leu His Ala Phe Glu Gln Pro Ser Ala Ala Glu Asn His
1125 1130 1135
Gly Val Val Pro Ala Lys Arg Phe Gln His Ala Val Gln Ala Ala Gly
1140 1145 1150
Ile Gly Pro Val Gly Gln Asp Gly Thr Thr Asp Ile Pro His Leu Ser
1155 1160 1165
Arg Arg Leu Ile Val Lys Tyr Ala Lys Asp Leu Glu Gln Leu Gly Leu
1170 1175 1180
Leu
1185
<210> 6
<211> 1186
<212> PRT
<213> Segniliparus rotundus
<400> 6
Met Thr Gln Ser His Thr Gln Gly Pro Gln Ala Ser Ala Ala His Ser
1 5 10 15
Arg Leu Ala Arg Arg Ala Ala Glu Leu Leu Ala Thr Asp Pro Gln Ala
20 25 30
Ala Ala Thr Leu Pro Asp Pro Glu Val Val Arg Gln Ala Thr Arg Pro
35 40 45
Gly Leu Arg Leu Ala Glu Arg Val Asp Ala Ile Leu Ser Gly Tyr Ala
50 55 60
Asp Arg Pro Ala Leu Gly Gln Arg Ser Phe Gln Thr Val Lys Asp Pro
65 70 75 80
Ile Thr Gly Arg Ser Ser Val Glu Leu Leu Pro Thr Phe Asp Thr Ile
85 90 95
Thr Tyr Arg Glu Leu Arg Glu Arg Ala Thr Ala Ile Ala Ser Asp Leu
100 105 110
Ala His His Pro Gln Ala Pro Ala Lys Pro Gly Asp Phe Leu Ala Ser
115 120 125
Ile Gly Phe Ile Ser Val Asp Tyr Val Ala Ile Asp Ile Ala Gly Val
130 135 140
Phe Ala Gly Leu Thr Ala Val Pro Leu Gln Thr Gly Ala Thr Leu Ala
145 150 155 160
Thr Leu Thr Ala Ile Thr Ala Glu Thr Ala Pro Thr Leu Phe Ala Ala
165 170 175
Ser Ile Glu His Leu Pro Thr Ala Val Asp Ala Val Leu Ala Thr Pro
180 185 190
Ser Val Arg Arg Leu Leu Val Phe Asp Tyr Arg Ala Gly Ser Asp Glu
195 200 205
Asp Arg Glu Ala Val Glu Ala Ala Lys Arg Lys Ile Ala Asp Ala Gly
210 215 220
Ser Ser Val Leu Val Asp Val Leu Asp Glu Val Ile Ala Arg Gly Lys
225 230 235 240
Ser Ala Pro Lys Ala Pro Leu Pro Pro Ala Thr Asp Ala Gly Asp Asp
245 250 255
Ser Leu Ser Leu Leu Ile Tyr Thr Ser Gly Ser Thr Gly Thr Pro Lys
260 265 270
Gly Ala Met Tyr Pro Glu Arg Asn Val Ala His Phe Trp Gly Gly Val
275 280 285
Trp Ala Ala Ala Phe Asp Glu Asp Ala Ala Pro Pro Val Pro Ala Ile
290 295 300
Asn Ile Thr Phe Leu Pro Leu Ser His Val Ala Ser Arg Leu Ser Leu
305 310 315 320
Met Pro Thr Leu Ala Arg Gly Gly Leu Met His Phe Val Ala Lys Ser
325 330 335
Asp Leu Ser Thr Leu Phe Glu Asp Leu Lys Leu Ala Arg Pro Thr Asn
340 345 350
Leu Phe Leu Val Pro Arg Val Val Glu Met Leu Tyr Gln His Tyr Gln
355 360 365
Ser Glu Leu Asp Arg Arg Gly Val Gln Asp Gly Thr Arg Glu Ala Glu
370 375 380
Ala Val Lys Asp Asp Leu Arg Thr Gly Leu Leu Gly Gly Arg Ile Leu
385 390 395 400
Thr Ala Gly Phe Gly Ser Ala Pro Leu Ser Ala Glu Leu Ala Gly Phe
405 410 415
Ile Glu Ser Leu Leu Gln Ile His Leu Val Asp Gly Tyr Gly Ser Thr
420 425 430
Glu Ala Gly Pro Val Trp Arg Asp Gly Tyr Leu Val Lys Pro Pro Val
435 440 445
Thr Asp Tyr Lys Leu Ile Asp Val Pro Glu Leu Gly Tyr Phe Ser Thr
450 455 460
Asp Ser Pro His Pro Arg Gly Glu Leu Ala Ile Lys Thr Gln Thr Ile
465 470 475 480
Leu Pro Gly Tyr Tyr Lys Arg Pro Glu Thr Thr Ala Glu Val Phe Asp
485 490 495
Glu Asp Gly Phe Tyr Leu Thr Gly Asp Val Val Ala Gln Ile Gly Pro
500 505 510
Glu Gln Phe Ala Tyr Val Asp Arg Arg Lys Asn Val Leu Lys Leu Ser
515 520 525
Gln Gly Glu Phe Val Thr Leu Ala Lys Leu Glu Ala Ala Tyr Ser Ser
530 535 540
Ser Pro Leu Val Arg Gln Leu Phe Val Tyr Gly Ser Ser Glu Arg Ser
545 550 555 560
Tyr Leu Leu Ala Val Ile Val Pro Thr Pro Asp Ala Leu Lys Lys Phe
565 570 575
Gly Val Gly Glu Ala Ala Lys Ala Ala Leu Gly Glu Ser Leu Gln Lys
580 585 590
Ile Ala Arg Asp Glu Gly Leu Gln Ser Tyr Glu Val Pro Arg Asp Phe
595 600 605
Ile Ile Glu Thr Asp Pro Phe Thr Val Glu Asn Gly Leu Leu Ser Asp
610 615 620
Ala Arg Lys Ser Leu Arg Pro Lys Leu Lys Glu His Tyr Gly Glu Arg
625 630 635 640
Leu Glu Ala Met Tyr Lys Glu Leu Ala Asp Gly Gln Ala Asn Glu Leu
645 650 655
Arg Asp Ile Arg Arg Gly Val Gln Gln Arg Pro Thr Leu Glu Thr Val
660 665 670
Arg Arg Ala Ala Ala Ala Met Leu Gly Ala Ser Ala Ala Glu Ile Lys
675 680 685
Pro Asp Ala His Phe Thr Asp Leu Gly Gly Asp Ser Leu Ser Ala Leu
690 695 700
Thr Phe Ser Asn Phe Leu His Asp Leu Phe Glu Val Asp Val Pro Val
705 710 715 720
Gly Val Ile Val Ser Ala Ala Asn Thr Leu Gly Ser Val Ala Glu His
725 730 735
Ile Asp Ala Gln Leu Ala Gly Gly Arg Ala Arg Pro Thr Phe Ala Thr
740 745 750
Val His Gly Lys Gly Ser Thr Thr Ile Lys Ala Ser Asp Leu Thr Leu
755 760 765
Asp Lys Phe Ile Asp Glu Gln Thr Leu Glu Ala Ala Lys His Leu Pro
770 775 780
Lys Pro Ala Asp Pro Pro Arg Thr Val Leu Leu Thr Gly Ala Asn Gly
785 790 795 800
Trp Leu Gly Arg Phe Leu Ala Leu Glu Trp Leu Glu Arg Leu Ala Pro
805 810 815
Ala Gly Gly Lys Leu Ile Thr Ile Val Arg Gly Lys Asp Ala Ala Gln
820 825 830
Ala Lys Ala Arg Leu Asp Ala Ala Tyr Glu Ser Gly Asp Pro Lys Leu
835 840 845
Ala Gly His Tyr Gln Asp Leu Ala Ala Thr Thr Leu Glu Val Leu Ala
850 855 860
Gly Asp Phe Ser Glu Pro Arg Leu Gly Leu Asp Glu Ala Thr Trp Asn
865 870 875 880
