EA010179B1 - Биохимический синтез 1,4-бутандиамина - Google Patents
Биохимический синтез 1,4-бутандиамина Download PDFInfo
- Publication number
- EA010179B1 EA010179B1 EA200700329A EA200700329A EA010179B1 EA 010179 B1 EA010179 B1 EA 010179B1 EA 200700329 A EA200700329 A EA 200700329A EA 200700329 A EA200700329 A EA 200700329A EA 010179 B1 EA010179 B1 EA 010179B1
- Authority
- EA
- Eurasian Patent Office
- Prior art keywords
- gene
- activity
- gene encoding
- increased
- acetylglutamate
- Prior art date
Links
- 230000015572 biosynthetic process Effects 0.000 title claims abstract description 68
- 238000003786 synthesis reaction Methods 0.000 title claims abstract description 20
- KIDHWZJUCRJVML-UHFFFAOYSA-N putrescine Chemical compound NCCCCN KIDHWZJUCRJVML-UHFFFAOYSA-N 0.000 claims abstract description 113
- 230000000694 effects Effects 0.000 claims abstract description 79
- 108700005126 Ornithine decarboxylases Proteins 0.000 claims abstract description 70
- 238000000034 method Methods 0.000 claims abstract description 69
- 102000052812 Ornithine decarboxylases Human genes 0.000 claims abstract description 68
- 230000001965 increasing effect Effects 0.000 claims abstract description 58
- 239000013612 plasmid Substances 0.000 claims abstract description 48
- 244000005700 microbiome Species 0.000 claims abstract description 28
- 238000000855 fermentation Methods 0.000 claims abstract description 15
- 230000004151 fermentation Effects 0.000 claims abstract description 15
- 239000013598 vector Substances 0.000 claims abstract description 11
- 108090000623 proteins and genes Proteins 0.000 claims description 106
- 102000004190 Enzymes Human genes 0.000 claims description 43
- 108090000790 Enzymes Proteins 0.000 claims description 43
- -1 β-acetylglutamate Chemical compound 0.000 claims description 26
- 102000011229 agmatinase Human genes 0.000 claims description 24
- 101000652415 Homo sapiens Agmatinase, mitochondrial Proteins 0.000 claims description 22
- 101000711499 Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) N(1)-aminopropylagmatine ureohydrolase Proteins 0.000 claims description 22
- 230000002018 overexpression Effects 0.000 claims description 20
- 102100032252 Antizyme inhibitor 2 Human genes 0.000 claims description 17
- 101000798222 Homo sapiens Antizyme inhibitor 2 Proteins 0.000 claims description 15
- 108700024157 Agmatine deiminases Proteins 0.000 claims description 14
- 241000894007 species Species 0.000 claims description 14
- 230000002255 enzymatic effect Effects 0.000 claims description 12
- 241001103870 Adia Species 0.000 claims description 10
- 239000004475 Arginine Substances 0.000 claims description 8
- 101150092493 CREA gene Proteins 0.000 claims description 8
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 claims description 8
- 101150112756 creC gene Proteins 0.000 claims description 8
- 101150056237 creB gene Proteins 0.000 claims description 4
- 108010032178 Amino-acid N-acetyltransferase Proteins 0.000 claims description 3
- QYPPJABKJHAVHS-UHFFFAOYSA-N Agmatine Natural products NCCCCNC(N)=N QYPPJABKJHAVHS-UHFFFAOYSA-N 0.000 claims description 2
- 108090000604 Hydrolases Proteins 0.000 claims description 2
- QYPPJABKJHAVHS-UHFFFAOYSA-P agmatinium(2+) Chemical compound NC(=[NH2+])NCCCC[NH3+] QYPPJABKJHAVHS-UHFFFAOYSA-P 0.000 claims description 2
- 241000219357 Cactaceae Species 0.000 claims 1
- 241000316914 Prococcus Species 0.000 claims 1
- 101150027964 ada gene Proteins 0.000 claims 1
- 229940014425 exodus Drugs 0.000 claims 1
- RFMMMVDNIPUKGG-YFKPBYRVSA-N N-acetyl-L-glutamic acid Chemical compound CC(=O)N[C@H](C(O)=O)CCC(O)=O RFMMMVDNIPUKGG-YFKPBYRVSA-N 0.000 abstract description 4
- 230000008569 process Effects 0.000 abstract description 3
- 102100021079 Ornithine decarboxylase Human genes 0.000 abstract 2
- 210000004027 cell Anatomy 0.000 description 57