Arg Leu Ala Asp Glu Val Asp Phe Ile Ser His Pro Gly Ala Leu Val
885 890 895
Asn His Val Leu Pro Tyr Asn Gln Leu Phe Gly Pro Asn Val Ala Gly
900 905 910
Val Ala Glu Ile Ile Lys Leu Ala Ile Thr Thr Arg Ile Lys Pro Val
915 920 925
Thr Tyr Leu Ser Thr Val Ala Val Ala Ala Gly Val Glu Pro Ser Ala
930 935 940
Leu Asp Glu Asp Gly Asp Ile Arg Thr Val Ser Ala Glu Arg Ser Val
945 950 955 960
Asp Glu Gly Tyr Ala Asn Gly Tyr Gly Asn Ser Lys Trp Gly Gly Glu
965 970 975
Val Leu Leu Arg Glu Ala His Asp Arg Thr Gly Leu Pro Val Arg Val
980 985 990
Phe Arg Ser Asp Met Ile Leu Ala His Gln Lys Tyr Thr Gly Gln Val
995 1000 1005
Asn Ala Thr Asp Gln Phe Thr Arg Leu Val Gln Ser Leu Leu Ala Thr
1010 1015 1020
Gly Leu Ala Pro Lys Ser Phe Tyr Glu Leu Asp Ala Gln Gly Asn Arg
1025 1030 1035 1040
Gln Arg Ala His Tyr Asp Gly Ile Pro Val Asp Phe Thr Ala Glu Ser
1045 1050 1055
Ile Thr Thr Leu Gly Gly Asp Gly Leu Glu Gly Tyr Arg Ser Tyr Asn
1060 1065 1070
Val Phe Asn Pro His Arg Asp Gly Val Gly Leu Asp Glu Phe Val Asp
1075 1080 1085
Trp Leu Ile Glu Ala Gly His Pro Ile Thr Arg Ile Asp Asp Tyr Asp
1090 1095 1100
Gln Trp Leu Ser Arg Phe Glu Thr Ser Leu Arg Gly Leu Pro Glu Ser
1105 1110 1115 1120
Lys Arg Gln Ala Ser Val Leu Pro Leu Leu His Ala Phe Ala Arg Pro
1125 1130 1135
Gly Pro Ala Val Asp Gly Ser Pro Phe Arg Asn Thr Val Phe Arg Thr
1140 1145 1150
Asp Val Gln Lys Ala Lys Ile Gly Ala Glu His Asp Ile Pro His Leu
1155 1160 1165
Gly Lys Ala Leu Val Leu Lys Tyr Ala Asp Asp Ile Lys Gln Leu Gly
1170 1175 1180
Leu Leu
1185
<210> 7
<211> 459
<212> PRT
<213> 紫色色杆菌
<400> 7
Met Gln Lys Gln Arg Thr Thr Ser Gln Trp Arg Glu Leu Asp Ala Ala
1 5 10 15
His His Leu His Pro Phe Thr Asp Thr Ala Ser Leu Asn Gln Ala Gly
20 25 30
Ala Arg Val Met Thr Arg Gly Glu Gly Val Tyr Leu Trp Asp Ser Glu
35 40 45
Gly Asn Lys Ile Ile Asp Gly Met Ala Gly Leu Trp Cys Val Asn Val
50 55 60
Gly Tyr Gly Arg Lys Asp Phe Ala Glu Ala Ala Arg Arg Gln Met Glu
65 70 75 80
Glu Leu Pro Phe Tyr Asn Thr Phe Phe Lys Thr Thr His Pro Ala Val
85 90 95
Val Glu Leu Ser Ser Leu Leu Ala Glu Val Thr Pro Ala Gly Phe Asp
100 105 110
Arg Val Phe Tyr Thr Asn Ser Gly Ser Glu Ser Val Asp Thr Met Ile
115 120 125
Arg Met Val Arg Arg Tyr Trp Asp Val Gln Gly Lys Pro Glu Lys Lys
130 135 140
Thr Leu Ile Gly Arg Trp Asn Gly Tyr His Gly Ser Thr Ile Gly Gly
145 150 155 160
Ala Ser Leu Gly Gly Met Lys Tyr Met His Glu Gln Gly Asp Leu Pro
165 170 175
Ile Pro Gly Met Ala His Ile Glu Gln Pro Trp Trp Tyr Lys His Gly
180 185 190
Lys Asp Met Thr Pro Asp Glu Phe Gly Val Val Ala Ala Arg Trp Leu
195 200 205
Glu Glu Lys Ile Leu Glu Ile Gly Ala Asp Lys Val Ala Ala Phe Val
210 215 220
Gly Glu Pro Ile Gln Gly Ala Gly Gly Val Ile Val Pro Pro Ala Thr
225 230 235 240
Tyr Trp Pro Glu Ile Glu Arg Ile Cys Arg Lys Tyr Asp Val Leu Leu
245 250 255
Val Ala Asp Glu Val Ile Cys Gly Phe Gly Arg Thr Gly Glu Trp Phe
260 265 270
Gly His Gln His Phe Gly Phe Gln Pro Asp Leu Phe Thr Ala Ala Lys
275 280 285
Gly Leu Ser Ser Gly Tyr Leu Pro Ile Gly Ala Val Phe Val Gly Lys
290 295 300
Arg Val Ala Glu Gly Leu Ile Ala Gly Gly Asp Phe Asn His Gly Phe
305 310 315 320
Thr Tyr Ser Gly His Pro Val Cys Ala Ala Val Ala His Ala Asn Val
325 330 335
Ala Ala Leu Arg Asp Glu Gly Ile Val Gln Arg Val Lys Asp Asp Ile
340 345 350
Gly Pro Tyr Met Gln Lys Arg Trp Arg Glu Thr Phe Ser Arg Phe Glu
355 360 365
His Val Asp Asp Val Arg Gly Val Gly Met Val Gln Ala Phe Thr Leu
370 375 380
Val Lys Asn Lys Ala Lys Arg Glu Leu Phe Pro Asp Phe Gly Glu Ile
385 390 395 400
Gly Thr Leu Cys Arg Asp Ile Phe Phe Arg Asn Asn Leu Ile Met Arg
405 410 415
Ala Cys Gly Asp His Ile Val Ser Ala Pro Pro Leu Val Met Thr Arg
420 425 430
Ala Glu Val Asp Glu Met Leu Ala Val Ala Glu Arg Cys Leu Glu Glu
435 440 445
Phe Glu Gln Thr Leu Lys Ala Arg Gly Leu Ala
450 455
<210> 8
<211> 468
<212> PRT
<213> 铜绿假单胞菌
<400> 8
Met Asn Ala Arg Leu His Ala Thr Ser Pro Leu Gly Asp Ala Asp Leu
1 5 10 15
Val Arg Ala Asp Gln Ala His Tyr Met His Gly Tyr His Val Phe Asp
20 25 30
Asp His Arg Val Asn Gly Ser Leu Asn Ile Ala Ala Gly Asp Gly Ala
35 40 45
Tyr Ile Tyr Asp Thr Ala Gly Asn Arg Tyr Leu Asp Ala Val Gly Gly
50 55 60
Met Trp Cys Thr Asn Ile Gly Leu Gly Arg Glu Glu Met Ala Arg Thr
65 70 75 80
Val Ala Glu Gln Thr Arg Leu Leu Ala Tyr Ser Asn Pro Phe Cys Asp
85 90 95
Met Ala Asn Pro Arg Ala Ile Glu Leu Cys Arg Lys Leu Ala Glu Leu
100 105 110
Ala Pro Gly Asp Leu Asp His Val Phe Leu Thr Thr Gly Gly Ser Thr
115 120 125
Ala Val Asp Thr Ala Ile Arg Leu Met His Tyr Tyr Gln Asn Cys Arg
130 135 140
Gly Lys Arg Ala Lys Lys His Val Ile Thr Arg Ile Asn Ala Tyr His
145 150 155 160
Gly Ser Thr Phe Leu Gly Met Ser Leu Gly Gly Lys Ser Ala Asp Arg
165 170 175
Pro Ala Glu Phe Asp Phe Leu Asp Glu Arg Ile His His Leu Ala Cys
180 185 190
Pro Tyr Tyr Tyr Arg Ala Pro Glu Gly Leu Gly Glu Ala Glu Phe Leu
195 200 205
Asp Gly Leu Val Asp Glu Phe Glu Arg Lys Ile Leu Glu Leu Gly Ala
210 215 220
Asp Arg Val Gly Ala Phe Ile Ser Glu Pro Val Phe Gly Ser Gly Gly
225 230 235 240
Val Ile Val Pro Pro Ala Gly Tyr His Arg Arg Met Trp Glu Leu Cys
245 250 255
Gln Arg Tyr Asp Val Leu Tyr Ile Ser Asp Glu Val Val Thr Ser Phe
260 265 270
Gly Arg Leu Gly His Phe Phe Ala Ser Gln Ala Val Phe Gly Val Gln
275 280 285
Pro Asp Ile Ile Leu Thr Ala Lys Gly Leu Thr Ser Gly Tyr Gln Pro
290 295 300
Leu Gly Ala Cys Ile Phe Ser Arg Arg Ile Trp Glu Val Ile Ala Glu
305 310 315 320
Pro Asp Lys Gly Arg Cys Phe Ser His Gly Phe Thr Tyr Ser Gly His
325 330 335
Pro Val Ala Cys Ala Ala Ala Leu Lys Asn Ile Glu Ile Ile Glu Arg
340 345 350
Glu Gly Leu Leu Ala His Ala Asp Glu Val Gly Arg Tyr Phe Glu Glu
355 360 365
Arg Leu Gln Ser Leu Arg Asp Leu Pro Ile Val Gly Asp Val Arg Gly
370 375 380
Met Arg Phe Met Ala Cys Val Glu Phe Val Ala Asp Lys Ala Ser Lys
385 390 395 400
Ala Leu Phe Pro Glu Ser Leu Asn Ile Gly Glu Trp Val His Leu Arg
405 410 415
Ala Gln Lys Arg Gly Leu Leu Val Arg Pro Ile Val His Leu Asn Val
420 425 430
Met Ser Pro Pro Leu Ile Leu Thr Arg Glu Gln Val Asp Thr Val Val
435 440 445
Arg Val Leu Arg Glu Ser Ile Glu Glu Thr Val Glu Asp Leu Val Arg
450 455 460
Ala Gly His Arg
465
<210> 9
<211> 454
<212> PRT
<213> 丁香假单胞菌
<400> 9
Met Ser Ala Asn Asn Pro Gln Thr Leu Glu Trp Gln Ala Leu Ser Ser
1 5 10 15
Glu His His Leu Ala Pro Phe Ser Asp Tyr Lys Gln Leu Lys Glu Lys
20 25 30
Gly Pro Arg Ile Ile Thr Arg Ala Glu Gly Val Tyr Leu Trp Asp Ser
35 40 45
Glu Gly Asn Lys Ile Leu Asp Gly Met Ser Gly Leu Trp Cys Val Ala
50 55 60
Ile Gly Tyr Gly Arg Glu Glu Leu Ala Asp Ala Ala Ser Lys Gln Met
65 70 75 80
Arg Glu Leu Pro Tyr Tyr Asn Leu Phe Phe Gln Thr Ala His Pro Pro
85 90 95
Val Leu Glu Leu Ala Lys Ala Ile Ser Asp Ile Ala Pro Glu Gly Met
100 105 110
Asn His Val Phe Phe Thr Gly Ser Gly Ser Glu Gly Asn Asp Thr Met
115 120 125
Leu Arg Met Val Arg His Tyr Trp Ala Leu Lys Gly Gln Pro Asn Lys
130 135 140
Lys Thr Ile Ile Ser Arg Val Asn Gly Tyr His Gly Ser Thr Val Ala
145 150 155 160
Gly Ala Ser Leu Gly Gly Met Thr Tyr Met His Glu Gln Gly Asp Leu
165 170 175
Pro Ile Pro Gly Val Val His Ile Pro Gln Pro Tyr Trp Phe Gly Glu
180 185 190
Gly Gly Asp Met Thr Pro Asp Glu Phe Gly Ile Trp Ala Ala Glu Gln
195 200 205
Leu Glu Lys Lys Ile Leu Glu Leu Gly Val Glu Asn Val Gly Ala Phe
210 215 220
Ile Ala Glu Pro Ile Gln Gly Ala Gly Gly Val Ile Val Pro Pro Asp
225 230 235 240
Ser Tyr Trp Pro Lys Ile Lys Glu Ile Leu Ser Arg Tyr Asp Ile Leu
245 250 255
Phe Ala Ala Asp Glu Val Ile Cys Gly Phe Gly Arg Thr Ser Glu Trp
260 265 270
Phe Gly Ser Asp Phe Tyr Gly Leu Arg Pro Asp Met Met Thr Ile Ala
275 280 285
Lys Gly Leu Thr Ser Gly Tyr Val Pro Met Gly Gly Leu Ile Val Arg
290 295 300
Asp Glu Ile Val Ala Val Leu Asn Glu Gly Gly Asp Phe Asn His Gly
305 310 315 320
Phe Thr Tyr Ser Gly His Pro Val Ala Ala Ala Val Ala Leu Glu Asn
325 330 335
Ile Arg Ile Leu Arg Glu Glu Lys Ile Val Glu Arg Val Arg Ser Glu
340 345 350
Thr Ala Pro Tyr Leu Gln Lys Arg Leu Arg Glu Leu Ser Asp His Pro
355 360 365
Leu Val Gly Glu Val Arg Gly Val Gly Leu Leu Gly Ala Ile Glu Leu
370 375 380
Val Lys Asp Lys Thr Thr Arg Glu Arg Tyr Thr Asp Lys Gly Ala Gly
385 390 395 400
Met Ile Cys Arg Thr Phe Cys Phe Asp Asn Gly Leu Ile Met Arg Ala
405 410 415
Val Gly Asp Thr Met Ile Ile Ala Pro Pro Leu Val Ile Ser Phe Ala
420 425 430
Gln Ile Asp Glu Leu Val Glu Lys Ala Arg Thr Cys Leu Asp Leu Thr
435 440 445
Leu Ala Val Leu Gln Gly
450
<210> 10
<211> 467
<212> PRT
<213> 球形红杆菌
<400> 10
Met Thr Arg Asn Asp Ala Thr Asn Ala Ala Gly Ala Val Gly Ala Ala
1 5 10 15
Met Arg Asp His Ile Leu Leu Pro Ala Gln Glu Met Ala Lys Leu Gly
20 25 30
Lys Ser Ala Gln Pro Val Leu Thr His Ala Glu Gly Ile Tyr Val His
35 40 45
Thr Glu Asp Gly Arg Arg Leu Ile Asp Gly Pro Ala Gly Met Trp Cys
50 55 60
Ala Gln Val Gly Tyr Gly Arg Arg Glu Ile Val Asp Ala Met Ala His
65 70 75 80
Gln Ala Met Val Leu Pro Tyr Ala Ser Pro Trp Tyr Met Ala Thr Ser
85 90 95
Pro Ala Ala Arg Leu Ala Glu Lys Ile Ala Thr Leu Thr Pro Gly Asp
100 105 110
Leu Asn Arg Ile Phe Phe Thr Thr Gly Gly Ser Thr Ala Val Asp Ser
115 120 125
Ala Leu Arg Phe Ser Glu Phe Tyr Asn Asn Val Leu Gly Arg Pro Gln
130 135 140
Lys Lys Arg Ile Ile Val Arg Tyr Asp Gly Tyr His Gly Ser Thr Ala
145 150 155 160
Leu Thr Ala Ala Cys Thr Gly Arg Thr Gly Asn Trp Pro Asn Phe Asp
165 170 175
Ile Ala Gln Asp Arg Ile Ser Phe Leu Ser Ser Pro Asn Pro Arg His
180 185 190
Ala Gly Asn Arg Ser Gln Glu Ala Phe Leu Asp Asp Leu Val Gln Glu
195 200 205