- 238000004519 manufacturing process Methods 0.000 description 37
- 239000012634 fragment Substances 0.000 description 24
- 235000010469 Glycine max Nutrition 0.000 description 22
- 239000002609 medium Substances 0.000 description 17
- 230000035772 mutation Effects 0.000 description 17
- 229960003104 ornithine Drugs 0.000 description 17
- 229960000723 ampicillin Drugs 0.000 description 15
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 15
- 238000004458 analytical method Methods 0.000 description 15
- AHLPHDHHMVZTML-BYPYZUCNSA-N L-Ornithine Chemical compound NCCC[C@H](N)C(O)=O AHLPHDHHMVZTML-BYPYZUCNSA-N 0.000 description 13
- AHLPHDHHMVZTML-UHFFFAOYSA-N Orn-delta-NH2 Natural products NCCCC(N)C(O)=O AHLPHDHHMVZTML-UHFFFAOYSA-N 0.000 description 13
- UTJLXEIPEHZYQJ-UHFFFAOYSA-N Ornithine Natural products OC(=O)C(C)CCCN UTJLXEIPEHZYQJ-UHFFFAOYSA-N 0.000 description 13
- 238000002360 preparation method Methods 0.000 description 13
- 238000006243 chemical reaction Methods 0.000 description 12
- 238000010276 construction Methods 0.000 description 12
- 229920000768 polyamine Polymers 0.000 description 12
- ATHGHQPFGPMSJY-UHFFFAOYSA-N spermidine Chemical compound NCCCCNCCCN ATHGHQPFGPMSJY-UHFFFAOYSA-N 0.000 description 12
- 230000009466 transformation Effects 0.000 description 12
- 238000012795 verification Methods 0.000 description 12
- 238000002474 experimental method Methods 0.000 description 10
- 239000013604 expression vector Substances 0.000 description 10
- 238000012163 sequencing technique Methods 0.000 description 10
- 239000000126 substance Substances 0.000 description 10
- 241000588724 Escherichia coli Species 0.000 description 9
- 230000014509 gene expression Effects 0.000 description 9
- 108091034117 Oligonucleotide Proteins 0.000 description 8
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 8
- 238000007630 basic procedure Methods 0.000 description 8
- 239000013611 chromosomal DNA Substances 0.000 description 8
- 230000003287 optical effect Effects 0.000 description 8
- 239000000047 product Substances 0.000 description 8
- 150000003839 salts Chemical class 0.000 description 8
- 239000007858 starting material Substances 0.000 description 8
- 229920001817 Agar Polymers 0.000 description 7
- 108020004705 Codon Proteins 0.000 description 7
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 7
- 239000008272 agar Substances 0.000 description 7
- 239000002773 nucleotide Substances 0.000 description 7
- 125000003729 nucleotide group Chemical group 0.000 description 7
- 102000004169 proteins and genes Human genes 0.000 description 7
- 108091008146 restriction endonucleases Proteins 0.000 description 7
- 108700016258 Agmatinases Proteins 0.000 description 6
- 229940063673 spermidine Drugs 0.000 description 6
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 5
- 101001027192 Homo sapiens Kelch-like protein 41 Proteins 0.000 description 5
- 102100037644 Kelch-like protein 41 Human genes 0.000 description 5
- 239000005700 Putrescine Substances 0.000 description 5
- 238000010367 cloning Methods 0.000 description 5
- 230000000052 comparative effect Effects 0.000 description 5
- 229930195712 glutamate Natural products 0.000 description 5
- 230000001939 inductive effect Effects 0.000 description 5
- 238000000926 separation method Methods 0.000 description 5
- 241000196324 Embryophyta Species 0.000 description 4
- 108010042407 Endonucleases Proteins 0.000 description 4
- 102000004533 Endonucleases Human genes 0.000 description 4
- 244000068988 Glycine max Species 0.000 description 4
- 239000006142 Luria-Bertani Agar Substances 0.000 description 4
- 239000003637 basic solution Substances 0.000 description 4
- 230000036983 biotransformation Effects 0.000 description 4
- VHRGRCVQAFMJIZ-UHFFFAOYSA-N cadaverine Chemical compound NCCCCCN VHRGRCVQAFMJIZ-UHFFFAOYSA-N 0.000 description 4
- 229910052799 carbon Inorganic materials 0.000 description 4
- 238000005119 centrifugation Methods 0.000 description 4
- 150000001875 compounds Chemical class 0.000 description 4
- 238000013461 design Methods 0.000 description 4
- 239000000463 material Substances 0.000 description 4
- 230000037361 pathway Effects 0.000 description 4
- 239000006228 supernatant Substances 0.000 description 4
- BMAUUIABJVXLIG-SSDOTTSWSA-N (2r)-2-acetyl-2,5-diaminopentanoic acid Chemical compound CC(=O)[C@@](N)(C(O)=O)CCCN BMAUUIABJVXLIG-SSDOTTSWSA-N 0.000 description 3
- 101100322581 Caenorhabditis elegans add-1 gene Proteins 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- 238000005481 NMR spectroscopy Methods 0.000 description 3
- 230000002210 biocatalytic effect Effects 0.000 description 3
- 238000002306 biochemical method Methods 0.000 description 3
- 230000001851 biosynthetic effect Effects 0.000 description 3
- 230000003833 cell viability Effects 0.000 description 3
- 239000013613 expression plasmid Substances 0.000 description 3
- 230000004048 modification Effects 0.000 description 3
- 238000012986 modification Methods 0.000 description 3
- 239000002243 precursor Substances 0.000 description 3
- 239000000376 reactant Substances 0.000 description 3
- 230000022532 regulation of transcription, DNA-dependent Effects 0.000 description 3
- 238000010561 standard procedure Methods 0.000 description 3
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 2
- 108700016156 Arginine decarboxylases Proteins 0.000 description 2
- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 2
- RGJOEKWQDUBAIZ-IBOSZNHHSA-N CoASH Chemical compound O[C@@H]1[C@H](OP(O)(O)=O)[C@@H](COP(O)(=O)OP(O)(=O)OCC(C)(C)[C@@H](O)C(=O)NCCC(=O)NCCS)O[C@H]1N1C2=NC=NC(N)=C2N=C1 RGJOEKWQDUBAIZ-IBOSZNHHSA-N 0.000 description 2
- 101710170109 Constitutive ornithine decarboxylase Proteins 0.000 description 2
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 2
- 244000166124 Eucalyptus globulus Species 0.000 description 2
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 2
- 229930195714 L-glutamate Natural products 0.000 description 2
- 101100272680 Paracentrotus lividus BP10 gene Proteins 0.000 description 2
- 241000588769 Proteus <enterobacteria> Species 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 101100108191 Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) add gene Proteins 0.000 description 2
- 238000009825 accumulation Methods 0.000 description 2
- ZSLZBFCDCINBPY-ZSJPKINUSA-N acetyl-CoA Chemical compound O[C@@H]1[C@H](OP(O)(O)=O)[C@@H](COP(O)(=O)OP(O)(=O)OCC(C)(C)[C@@H](O)C(=O)NCCC(=O)NCCSC(=O)C)O[C@H]1N1C2=NC=NC(N)=C2N=C1 ZSLZBFCDCINBPY-ZSJPKINUSA-N 0.000 description 2
- 230000009471 action Effects 0.000 description 2
- WNLRTRBMVRJNCN-UHFFFAOYSA-N adipic acid Chemical compound OC(=O)CCCCC(O)=O WNLRTRBMVRJNCN-UHFFFAOYSA-N 0.000 description 2
- 101150116939 agdA gene Proteins 0.000 description 2
- 230000030833 cell death Effects 0.000 description 2
- 238000003776 cleavage reaction Methods 0.000 description 2
- RGJOEKWQDUBAIZ-UHFFFAOYSA-N coenzime A Natural products OC1C(OP(O)(O)=O)C(COP(O)(=O)OP(O)(=O)OCC(C)(C)C(O)C(=O)NCCC(=O)NCCS)OC1N1C2=NC=NC(N)=C2N=C1 RGJOEKWQDUBAIZ-UHFFFAOYSA-N 0.000 description 2
- 239000005516 coenzyme A Substances 0.000 description 2
- 229940093530 coenzyme a Drugs 0.000 description 2
- 230000002950 deficient Effects 0.000 description 2
- KDTSHFARGAKYJN-UHFFFAOYSA-N dephosphocoenzyme A Natural products OC1C(O)C(COP(O)(=O)OP(O)(=O)OCC(C)(C)C(O)C(=O)NCCC(=O)NCCS)OC1N1C2=NC=NC(N)=C2N=C1 KDTSHFARGAKYJN-UHFFFAOYSA-N 0.000 description 2
- 230000002074 deregulated effect Effects 0.000 description 2
- 150000004985 diamines Chemical class 0.000 description 2
- JBKVHLHDHHXQEQ-UHFFFAOYSA-N epsilon-caprolactam Chemical compound O=C1CCCCCN1 JBKVHLHDHHXQEQ-UHFFFAOYSA-N 0.000 description 2
- 239000000284 extract Substances 0.000 description 2
- 108020001507 fusion proteins Proteins 0.000 description 2