Phe Glu Asp Arg Ile Glu Ser Leu Gly Pro Asp Thr Ile Ala Ala Phe
210 215 220
Leu Ala Glu Pro Ile Leu Ala Ser Gly Gly Val Ile Ile Pro Pro Ala
225 230 235 240
Gly Tyr His Ala Arg Phe Lys Ala Ile Cys Glu Lys His Asp Ile Leu
245 250 255
Tyr Ile Ser Asp Glu Val Val Thr Gly Phe Gly Arg Cys Gly Glu Trp
260 265 270
Phe Ala Ser Glu Lys Val Phe Gly Val Val Pro Asp Ile Ile Thr Phe
275 280 285
Ala Lys Gly Val Thr Ser Gly Tyr Val Pro Leu Gly Gly Leu Ala Ile
290 295 300
Ser Glu Ala Val Leu Ala Arg Ile Ser Gly Glu Asn Ala Lys Gly Ser
305 310 315 320
Trp Phe Thr Asn Gly Tyr Thr Tyr Ser Asn Gln Pro Val Ala Cys Ala
325 330 335
Ala Ala Leu Ala Asn Ile Glu Leu Met Glu Arg Glu Gly Ile Val Asp
340 345 350
Gln Ala Arg Glu Met Ala Asp Tyr Phe Ala Ala Ala Leu Ala Ser Leu
355 360 365
Arg Asp Leu Pro Gly Val Ala Glu Thr Arg Ser Val Gly Leu Val Gly
370 375 380
Cys Val Gln Cys Leu Leu Asp Pro Thr Arg Ala Asp Gly Thr Ala Glu
385 390 395 400
Asp Lys Ala Phe Thr Leu Lys Ile Asp Glu Arg Cys Phe Glu Leu Gly
405 410 415
Leu Ile Val Arg Pro Leu Gly Asp Leu Cys Val Ile Ser Pro Pro Leu
420 425 430
Ile Ile Ser Arg Ala Gln Ile Asp Glu Met Val Ala Ile Met Arg Gln
435 440 445
Ala Ile Thr Glu Val Ser Ala Ala His Gly Leu Thr Ala Lys Glu Pro
450 455 460
Ala Ala Val
465
<210> 11
<211> 459
<212> PRT
<213> 大肠杆菌
<400> 11
Met Asn Arg Leu Pro Ser Ser Ala Ser Ala Leu Ala Cys Ser Ala His
1 5 10 15
Ala Leu Asn Leu Ile Glu Lys Arg Thr Leu Asp His Glu Glu Met Lys
20 25 30
Ala Leu Asn Arg Glu Val Ile Glu Tyr Phe Lys Glu His Val Asn Pro
35 40 45
Gly Phe Leu Glu Tyr Arg Lys Ser Val Thr Ala Gly Gly Asp Tyr Gly
50 55 60
Ala Val Glu Trp Gln Ala Gly Ser Leu Asn Thr Leu Val Asp Thr Gln
65 70 75 80
Gly Gln Glu Phe Ile Asp Cys Leu Gly Gly Phe Gly Ile Phe Asn Val
85 90 95
Gly His Arg Asn Pro Val Val Val Ser Ala Val Gln Asn Gln Leu Ala
100 105 110
Lys Gln Pro Leu His Ser Gln Glu Leu Leu Asp Pro Leu Arg Ala Met
115 120 125
Leu Ala Lys Thr Leu Ala Ala Leu Thr Pro Gly Lys Leu Lys Tyr Ser
130 135 140
Phe Phe Cys Asn Ser Gly Thr Glu Ser Val Glu Ala Ala Leu Lys Leu
145 150 155 160
Ala Lys Ala Tyr Gln Ser Pro Arg Gly Lys Phe Thr Phe Ile Ala Thr
165 170 175
Ser Gly Ala Phe His Gly Lys Ser Leu Gly Ala Leu Ser Ala Thr Ala
180 185 190
Lys Ser Thr Phe Arg Lys Pro Phe Met Pro Leu Leu Pro Gly Phe Arg
195 200 205
His Val Pro Phe Gly Asn Ile Glu Ala Met Arg Thr Ala Leu Asn Glu
210 215 220
Cys Lys Lys Thr Gly Asp Asp Val Ala Ala Val Ile Leu Glu Pro Ile
225 230 235 240
Gln Gly Glu Gly Gly Val Ile Leu Pro Pro Pro Gly Tyr Leu Thr Ala
245 250 255
Val Arg Lys Leu Cys Asp Glu Phe Gly Ala Leu Met Ile Leu Asp Glu
260 265 270
Val Gln Thr Gly Met Gly Arg Thr Gly Lys Met Phe Ala Cys Glu His
275 280 285
Glu Asn Val Gln Pro Asp Ile Leu Cys Leu Ala Lys Ala Leu Gly Gly
290 295 300
Gly Val Met Pro Ile Gly Ala Thr Ile Ala Thr Glu Glu Val Phe Ser
305 310 315 320
Val Leu Phe Asp Asn Pro Phe Leu His Thr Thr Thr Phe Gly Gly Asn
325 330 335
Pro Leu Ala Cys Ala Ala Ala Leu Ala Thr Ile Asn Val Leu Leu Glu
340 345 350
Gln Asn Leu Pro Ala Gln Ala Glu Gln Lys Gly Asp Met Leu Leu Asp
355 360 365
Gly Phe Arg Gln Leu Ala Arg Glu Tyr Pro Asp Leu Val Gln Glu Ala
370 375 380
Arg Gly Lys Gly Met Leu Met Ala Ile Glu Phe Val Asp Asn Glu Ile
385 390 395 400
Gly Tyr Asn Phe Ala Ser Glu Met Phe Arg Gln Arg Val Leu Val Ala
405 410 415
Gly Thr Leu Asn Asn Ala Lys Thr Ile Arg Ile Glu Pro Pro Leu Thr
420 425 430
Leu Thr Ile Glu Gln Cys Glu Leu Val Ile Lys Ala Ala Arg Lys Ala
435 440 445
Leu Ala Ala Met Arg Val Ser Val Glu Glu Ala
450 455
<210> 12
<211> 453
<212> PRT
<213> 河流弧菌
<400> 12
Met Asn Lys Pro Gln Ser Trp Glu Ala Arg Ala Glu Thr Tyr Ser Leu
1 5 10 15
Tyr Gly Phe Thr Asp Met Pro Ser Leu His Gln Arg Gly Thr Val Val
20 25 30
Val Thr His Gly Glu Gly Pro Tyr Ile Val Asp Val Asn Gly Arg Arg
35 40 45
Tyr Leu Asp Ala Asn Ser Gly Leu Trp Asn Met Val Ala Gly Phe Asp
50 55 60
His Lys Gly Leu Ile Asp Ala Ala Lys Ala Gln Tyr Glu Arg Phe Pro
65 70 75 80
Gly Tyr His Ala Phe Phe Gly Arg Met Ser Asp Gln Thr Val Met Leu
85 90 95
Ser Glu Lys Leu Val Glu Val Ser Pro Phe Asp Ser Gly Arg Val Phe
100 105 110
Tyr Thr Asn Ser Gly Ser Glu Ala Asn Asp Thr Met Val Lys Met Leu
115 120 125
Trp Phe Leu His Ala Ala Glu Gly Lys Pro Gln Lys Arg Lys Ile Leu
130 135 140
Thr Arg Trp Asn Ala Tyr His Gly Val Thr Ala Val Ser Ala Ser Met
145 150 155 160
Thr Gly Lys Pro Tyr Asn Ser Val Phe Gly Leu Pro Leu Pro Gly Phe
165 170 175
Val His Leu Thr Cys Pro His Tyr Trp Arg Tyr Gly Glu Glu Gly Glu
180 185 190
Thr Glu Glu Gln Phe Val Ala Arg Leu Ala Arg Glu Leu Glu Glu Thr
195 200 205
Ile Gln Arg Glu Gly Ala Asp Thr Ile Ala Gly Phe Phe Ala Glu Pro
210 215 220
Val Met Gly Ala Gly Gly Val Ile Pro Pro Ala Lys Gly Tyr Phe Gln