- 102000037865 fusion proteins Human genes 0.000 description 2
- 239000008103 glucose Substances 0.000 description 2
- 238000004128 high performance liquid chromatography Methods 0.000 description 2
- 229920001519 homopolymer Polymers 0.000 description 2
- LELOWRISYMNNSU-UHFFFAOYSA-N hydrogen cyanide Chemical compound N#C LELOWRISYMNNSU-UHFFFAOYSA-N 0.000 description 2
- 230000006872 improvement Effects 0.000 description 2
- 239000000178 monomer Substances 0.000 description 2
- 229930014626 natural product Natural products 0.000 description 2
- 230000007017 scission Effects 0.000 description 2
- PFNFFQXMRSDOHW-UHFFFAOYSA-N spermine Chemical compound NCCCNCCCCNCCCN PFNFFQXMRSDOHW-UHFFFAOYSA-N 0.000 description 2
- 230000002103 transcriptional effect Effects 0.000 description 2
- 102000004092 Amidohydrolases Human genes 0.000 description 1
- 108090000531 Amidohydrolases Proteins 0.000 description 1
- 101150101995 BP10 gene Proteins 0.000 description 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- NVDWNVIZFNLMSE-GDVGLLTNSA-N C(C)(=O)C([C@H](N)C(=O)O)CCN Chemical compound C(C)(=O)C([C@H](N)C(=O)O)CCN NVDWNVIZFNLMSE-GDVGLLTNSA-N 0.000 description 1
- 101150083464 CP gene Proteins 0.000 description 1
- 101100346189 Caenorhabditis elegans mpc-1 gene Proteins 0.000 description 1
- 108090000489 Carboxy-Lyases Proteins 0.000 description 1
- 108010077448 Diamine N-acetyltransferase Proteins 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- 102000004157 Hydrolases Human genes 0.000 description 1
- 108010093096 Immobilized Enzymes Proteins 0.000 description 1
- 101710088686 Inducible ornithine decarboxylase Proteins 0.000 description 1
- 229910052779 Neodymium Inorganic materials 0.000 description 1
- 229920003189 Nylon 4,6 Polymers 0.000 description 1
- 229920002292 Nylon 6 Polymers 0.000 description 1
- 238000012408 PCR amplification Methods 0.000 description 1
- 241001275117 Seres Species 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- 108020005038 Terminator Codon Proteins 0.000 description 1
- 102000005421 acetyltransferase Human genes 0.000 description 1
- 108020002494 acetyltransferase Proteins 0.000 description 1
- 239000001361 adipic acid Substances 0.000 description 1
- 235000011037 adipic acid Nutrition 0.000 description 1
- 150000001412 amines Chemical class 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 125000003277 amino group Chemical group 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 206010003246 arthritis Diseases 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 230000003851 biochemical process Effects 0.000 description 1
- 239000001569 carbon dioxide Substances 0.000 description 1
- 229910002092 carbon dioxide Inorganic materials 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 238000006555 catalytic reaction Methods 0.000 description 1
- 239000013592 cell lysate Substances 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 229910052804 chromium Inorganic materials 0.000 description 1
- 229910052802 copper Inorganic materials 0.000 description 1
- 239000012228 culture supernatant Substances 0.000 description 1
- 230000000911 decarboxylating effect Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 230000004069 differentiation Effects 0.000 description 1
- 229920006351 engineering plastic Polymers 0.000 description 1
- 239000003797 essential amino acid Substances 0.000 description 1
- 235000020776 essential amino acid Nutrition 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 239000003925 fat Substances 0.000 description 1
- 230000008713 feedback mechanism Effects 0.000 description 1
- 239000003337 fertilizer Substances 0.000 description 1
- 238000012239 gene modification Methods 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 230000005017 genetic modification Effects 0.000 description 1
- 235000013617 genetically modified food Nutrition 0.000 description 1
- 239000003966 growth inhibitor Substances 0.000 description 1
- GDRJDUSGGPSMEI-UHFFFAOYSA-N heptane-1,4,7-triamine Chemical compound NCCCC(N)CCCN GDRJDUSGGPSMEI-UHFFFAOYSA-N 0.000 description 1
- 238000011141 high resolution liquid chromatography Methods 0.000 description 1
- 238000009396 hybridization Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 238000009776 industrial production Methods 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 239000013067 intermediate product Substances 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- BBJIPMIXTXKYLZ-UHFFFAOYSA-N isoglutamic acid Chemical compound OC(=O)CC(N)CC(O)=O BBJIPMIXTXKYLZ-UHFFFAOYSA-N 0.000 description 1
- 125000001449 isopropyl group Chemical group [H]C([H])([H])C([H])(*)C([H])([H])[H] 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 150000002825 nitriles Chemical class 0.000 description 1
- 229920001778 nylon Polymers 0.000 description 1
- 239000003921 oil Substances 0.000 description 1
- 238000012261 overproduction Methods 0.000 description 1
- 230000036961 partial effect Effects 0.000 description 1
- 239000000575 pesticide Substances 0.000 description 1
- 150000002989 phenols Chemical class 0.000 description 1
- ZWLUXSQADUDCSB-UHFFFAOYSA-N phthalaldehyde Chemical class O=CC1=CC=CC=C1C=O ZWLUXSQADUDCSB-UHFFFAOYSA-N 0.000 description 1
- 230000035790 physiological processes and functions Effects 0.000 description 1
- 238000006068 polycondensation reaction Methods 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 230000002829 reductive effect Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 230000000284 resting effect Effects 0.000 description 1
- 238000003757 reverse transcription PCR Methods 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 102220004442 rs121918685 Human genes 0.000 description 1
- 102220005241 rs33951465 Human genes 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 229910052709 silver Inorganic materials 0.000 description 1
- 239000000344 soap Substances 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 239000000243 solution Substances 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 229940063675 spermine Drugs 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 238000001308 synthesis method Methods 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 230000036962 time dependent Effects 0.000 description 1
- 231100000167 toxic agent Toxicity 0.000 description 1
- 239000011573 trace mineral Substances 0.000 description 1
- 235000013619 trace mineral Nutrition 0.000 description 1
- 238000000844 transformation Methods 0.000 description 1
- 230000014616 translation Effects 0.000 description 1
- 239000011782 vitamin Substances 0.000 description 1
- 229930003231 vitamin Natural products 0.000 description 1
- 229940088594 vitamin Drugs 0.000 description 1
- 235000013343 vitamin Nutrition 0.000 description 1
- 150000003722 vitamin derivatives Chemical class 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/10—Transferases (2.)
- C12N9/1025—Acyltransferases (2.3)
- C12N9/1029—Acyltransferases (2.3) transferring groups other than amino-acyl groups (2.3.1)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/88—Lyases (4.)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P13/00—Preparation of nitrogen-containing organic compounds
- C12P13/001—Amines; Imines
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Zoology (AREA)
- Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Genetics & Genomics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Microbiology (AREA)
- General Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Biomedical Technology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Enzymes And Modification Thereof (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP04077046 | 2004-07-15 | ||