225 230 235 240
Ala Ile Leu Pro Ile Leu Arg Lys Tyr Asp Ile Pro Val Ile Ser Asp
245 250 255
Glu Val Ile Cys Gly Phe Gly Arg Thr Gly Asn Thr Trp Gly Cys Val
260 265 270
Thr Tyr Asp Phe Thr Pro Asp Ala Ile Ile Ser Ser Lys Asn Leu Thr
275 280 285
Ala Gly Phe Phe Pro Met Gly Ala Val Ile Leu Gly Pro Glu Leu Ser
290 295 300
Lys Arg Leu Glu Thr Ala Ile Glu Ala Ile Glu Glu Phe Pro His Gly
305 310 315 320
Phe Thr Ala Ser Gly His Pro Val Gly Cys Ala Ile Ala Leu Lys Ala
325 330 335
Ile Asp Val Val Met Asn Glu Gly Leu Ala Glu Asn Val Arg Arg Leu
340 345 350
Ala Pro Arg Phe Glu Glu Arg Leu Lys His Ile Ala Glu Arg Pro Asn
355 360 365
Ile Gly Glu Tyr Arg Gly Ile Gly Phe Met Trp Ala Leu Glu Ala Val
370 375 380
Lys Asp Lys Ala Ser Lys Thr Pro Phe Asp Gly Asn Leu Ser Val Ser
385 390 395 400
Glu Arg Ile Ala Asn Thr Cys Thr Asp Leu Gly Leu Ile Cys Arg Pro
405 410 415
Leu Gly Gln Ser Val Val Leu Cys Pro Pro Phe Ile Leu Thr Glu Ala
420 425 430
Gln Met Asp Glu Met Phe Asp Lys Leu Glu Lys Ala Leu Asp Lys Val
435 440 445
Phe Ala Glu Val Ala
450
<210> 13
<211> 401
<212> PRT
<213> 大肠杆菌
<400> 13
Met Arg Glu Ala Phe Ile Cys Asp Gly Ile Arg Thr Pro Ile Gly Arg
1 5 10 15
Tyr Gly Gly Ala Leu Ser Ser Val Arg Ala Asp Asp Leu Ala Ala Ile
20 25 30
Pro Leu Arg Glu Leu Leu Val Arg Asn Pro Arg Leu Asp Ala Glu Cys
35 40 45
Ile Asp Asp Val Ile Leu Gly Cys Ala Asn Gln Ala Gly Glu Asp Asn
50 55 60
Arg Asn Val Ala Arg Met Ala Thr Leu Leu Ala Gly Leu Pro Gln Ser
65 70 75 80
Val Ser Gly Thr Thr Ile Asn Arg Leu Cys Gly Ser Gly Leu Asp Ala
85 90 95
Leu Gly Phe Ala Ala Arg Ala Ile Lys Ala Gly Asp Gly Asp Leu Leu
100 105 110
Ile Ala Gly Gly Val Glu Ser Met Ser Arg Ala Pro Phe Val Met Gly
115 120 125
Lys Ala Ala Ser Ala Phe Ser Arg Gln Ala Glu Met Phe Asp Thr Thr
130 135 140
Ile Gly Trp Arg Phe Val Asn Pro Leu Met Ala Gln Gln Phe Gly Thr
145 150 155 160
Asp Ser Met Pro Glu Thr Ala Glu Asn Val Ala Glu Leu Leu Lys Ile
165 170 175
Ser Arg Glu Asp Gln Asp Ser Phe Ala Leu Arg Ser Gln Gln Arg Thr
180 185 190
Ala Lys Ala Gln Ser Ser Gly Ile Leu Ala Glu Glu Ile Val Pro Val
195 200 205
Val Leu Lys Asn Lys Lys Gly Val Val Thr Glu Ile Gln His Asp Glu
210 215 220
His Leu Arg Pro Glu Thr Thr Leu Glu Gln Leu Arg Gly Leu Lys Ala
225 230 235 240
Pro Phe Arg Ala Asn Gly Val Ile Thr Ala Gly Asn Ala Ser Gly Val
245 250 255
Asn Asp Gly Ala Ala Ala Leu Ile Ile Ala Ser Glu Gln Met Ala Ala
260 265 270
Ala Gln Gly Leu Thr Pro Arg Ala Arg Ile Val Ala Met Ala Thr Ala
275 280 285
Gly Val Glu Pro Arg Leu Met Gly Leu Gly Pro Val Pro Ala Thr Arg
290 295 300
Arg Val Leu Glu Arg Ala Gly Leu Ser Ile His Asp Met Asp Val Ile
305 310 315 320
Glu Leu Asn Glu Ala Phe Ala Ala Gln Ala Leu Gly Val Leu Arg Glu
325 330 335
Leu Gly Leu Pro Asp Asp Ala Pro His Val Asn Pro Asn Gly Gly Ala
340 345 350
Ile Ala Leu Gly His Pro Leu Gly Met Ser Gly Ala Arg Leu Ala Leu
355 360 365
Ala Ala Ser His Glu Leu His Arg Arg Asn Gly Arg Tyr Ala Leu Cys
370 375 380
Thr Met Cys Ile Gly Val Gly Gln Gly Ile Ala Met Ile Leu Glu Arg
385 390 395 400
Val
<210> 14
<211> 438
<212> PRT
<213> 氨基丁酸羧菌
<400> 14
Met Asp Trp Lys Lys Ile Tyr Glu Asp Arg Thr Cys Thr Ala Asp Glu
1 5 10 15
Ala Val Lys Ser Ile Lys Ser Gly Asp Arg Val Leu Phe Ala His Cys
20 25 30
Val Ala Glu Pro Pro Val Leu Val Glu Ala Met Val Ala Asn Ala Ala
35 40 45
Ala Tyr Lys Asn Val Thr Val Ser His Met Val Thr Leu Gly Lys Gly
50 55 60
Glu Tyr Ser Lys Pro Glu Tyr Lys Glu Asn Phe Thr Phe Glu Gly Trp
65 70 75 80
Phe Thr Ser Pro Ser Thr Arg Gly Ser Ile Ala Glu Gly His Gly Gln
85 90 95
Phe Val Pro Val Phe Phe His Glu Val Pro Ser Leu Ile Arg Lys Asp
100 105 110
Ile Phe His Val Asp Val Phe Met Val Met Val Ser Pro Pro Asp His
115 120 125
Asn Gly Phe Cys Cys Val Gly Val Ser Ser Asp Tyr Thr Met Gln Ala
130 135 140
Ile Lys Ser Ala Lys Ile Val Leu Ala Glu Val Asn Asp Gln Val Pro
145 150 155 160
Val Val Tyr Gly Asp Thr Phe Val His Val Ser Glu Ile Asp Lys Phe
165 170 175
Val Glu Thr Ser His Pro Leu Pro Glu Ile Gly Leu Pro Lys Ile Gly
180 185 190
Glu Val Glu Ala Ala Ile Gly Lys His Cys Ala Ser Leu Ile Glu Asp
195 200 205
Gly Ser Thr Leu Gln Leu Gly Ile Gly Ala Ile Pro Asp Ala Val Leu
210 215 220
Ser Gln Leu Lys Asp Lys Lys His Leu Gly Ile His Ser Glu Met Ile
225 230 235 240
Ser Asp Gly Val Val Asp Leu Tyr Glu Ala Gly Val Ile Asp Cys Ser
245 250 255
Gln Lys Ser Ile Asp Lys Gly Lys Met Ala Ile Thr Phe Leu Met Gly
260 265 270
Thr Lys Arg Leu Tyr Asp Phe Ala Ala Asn Asn Pro Lys Val Glu Leu
275 280 285
Lys Pro Val Asp Tyr Ile Asn His Pro Ser Val Val Ala Gln Cys Ser
290 295 300
Lys Met Val Cys Ile Asn Ala Cys Leu Gln Val Asp Phe Met Gly Gln
305 310 315 320
Ile Val Ser Asp Ser Ile Gly Thr Lys Gln Phe Ser Gly Val Gly Gly