| PCT/EP2005/007606 WO2006005603A1 (en) | 2004-07-15 | 2005-07-11 | Biochemical synthesis of 1,4-butanediamine |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| EA200700329A1 EA200700329A1 (ru) | 2007-08-31 |
| EA010179B1 true EA010179B1 (ru) | 2008-06-30 |
Family
ID=34928370
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| EA200700329A EA010179B1 (ru) | 2004-07-15 | 2005-07-11 | Биохимический синтез 1,4-бутандиамина |
Country Status (18)
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2616002C2 (ru) * | 2012-10-22 | 2017-04-12 | СиДжей ЧеилДжеданг Корп. | Способ очистки 1,4-диаминобутана, очищенный указанным способом 1,4-диаминобутан и полученный из него полиамид |
Families Citing this family (26)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US8044166B2 (en) | 2006-08-01 | 2011-10-25 | Basf Aktiengesellschaft | Process for preparing pentamethylene 1,5-diisocyanate |
| CN101063144B (zh) * | 2007-05-10 | 2010-09-15 | 南京农业大学 | 乳酸菌谷氨酸脱羧酶基因的克隆、表达及应用 |
| KR101621256B1 (ko) | 2008-03-12 | 2016-05-16 | 도레이 카부시키가이샤 | 디아민 및 폴리아미드의 제조 방법 |
| MY175283A (en) | 2008-04-10 | 2020-06-18 | Korea Advanced Inst Sci & Tech | Mutant microorganisms having high ability to produce putrescine and method for producing putrescine using the same |
| FR2933414B1 (fr) * | 2008-07-07 | 2010-08-13 | Arkema France | Polyamide, composition comprenant un tel polyamide et leurs utilisations |
| EP2456879B1 (en) * | 2009-07-24 | 2018-04-04 | DSM IP Assets B.V. | Process for preparing 1,4-butanediamine via n-protected 1,4-butanediamine |
| JP2013507145A (ja) * | 2009-10-13 | 2013-03-04 | ゲノマチカ， インク． | １，４−ブタンジオール、４−ヒドロキシブタナール、４−ヒドロキシブチリル−ＣｏＡ、プトレシン及び関連化合物の生成のための微生物体並びに関連する方法 |
| KR101174267B1 (ko) * | 2010-01-06 | 2012-08-14 | 씨제이제일제당 (주) | Ｌ-오르니틴 또는 ｌ-아르기닌 생산 변이주 및 이의 제조방법 |
| KR101348461B1 (ko) * | 2010-12-08 | 2014-01-08 | 씨제이제일제당 (주) | 퓨트레신을 생산하는 미생물 및 이를 이용하여 퓨트레신을 생산하는 방법 |
| KR101286158B1 (ko) * | 2011-08-24 | 2013-07-15 | 씨제이제일제당 (주) | 발효액에서 1,4-디아미노부탄의 분리 및 정제하는 방법 |
| WO2013105827A2 (ko) * | 2012-01-11 | 2013-07-18 | 씨제이제일제당 (주) | 퓨트레신 생산능이 향상된 재조합 미생물 및 이를 이용하여 퓨트레신을 생산하는 방법 |
| DK2806022T3 (en) | 2012-01-20 | 2018-08-13 | Cj Cheiljedang Corp | Recombinant microorganism with improved putrescine productivity and method of producing putrescine using the same |
| KR101607741B1 (ko) | 2013-03-20 | 2016-03-31 | 씨제이제일제당 (주) | 퓨트레신 생산 재조합 미생물 및 이를 이용한 퓨트레신 생산방법 |
| KR101835164B1 (ko) | 2013-07-17 | 2018-03-06 | 씨제이제일제당 (주) | 향상된 퓨트레신 생산능을 가지는 변이된 오르니틴 디카복실레이즈 단백질 및 이의 용도 |
| CN103951504A (zh) * | 2014-04-21 | 2014-07-30 | 扬州市嘉康菇业发展有限公司 | 一种促进金针菇菌丝体快速生长的培养基的制备方法 |
| CN106574234B (zh) | 2014-04-25 | 2020-06-09 | Cj第一制糖株式会社 | 产生二胺的微生物和使用该微生物产生二胺的方法 |
| ES2717600T3 (es) | 2014-04-25 | 2019-06-24 | Cj Cheiljedang Corp | Microorganismo productor de diamina y método para producir diamina usando el mismo |
| KR101723290B1 (ko) | 2014-04-25 | 2017-04-05 | 씨제이제일제당 (주) | 퓨트레신 생산 변이주 및 이를 이용한 퓨트레신 생산방법 |
| JP2017158434A (ja) * | 2014-07-22 | 2017-09-14 | 協同乳業株式会社 | バクテリア混合培養によるプトレッシン製造方法 |
| KR101813759B1 (ko) | 2015-06-24 | 2018-01-02 | 씨제이제일제당 (주) | 퓨트레신 또는 오르니틴 생산 미생물 및 이를 이용한 퓨트레신 또는 오르니틴 생산방법 |
| KR101735935B1 (ko) | 2015-07-20 | 2017-05-16 | 씨제이제일제당 (주) | 퓨트레신 또는 오르니틴 생산 미생물 및 이를 이용한 퓨트레신 또는 오르니틴 생산방법 |
| KR102011394B1 (ko) | 2017-07-19 | 2019-10-22 | 씨제이제일제당 주식회사 | 퓨트레신을 생산하는 미생물 및 이를 이용한 퓨트레신 생산방법 |
| EP3808848A1 (en) | 2019-10-14 | 2021-04-21 | Eberhard Karls Universität Tübingen | Regulatory element of an arginine decarboxylase gene and methods and uses thereof |
| KR102246288B1 (ko) | 2020-08-13 | 2021-04-29 | 씨제이제일제당 주식회사 | 퓨트레신 생산 미생물 및 이를 이용한 퓨트레신 생산방법 |
| CN113061562B (zh) * | 2021-03-22 | 2022-09-27 | 江南大学 | 一种利用钝齿棒杆菌发酵生产1,4-丁二胺的方法 |
| CN117736951A (zh) * | 2023-11-27 | 2024-03-22 | 天津科技大学 | 生产1,4-丁二胺的大肠杆菌底盘菌株及其应用 |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0726240A1 (en) * | 1995-02-10 | 1996-08-14 | Taguidell, S.L. | Obtaining and use of diamines, polyamines and other complementary active elements from treated natural products |
| WO2001011062A2 (en) * | 1999-08-10 | 2001-02-15 | John Innes Centre | Polyamine accumulation in plants |
| EP1260588A2 (en) * | 2001-05-25 | 2002-11-27 | Ajinomoto Co., Ltd. | Methods of producing agmatine and arginine decarboxylase |
Family Cites Families (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US2130948A (en) | 1937-04-09 | 1938-09-20 | Du Pont | Synthetic fiber |
-
2005
- 2005-07-11 EA EA200700329A patent/EA010179B1/ru not_active IP Right Cessation
- 2005-07-11 AU AU2005261861A patent/AU2005261861B2/en not_active Ceased
- 2005-07-11 EP EP05767851.8A patent/EP1784496B1/en not_active Expired - Lifetime
- 2005-07-11 ES ES05767851.8T patent/ES2581244T3/es not_active Expired - Lifetime
- 2005-07-11 US US11/632,458 patent/US8497098B2/en not_active Expired - Fee Related
- 2005-07-11 JP JP2007520744A patent/JP4836948B2/ja not_active Expired - Fee Related
- 2005-07-11 UA UAA200701584A patent/UA90479C2/ru unknown
- 2005-07-11 BR BRPI0513343-2A patent/BRPI0513343B1/pt not_active IP Right Cessation
- 2005-07-11 CN CN2005800236901A patent/CN101010433B/zh not_active Expired - Fee Related
- 2005-07-11 DK DK05767851.8T patent/DK1784496T3/en active
- 2005-07-11 NZ NZ552631A patent/NZ552631A/en not_active IP Right Cessation
- 2005-07-11 CA CA2571528A patent/CA2571528C/en not_active Expired - Fee Related
- 2005-07-11 WO PCT/EP2005/007606 patent/WO2006005603A1/en active Application Filing
- 2005-07-11 EP EP15175520.4A patent/EP2949755B1/en not_active Expired - Lifetime
- 2005-07-11 MX MX2007000566A patent/MX2007000566A/es active IP Right Grant
- 2005-07-15 TW TW094124157A patent/TWI346139B/zh not_active IP Right Cessation
- 2005-07-15 MY MYPI20053244 patent/MY152156A/en unknown
-
2007
- 2007-01-03 ZA ZA200700104A patent/ZA200700104B/en unknown
- 2007-01-17 IN IN479DE2007 patent/IN2007DE00479A/en unknown
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0726240A1 (en) * | 1995-02-10 | 1996-08-14 | Taguidell, S.L. | Obtaining and use of diamines, polyamines and other complementary active elements from treated natural products |
| WO2001011062A2 (en) * | 1999-08-10 | 2001-02-15 | John Innes Centre | Polyamine accumulation in plants |
| EP1260588A2 (en) * | 2001-05-25 | 2002-11-27 | Ajinomoto Co., Ltd. | Methods of producing agmatine and arginine decarboxylase |
Non-Patent Citations (11)
| Title |
|---|
| COHEN S.S.: "A guide to the polyamines", 1998, OXFORD UNIVERSITY PRESS, OXFORD, XP002300280, ISBN: 0195110641, pages 122-183 * |
| CUNIN R. ET AL.: "Biosynthesis and metabolism of arginine in bacteria", MICROBIOLOGICAL REVIEWS, vol. 3, no. 50, September 1986 (1986-09), pages 314-352, XP001068304, ISSN: 0146-0749, tables 1, 3 * |
| FUKUCHI J-I. ET AL.: "Decrease in cell viability due to the accumulation of spermidine in spermidine acetyltransferase-deficient mutant of Escherichia coli", JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 270, no. 32, 1995, pages 18831-18835, XP002300277, ISSN: 0021-9258, cited in the application, abstract * |
| KASHIWAGI K. ET AL.: "Adjustment of polyamine contents in Escherichia coli." JOURNAL OF BACTERIOLOGY. JUL 1988, vol. 170, no. 7, July 1988 (1988-07), pages 3131-3135, XP008036641, ISSN: 0021-9193, cited 1n the application, abstract, page 3132, right-hand column, line 15 - page 3133, left-hand column, line 26, tables 1-3, page 3134, right-hand column, lines 2-10 * |
| KLEIN R.D. ET AL.: "Reconstitution of a bacterial/plant polyamine biosynthesis pathway in Saccharomyces cerevisiae", MICROBIOLOGY, vol. 145, no. 2, February 1999 (1999-02), pages 301-307, XP002232122, ISSN: 1350-0872, abstract * |
| MACRAE M. ET AL.: "Complementation of a polyamine-deficient Escherichia coli mutant by expression of mouse ornithine decarboxylase", MOLECULAR AND CELLULAR BIOLOGY, vol. 7, no. 1, January 1987 (1987-01), pages 564-567, XP002300275, ISSN: 0270-7306, abstract, table 1, figure 2 * |