325 330 335
Gln Val Asp Phe Val Arg Gly Ala Ser Met Ser Ile Asp Gly Lys Gly
340 345 350
Lys Ala Ile Ile Ala Met Pro Ser Val Ala Lys Lys Lys Asp Gly Ser
355 360 365
Met Ile Ser Lys Ile Val Pro Phe Ile Asp His Gly Ala Ala Val Thr
370 375 380
Thr Ser Arg Asn Asp Ala Asp Tyr Val Val Thr Glu Tyr Gly Ile Ala
385 390 395 400
Glu Met Lys Gly Lys Ser Leu Gln Asp Arg Ala Arg Ala Leu Ile Asn
405 410 415
Ile Ala His Pro Asp Phe Lys Asp Glu Leu Lys Ala Glu Phe Glu Lys
420 425 430
Arg Phe Asn Ala Ala Phe
435
<210> 15
<211> 397
<212> PRT
<213> 齿垢密螺旋体
<400> 15
Met Ile Val Lys Pro Met Val Arg Asn Asn Ile Cys Leu Asn Ala His
1 5 10 15
Pro Gln Gly Cys Lys Lys Gly Val Glu Asp Gln Ile Glu Tyr Thr Lys
20 25 30
Lys Arg Ile Thr Ala Glu Val Lys Ala Gly Ala Lys Ala Pro Lys Asn
35 40 45
Val Leu Val Leu Gly Cys Ser Asn Gly Tyr Gly Leu Ala Ser Arg Ile
50 55 60
Thr Ala Ala Phe Gly Tyr Gly Ala Ala Thr Ile Gly Val Ser Phe Glu
65 70 75 80
Lys Ala Gly Ser Glu Thr Lys Tyr Gly Thr Pro Gly Trp Tyr Asn Asn
85 90 95
Leu Ala Phe Asp Glu Ala Ala Lys Arg Glu Gly Leu Tyr Ser Val Thr
100 105 110
Ile Asp Gly Asp Ala Phe Ser Asp Glu Ile Lys Ala Gln Val Ile Glu
115 120 125
Glu Ala Lys Lys Lys Gly Ile Lys Phe Asp Leu Ile Val Tyr Ser Leu
130 135 140
Ala Ser Pro Val Arg Thr Asp Pro Asp Thr Gly Ile Met His Lys Ser
145 150 155 160
Val Leu Lys Pro Phe Gly Lys Thr Phe Thr Gly Lys Thr Val Asp Pro
165 170 175
Phe Thr Gly Glu Leu Lys Glu Ile Ser Ala Glu Pro Ala Asn Asp Glu
180 185 190
Glu Ala Ala Ala Thr Val Lys Val Met Gly Gly Glu Asp Trp Glu Arg
195 200 205
Trp Ile Lys Gln Leu Ser Lys Glu Gly Leu Leu Glu Glu Gly Cys Ile
210 215 220
Thr Leu Ala Tyr Ser Tyr Ile Gly Pro Glu Ala Thr Gln Ala Leu Tyr
225 230 235 240
Arg Lys Gly Thr Ile Gly Lys Ala Lys Glu His Leu Glu Ala Thr Ala
245 250 255
His Arg Leu Asn Lys Glu Asn Pro Ser Ile Arg Ala Phe Val Ser Val
260 265 270
Asn Lys Gly Leu Val Thr Arg Ala Ser Ala Val Ile Pro Val Ile Pro
275 280 285
Leu Tyr Leu Ala Ser Leu Phe Lys Val Met Lys Glu Lys Gly Asn His
290 295 300
Glu Gly Cys Ile Glu Gln Ile Thr Arg Leu Tyr Ala Glu Arg Leu Tyr
305 310 315 320
Arg Lys Asp Gly Thr Ile Pro Val Asp Glu Glu Asn Arg Ile Arg Ile
325 330 335
Asp Asp Trp Glu Leu Glu Glu Asp Val Gln Lys Ala Val Ser Ala Leu
340 345 350
Met Glu Lys Val Thr Gly Glu Asn Ala Glu Ser Leu Thr Asp Leu Ala
355 360 365
Gly Tyr Arg His Asp Phe Leu Ala Ser Asn Gly Phe Asp Val Glu Gly
370 375 380
Ile Asn Tyr Glu Ala Glu Val Glu Arg Phe Asp Arg Ile
385 390 395
<210> 16
<211> 539
<212> PRT
<213> Euglena gracilis
<400> 16
Met Ser Cys Pro Ala Ser Pro Ser Ala Ala Val Val Ser Ala Gly Ala
1 5 10 15
Leu Cys Leu Cys Val Ala Thr Val Leu Leu Ala Thr Gly Ser Asn Pro
20 25 30
Thr Ala Leu Ser Thr Ala Ser Thr Arg Ser Pro Thr Ser Leu Val Arg
35 40 45
Gly Val Asp Arg Gly Leu Met Arg Pro Thr Thr Ala Ala Ala Leu Thr
50 55 60
Thr Met Arg Glu Val Pro Gln Met Ala Glu Gly Phe Ser Gly Glu Ala
65 70 75 80
Thr Ser Ala Trp Ala Ala Ala Gly Pro Gln Trp Ala Ala Pro Leu Val
85 90 95
Ala Ala Ala Ser Ser Ala Leu Ala Leu Trp Trp Trp Ala Ala Arg Arg
100 105 110
Ser Val Arg Arg Pro Leu Ala Ala Leu Ala Glu Leu Pro Thr Ala Val
115 120 125
Thr His Leu Ala Pro Pro Met Ala Met Phe Thr Thr Thr Ala Lys Val
130 135 140
Ile Gln Pro Lys Ile Arg Gly Phe Ile Cys Thr Thr Thr His Pro Ile
145 150 155 160
Gly Cys Glu Lys Arg Val Gln Glu Glu Ile Ala Tyr Ala Arg Ala His
165 170 175
Pro Pro Thr Ser Pro Gly Pro Lys Arg Val Leu Val Ile Gly Cys Ser
180 185 190
Thr Gly Tyr Gly Leu Ser Thr Arg Ile Thr Ala Ala Phe Gly Tyr Gln
195 200 205
Ala Ala Thr Leu Gly Val Phe Leu Ala Gly Pro Pro Thr Lys Gly Arg
210 215 220
Pro Ala Ala Ala Gly Trp Tyr Asn Thr Val Ala Phe Glu Lys Ala Ala
225 230 235 240
Leu Glu Ala Gly Leu Tyr Ala Arg Ser Leu Asn Gly Asp Ala Phe Asp
245 250 255
Ser Thr Thr Lys Ala Arg Thr Val Glu Ala Ile Lys Arg Asp Leu Gly
260 265 270
Thr Val Asp Leu Val Val Tyr Ser Ile Ala Ala Pro Lys Arg Thr Asp
275 280 285
Pro Ala Thr Gly Val Leu His Lys Ala Cys Leu Lys Pro Ile Gly Ala
290 295 300
Thr Tyr Thr Asn Arg Thr Val Asn Thr Asp Lys Ala Glu Val Thr Asp
305 310 315 320
Val Ser Ile Glu Pro Ala Ser Pro Glu Glu Ile Ala Asp Thr Val Lys
325 330 335
Val Met Gly Gly Glu Asp Trp Glu Leu Trp Ile Gln Ala Leu Ser Glu
340 345 350
Ala Gly Val Leu Ala Glu Gly Ala Lys Thr Val Ala Tyr Ser Tyr Ile
355 360 365
Gly Pro Glu Met Thr Trp Pro Val Tyr Trp Ser Gly Thr Ile Gly Glu
370 375 380
Ala Lys Lys Asp Val Glu Lys Ala Ala Lys Arg Ile Thr Gln Gln Tyr
385 390 395 400
Gly Cys Pro Ala Tyr Pro Val Val Ala Lys Ala Leu Val Thr Gln Ala
405 410 415
Ser Ser Ala Ile Pro Val Val Pro Leu Tyr Ile Cys Leu Leu Tyr Arg
420 425 430