| NAKADA Y. ET AL.: "Identification of the putrescine biosynthetic genes in Pseudomonas aeruginosa and characterization of agmatine deiminase and N-carbamoylputrescine amidohydrolase of the arginine decarboxylase pathway." MICROBIOLOGY, vol. 149, no. 3, March 2003 (2003-03), pages 707-714, XP002300276, ISSN: 1350-0872, abstract, table 3, figure 1 * |
| RAJAGOPAL B.S. ET AL.: "Use of Inducible feedback-resistant N-acetylglutamate synthetase (argA) genes for enhanced arginine biosynthesis by genetically engineered Escherichia coli K-12 strains", APPLIED AND ENVIRONMENTAL MICROBIOLOGY, vol. 64, no. 5, May 1998 (1998-05), pages 1805-1811, XP002169946, ISSN: 0099-2240, abstract figure 1 * |
| SAKANYAN V. ET AL.: "Genes and enzymes of the acetyl cycle of arginine biosynthesis in Corynebacterium glutamicum: enzyme evolution in the early steps of the arginine pathway", MICROBIOLOGY, vol. PART 1, no. 142, January 1996 (1996-01), pages 99-108, XP001063142, ISSN: 1350-0872, abstract, figure 1 * |
| SUZUKI T. ET AL.: "Antizyme protects against abnormal accumulation and toxicity of polyamines in ornithine decarboxylase-overproducing cells", PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, vol. 91, no. 19, 1994, pages 8930-8934, XP002300278, ISSN: 0027-8424, cited in the application, abstract * |
| TABOR C.W. ET AL.: "Polyamines in microorganisms", MICROBIOLOGICAL REVIEWS, vol. 49, no. 1, March 1985 (1985-03), pages 81-99, XP002300279, ISSN: 0146-0749, the whole document * |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2616002C2 (ru) * | 2012-10-22 | 2017-04-12 | СиДжей ЧеилДжеданг Корп. | Способ очистки 1,4-диаминобутана, очищенный указанным способом 1,4-диаминобутан и полученный из него полиамид |
Also Published As
| Publication number | Publication date |
|---|---|
| JP4836948B2 (ja) | 2011-12-14 |
| AU2005261861A1 (en) | 2006-01-19 |
| UA90479C2 (en) | 2010-05-11 |
| EP2949755A1 (en) | 2015-12-02 |
| CA2571528A1 (en) | 2006-01-19 |
| CN101010433A (zh) | 2007-08-01 |
| EP2949755B1 (en) | 2018-03-28 |
| TW200605869A (en) | 2006-02-16 |
| CA2571528C (en) | 2016-02-16 |
| BRPI0513343B1 (pt) | 2020-11-03 |
| AU2005261861B2 (en) | 2010-08-26 |
| EP1784496A1 (en) | 2007-05-16 |
| BRPI0513343A (pt) | 2008-05-06 |
| ES2581244T3 (es) | 2016-09-02 |
| EP1784496B1 (en) | 2016-04-06 |
| ZA200700104B (en) | 2008-05-28 |
| MY152156A (en) | 2014-08-15 |
| US8497098B2 (en) | 2013-07-30 |
| JP2008505651A (ja) | 2008-02-28 |
| EA200700329A1 (ru) | 2007-08-31 |
| MX2007000566A (es) | 2007-04-02 |
| DK1784496T3 (en) | 2016-07-25 |
| US20090011478A1 (en) | 2009-01-08 |
| IN2007DE00479A (GUID-C5D7CC26-194C-43D0-91A1-9AE8C70A9BFF.html) | 2007-08-17 |
| TWI346139B (en) | 2011-08-01 |
| CN101010433B (zh) | 2012-03-07 |
| WO2006005603A1 (en) | 2006-01-19 |
| NZ552631A (en) | 2009-09-25 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| EA010179B1 (ru) | Биохимический синтез 1,4-бутандиамина | |
| Blombach et al. | Corynebacterium glutamicum tailored for high-yield L-valine production | |
| US20160319311A1 (en) | Biochemical synthesis of 1,4-butanediamine | |
| JP5140848B2 (ja) | 没食子酸の製造法 | |
| JP6951702B2 (ja) | トレハンジェリンの製造法 | |
| KR101292838B1 (ko) | 재조합 대장균을 이용한 ５―아미노발레르산의 제조 방법 | |
| WO2020213374A1 (ja) | ペルオキシダーゼの組換え生産 | |
| JP2016503650A (ja) | Ｄｌ−アラニンを生産する遺伝子操作細菌、及び前記遺伝子操作細菌を用いることによってｄｌ−アラニンを生産する方法 | |
| BRPI0513362B1 (pt) | Process for obtaining 1,4-butanodiamine in a fermentation process |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| MM4A | Lapse of a eurasian patent due to non-payment of renewal fees within the time limit in the following designated state(s) |
Designated state(s): AM AZ BY KZ KG MD TJ TM |
|
| MM4A | Lapse of a eurasian patent due to non-payment of renewal fees within the time limit in the following designated state(s) |
Designated state(s): RU |