Val Met Lys Glu Lys Gly Thr His Glu Gly Cys Ile Glu Gln Met Val
435 440 445
Arg Leu Leu Thr Thr Lys Leu Tyr Pro Glu Asn Gly Ala Pro Ile Val
450 455 460
Asp Glu Ala Gly Arg Val Arg Val Asp Asp Trp Glu Met Ala Glu Asp
465 470 475 480
Val Gln Gln Ala Val Lys Asp Leu Trp Ser Gln Val Ser Thr Ala Asn
485 490 495
Leu Lys Asp Ile Ser Asp Phe Ala Gly Tyr Gln Thr Glu Phe Leu Arg
500 505 510
Leu Phe Gly Phe Gly Ile Asp Gly Val Asp Tyr Asp Gln Pro Val Asp
515 520 525
Val Glu Ala Asp Leu Pro Ser Ala Ala Gln Gln
530 535
<210> 17
<211> 550
<212> PRT
<213> 鼠伤寒沙门氏菌
<400> 17
Met Gln Asn Pro Tyr Thr Val Ala Asp Tyr Leu Leu Asp Arg Leu Ala
1 5 10 15
Gly Cys Gly Ile Gly His Leu Phe Gly Val Pro Gly Asp Tyr Asn Leu
20 25 30
Gln Phe Leu Asp His Val Ile Asp His Pro Thr Leu Arg Trp Val Gly
35 40 45
Cys Ala Asn Glu Leu Asn Ala Ala Tyr Ala Ala Asp Gly Tyr Ala Arg
50 55 60
Met Ser Gly Ala Gly Ala Leu Leu Thr Thr Phe Gly Val Gly Glu Leu
65 70 75 80
Ser Ala Ile Asn Gly Ile Ala Gly Ser Tyr Ala Glu Tyr Val Pro Val
85 90 95
Leu His Ile Val Gly Ala Pro Cys Ser Ala Ala Gln Gln Arg Gly Glu
100 105 110
Leu Met His His Thr Leu Gly Asp Gly Asp Phe Arg His Phe Tyr Arg
115 120 125
Met Ser Gln Ala Ile Ser Ala Ala Ser Ala Ile Leu Asp Glu Gln Asn
130 135 140
Ala Cys Phe Glu Ile Asp Arg Val Leu Gly Glu Met Leu Ala Ala Arg
145 150 155 160
Arg Pro Gly Tyr Ile Met Leu Pro Ala Asp Val Ala Lys Lys Thr Ala
165 170 175
Ile Pro Pro Thr Gln Ala Leu Ala Leu Pro Val His Glu Ala Gln Ser
180 185 190
Gly Val Glu Thr Ala Phe Arg Tyr His Ala Arg Gln Cys Leu Met Asn
195 200 205
Ser Arg Arg Ile Ala Leu Leu Ala Asp Phe Leu Ala Gly Arg Phe Gly
210 215 220
Leu Arg Pro Leu Leu Gln Arg Trp Met Ala Glu Thr Pro Ile Ala His
225 230 235 240
Ala Thr Leu Leu Met Gly Lys Gly Leu Phe Asp Glu Gln His Pro Asn
245 250 255
Phe Val Gly Thr Tyr Ser Ala Gly Ala Ser Ser Lys Glu Val Arg Gln
260 265 270
Ala Ile Glu Asp Ala Asp Arg Val Ile Cys Val Gly Thr Arg Phe Val
275 280 285
Asp Thr Leu Thr Ala Gly Phe Thr Gln Gln Leu Pro Ala Glu Arg Thr
290 295 300
Leu Glu Ile Gln Pro Tyr Ala Ser Arg Ile Gly Glu Thr Trp Phe Asn
305 310 315 320
Leu Pro Met Ala Gln Ala Val Ser Thr Leu Arg Glu Leu Cys Leu Glu
325 330 335
Cys Ala Phe Ala Pro Pro Pro Thr Arg Ser Ala Gly Gln Pro Val Arg
340 345 350
Ile Asp Lys Gly Glu Leu Thr Gln Glu Ser Phe Trp Gln Thr Leu Gln
355 360 365
Gln Tyr Leu Lys Pro Gly Asp Ile Ile Leu Val Asp Gln Gly Thr Ala
370 375 380
Ala Phe Gly Ala Ala Ala Leu Ser Leu Pro Asp Gly Ala Glu Val Val
385 390 395 400
Leu Gln Pro Leu Trp Gly Ser Ile Gly Tyr Ser Leu Pro Ala Ala Phe
405 410 415
Gly Ala Gln Thr Ala Cys Pro Asp Arg Arg Val Ile Leu Ile Ile Gly
420 425 430
Asp Gly Ala Ala Gln Leu Thr Ile Gln Glu Met Gly Ser Met Leu Arg
435 440 445
Asp Gly Gln Ala Pro Val Ile Leu Leu Leu Asn Asn Asp Gly Tyr Thr
450 455 460
Val Glu Arg Ala Ile His Gly Ala Ala Gln Arg Tyr Asn Asp Ile Ala
465 470 475 480
Ser Trp Asn Trp Thr Gln Ile Pro Pro Ala Leu Asn Ala Ala Gln Gln
485 490 495
Ala Glu Cys Trp Arg Val Thr Gln Ala Ile Gln Leu Ala Glu Val Leu
500 505 510
Glu Arg Leu Ala Arg Pro Gln Arg Leu Ser Phe Ile Glu Val Met Leu
515 520 525
Pro Lys Ala Asp Leu Pro Glu Leu Leu Arg Thr Val Thr Arg Ala Leu
530 535 540
Glu Ala Arg Asn Gly Gly
545 550
Claims (49)
1.生产3-氧代-6-羟基己酰基CoA或其盐的方法,所述方法包括使用归类于EC.2.3.1.-下的具有β-酮硫解酶活性的多肽将4-羟基丁酰基CoA酶促转化为3-氧代-6-羟基己酰基CoA。
2.权利要求1的方法,其中所述具有β-酮硫解酶活性的多肽归类于EC 2.3.1.16下。
3.权利要求1的方法,其中所述具有β-酮硫解酶活性的多肽归类于EC 2.3.1.174下。
4.权利要求1-3中任一项的方法,其中所述具有β-酮硫解酶活性的多肽与SEQ ID NO:1、13或14所列的氨基酸序列具有至少70%序列同一性。
5.权利要求1-4中任一项的方法,其还包含使用3-羟基酰基CoA脱氢酶或3-酮酰基CoA还原酶、烯酰CoA水合酶、反式-2-烯酰CoA还原酶,和硫酯酶或CoA转移酶将3-氧代-6-羟基己酰基CoA酶促转化为6-羟基己酸。
6.权利要求5的方法,其中所述3-羟基酰基CoA脱氢酶或所述3-酮酰基CoA还原酶归类于EC 1.1.1.35、EC 1.1.1.36、EC 1.1.1.100,或EC 1.1.1.157下。
7.权利要求5或权利要求6的方法,其中所述烯酰CoA水合酶归类于EC 4.2.1.17或EC4.2.1.119下。
8.权利要求5-7中任一项的方法,其中所述反式-2-烯酰CoA还原酶归类于EC1.3.1.38、EC 1.3.1.44,或EC 1.3.1.8下。
9.生物合成6-羟基己酸的方法,所述方法包括使用归类于EC.2.3.1.-下的具有β-酮硫解酶活性的多肽从4-羟基丁酰基CoA酶促合成3-氧代-6-羟基己酰基CoA,和将3-氧代-6-羟基己酰基CoA酶促转化为6-羟基己酸。
10.权利要求9的方法,其中使用3-羟基酰基CoA脱氢酶或3-酮酰基CoA还原酶将3-氧代-6-羟基己酰基CoA转化为3-羟基-6-羟基己酰基CoA,使用烯酰CoA水合酶将3-羟基-6-羟基己酰基CoA转化为2,3-脱氢-6-羟基己酰基CoA,使用反式-2-烯酰CoA还原酶将2,3-脱氢-6-羟基己酰基CoA转化为6-羟基己酰基CoA,以及使用硫酯酶或CoA转移酶将6-羟基己酰基CoA转化为6-羟基己酸。
11.权利要求5-10中任一项的方法,所述方法还包括在一个步骤或多个步骤中将6-羟基己酸酶促转化为己二酸、6-氨基己酸、己内酰胺、六亚甲基二胺,或1,6-己二醇。
12.权利要求11的方法,其中使用以下的一种或多种酶将6-羟基己酸转化为己二酸:单加氧酶、醇脱氢酶、4-羟基丁酸脱氢酶、5-羟基戊酸脱氢酶、6-羟基己酸脱氢酶、7-氧代庚酸脱氢酶、6-氧代己酸脱氢酶、5-氧代戊酸脱氢酶,或醛脱氢酶。
13.权利要求11的方法,其中使用以下的一种或多种酶将6-羟基己酸转化为6-氨基己酸:醇脱氢酶、6-羟基己酸脱氢酶、5-羟基戊酸脱氢酶、4-羟基丁酸脱氢酶,和ω-转氨酶。
14.权利要求11的方法,其中使用以下的一种或多种酶将6-羟基己酸转化为己内酰胺:醇脱氢酶、6-羟基己酸脱氢酶、5-羟基戊酸脱氢酶、4-羟基丁酸脱氢酶、ω-转氨酶,和酰胺水解酶(amidohydrolase)。
15.权利要求11的方法,其中使用以下的一种或多种酶将6-羟基己酸转化为六亚甲基二胺:ω-转氨酶、醇脱氢酶、N-乙酰基转移酶,和乙酰腐胺脱酰基酶(acetylputrescinedeacylase)。
16.权利要求13、权利要求14,或权利要求15的方法,其中所述ω-转氨酶与SEQ ID NO:7-12中所列的任一个氨基酸序列具有至少70%序列同一性。
17.权利要求11的方法,其中使用羧酸还原酶和醇脱氢酶将6-羟基己酸转化为1,6-己二醇。
18.权利要求15-17中任一项的方法,其中所述羧酸还原酶与SEQ ID NO:2-6中所列的任一个氨基酸序列具有至少70%序列同一性。
19.权利要求1-18中任一项的方法,其中从2-酮戊二酸酶促生产所述4-羟基丁酰基CoA。
20.权利要求19的方法,其中使用以下的一种或多种酶从2-酮戊二酸酶促生产4-羟基丁酰基CoA:谷氨酸合酶;2-酮戊二酸脱羧酶;支链脱羧酶;谷氨酸脱羧酶;ω-转氨酶;CoA转移酶;CoA连接酶,和醇脱氢酶。
21.前述权利要求中任一项的方法,其中所述方法在重组宿主中进行。
22.权利要求21的方法,其中所述宿主经受在需氧、厌氧,或微需氧培养条件下的培养策略。
23.权利要求21或权利要求22的方法,其中在营养限制的条件下培养所述宿主。
24.根据权利要求21-23中任一项的方法,其中使用陶瓷膜保留所述宿主以在发酵期间维持高细胞密度。
25.权利要求21-24中任一项的方法,其中补料到发酵的主要碳源源自生物原料。
26.权利要求25的方法,其中所述生物原料是或源自单糖、二糖、木质纤维素、半纤维素、纤维素、木质素、乙酰丙酸、甲酸、甘油三酯、甘油、脂肪酸、农业废物、浓缩的酒糟可溶物(condensed distillers'solubles),或城市废物。
27.权利要求21-24中任一项的方法,其中补料到发酵的主要碳源源自非生物原料。
28.权利要求27的方法,其中所述非生物原料是或源自天然气、合成气、CO2/H2、甲醇、乙醇、苯甲酸盐/酯、非挥发性残留物(NVR),来自环己烷氧化过程的碱洗液(caustic wash)废物流,或对苯二甲酸/间苯二甲酸混合物废物流。
29.权利要求21-28中任一项的方法,其中所述宿主是原核生物。
30.权利要求29的方法,其中所述原核生物选自下组:埃希氏菌属(Escherichia);梭菌属(Clostridia);棒状杆菌属(Corynebacteria);贪铜菌属(Cupriavidus);假单胞菌属(Pseudomonas);代尔夫特菌属(Delftia);芽孢杆菌属(Bacillus);乳杆菌属(Lactobacillus);乳球菌属(Lactococcus);和红球菌属(Rhodococcus)。
31.权利要求30的方法,其中所述原核生物选自下组:大肠杆菌(Escherichia coli)、杨氏梭菌(Clostridium ljungdahlii)、自产乙醇梭菌(Clostridium autoethanogenum)、克鲁佛梭菌(Clostridium kluyveri)、谷氨酸棒状杆菌(Corynebacterium glutamicum)、钩虫贪铜菌(Cupriavidus necator)、耐金属贪铜菌(Cupriavidus metallidurans)、荧光假单胞菌(Pseudomonas fluorescens)、恶臭假单胞菌(Pseudomonas putida)、食油假单胞菌(Pseudomonas oleavorans)、食酸代尔夫特菌(Delftia acidovorans)、枯草芽胞杆菌(Bacillus subtillis)、德氏乳杆菌(Lactobacillus delbrueckii)、乳酸乳球菌(Lactococcus lactis),和马红球菌(Rhodococcus equi)。
32.权利要求21-28中任一项的方法,其中所述宿主是真核生物。
33.权利要求32的方法,其中所述真核生物选自下组:曲霉属(Aspergillus)、酵母属(Saccharomyces)、毕赤氏酵属(Pichia)、耶罗维亚酵母属(Yarrowia)、伊萨酵母属(Issatchenkia)、德巴利酵母属(Debaryomyces)、Arxula属,和克鲁维酵母菌属(Kluyveromyces)。
34.权利要求33的方法,其中所述真核生物选自下组:黑曲霉(Aspergillus niger)、酿酒酵母(Saccharomyces cerevisiae)、巴斯德毕赤酵母(Pichia pastoris)、解脂耶罗维亚酵母(Yarrowia lipolytica)、东方伊萨酵母(Issathenkia orientalis)、汉逊德巴利酵母(Debaryomyces hansenii)、Arxula adenoinivorans,和乳酸克鲁维酵母(Kluyveromyceslactis)。
35.权利要求21的方法,其中通过在选择的环境中连续培养改善所述宿主对高浓度的C6构件块的耐受性。
36.权利要求21-35中任一项的方法,其中所述宿主包含对一种或多种下述酶的弱化:聚羟基烷酸酯(polyhydroxyalkanoate)合酶、乙酰CoA硫酯酶、形成乙酸的磷酸转乙酰酶、乙酸激酶、乳酸脱氢酶、menaquinol-富马酸氧化还原酶、形成乙醇的醇脱氢酶、丙糖磷酸异构酶、丙酮酸脱羧酶、葡萄糖-6-磷酸异构酶、消耗NADH的转氢酶、NADH特异性谷氨酸脱氢酶,利用NADH/NADPH的谷氨酸脱氢酶、庚二酰CoA脱氢酶;接受C6构建块和中心前体作为底物的酰基CoA脱氢酶;丁酰基CoA脱氢酶;或己二酰CoA合成酶。
37.权利要求21-36中任一项的方法,其中所述宿主过表达编码以下酶的一种或多种基因:乙酰CoA合成酶、6-磷酸葡萄糖酸脱氢酶;转酮醇酶;嘌呤核苷酸转氢酶;甘油醛-3P-脱氢酶;苹果酸酶;葡萄糖-6-磷酸脱氢酶;葡萄糖脱氢酶;果糖1,6二磷酸酶;L-丙氨酸脱氢酶;L-谷氨酸脱氢酶;甲酸脱氢酶;L-谷氨酰胺合成酶;二胺转运蛋白;二羧酸转运蛋白;和/或多药转运蛋白。
38.重组宿主,其包含至少一种编码以下酶的外源核酸(i)β-酮硫解酶,(ii)硫酯酶或CoA转移酶,以及(iii)3-羟基酰基CoA脱氢酶或3-酮酰基CoA还原酶,(iv)烯酰CoA水合酶,和(v)反式-2-烯酰CoA还原酶的一种或多种,所述宿主生产6-羟基己酸。
39.权利要求38的重组宿主,所述宿主还包含以下外源酶的一种或多种:单加氧酶、醇脱氢酶、4-羟基丁酸脱氢酶、5-羟基戊酸脱氢酶、6-羟基己酸脱氢酶、7-氧代庚酸脱氢酶、6-氧代己酸脱氢酶、5-氧代戊酸脱氢酶,或者醛脱氢酶,所述宿主进一步生产己二酸。
40.权利要求38的重组宿主,所述宿主还包含以下外源酶一种或多种:单加氧酶、转氨酶、6-羟基己酸脱氢酶、5-羟基戊酸脱氢酶、4-羟基丁酸脱氢酶,和醇脱氢酶,所述宿主进一步生产6-氨基己酸。
41.权利要求40的重组宿主,所述宿主还包含外源酰胺水解酶,所述宿主进一步生产己内酰胺。
42.权利要求38的重塑宿主,所述宿主还包含以下外源酶一种或多种:羧酸还原酶、ω-转氨酶、脱酰基酶、N-乙酰基转移酶,或醇脱氢酶,所述宿主进一步生产六亚甲基二胺。
43.权利要求38的重组宿主,所述宿主还包含外源羧酸还原酶和外源醇脱氢酶,所述宿主进一步生产1,6-己二醇。
44.权利要求38-43中任一项的重组宿主,所述宿主还包含以下外源酶一种或多种:谷氨酸合成酶;2-酮戊二酸脱羧酶;支链脱羧酶;谷氨酸脱羧酶;ω-转氨酶;CoA连接酶;CoA转移酶,和醇脱氢酶。
45.生物衍生的产品,生物基的产品或发酵衍生的产品,其中所述产品包含:
i.组合物,所述组合物包含至少一种根据权利要求1-44中任一项,或图1-5中任一项的生物衍生的、生物基或发酵衍生的化合物,或其任何组合,
ii.生物衍生的、生物基或发酵衍生的聚合物,其包含i.的生物衍生的、生物基的或发酵衍生的组合物或化合物,或其任何组合,
iii.生物衍生的、生物基或发酵衍生的树脂,其包含i.的生物衍生的、生物基的或发酵衍生的化合物或生物衍生的、生物基的或发酵衍生的组合物或其任何组合,或者ii.的生物衍生的、生物基的或发酵衍生的聚合物或其任何组合,
iv.模制物质,其通过使ii.的生物衍生的、生物基的或发酵衍生的聚合物或iii.的生物衍生的、生物基的或发酵衍生的树脂或其任何组合模制获得,
v.生物衍生的、生物基的或发酵衍生的配制剂,其包含i.的生物衍生的、生物基的或发酵衍生的组合物,i.的生物衍生的、生物基的或发酵衍生的化合物,ii.的生物衍生的、生物基的或发酵衍生的聚合物,iii.生物衍生的、生物基的或发酵衍生的树脂,或iv.的生物衍生的、生物基的或发酵衍生的模制物质,或其任何组合,或
vi.生物衍生的、生物基的或发酵衍生的半固体或非半固体流,其包含i.的生物衍生的、生物基的或发酵衍生的组合物,i.的生物衍生的、生物基的或发酵衍生的化合物,ii.的生物衍生的、生物基的或发酵衍生的聚合物,iii.的生物衍生的、生物基的或发酵衍生的树脂,v.的生物衍生的、生物基的或发酵衍生的配制剂,或iv.的生物衍生的、生物基的或发酵衍生的模制物质,或其任何组合。
46.非天然存在的生物体,其包含至少一种外源核酸,所述外源核酸编码至少一种多肽,所述多肽具有图1至5之一中描绘的至少一种酶活性。
47.非天然存在的生物化学网络,其包含4-羟基丁酰基CoA、编码归类于EC.2.3.1下的具有β-酮硫解酶活性的多肽的外源核酸,和3-氧代-6-羟基己酰基CoA。
48.核酸构建体或表达载体,其包含
(a)编码具有β-酮硫解酶活性的多肽的多核苷酸,其中所述多核苷酸可操作地连接于一种或多种指导所述多肽生产的异源控制序列,并且其中所述具有β-酮硫解酶活性的多肽选自下组:(a)与SEQ ID NOs:1、13或14的多肽具有至少70%序列同一性的多肽;
(b)编码具有ω-转氨酶活性的多肽的多核苷酸,其中所述多核苷酸可操作地连接于一种或多种指导多肽生产的异源控制序列,并且其中所述具有ω-转氨酶活性的多肽选自下组:(a)与SEQ ID NOs:7-12的多肽具有至少70%序列同一性的多肽;
(c)编码具有羧酸还原酶活性的多肽的多核苷酸,其中所述多核苷酸可操作地连接于一种或多种指导多肽生产的异源控制序列,并且其中所述具有羧酸还原酶活性的多肽选自下组:(a)与SEQ ID NOs:2-6的多肽具有至少70%序列同一性的多肽;或者
(d)编码具有以下酶活性的多肽的多核苷酸:3-羟基酰基CoA脱氢酶、3-酮酰基CoA还原酶、烯酰CoA水合酶、反式-2-烯酰CoA还原酶、硫酯酶CoA转移酶、单加氧酶、醇脱氢酶、4-羟基丁酸脱氢酶、5-羟基戊酸脱氢酶、6-羟基己酸脱氢酶、7-氧代庚酸脱氢酶、6-氧代己酸脱氢酶、5-氧代戊酸脱氢酶、醛脱氢酶、6-羟基己酸脱氢酶、5-羟基戊酸脱氢酶、ω-转氨酶、酰胺水解酶、谷氨酸合酶、2-酮戊二酸脱羧酶、支链脱羧酶、谷氨酸脱羧酶、ω-转氨酶、CoA转移酶、CoA连接酶。
49.组合物,其包含权利要求48的核酸构建体或表达载体。
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