JP2012523235A5 - - Google Patents
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- JP2012523235A5 JP2012523235A5 JP2012504868A JP2012504868A JP2012523235A5 JP 2012523235 A5 JP2012523235 A5 JP 2012523235A5 JP 2012504868 A JP2012504868 A JP 2012504868A JP 2012504868 A JP2012504868 A JP 2012504868A JP 2012523235 A5 JP2012523235 A5 JP 2012523235A5
- Authority
- JP
- Japan
- Prior art keywords
- seq
- nucleic acid
- plasmid
- acid molecule
- polypeptide
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
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- 239000013612 plasmid Substances 0.000 claims description 29
- 150000007523 nucleic acids Chemical group 0.000 claims description 16
- 238000000034 method Methods 0.000 claims description 14
- 108020004707 nucleic acids Proteins 0.000 claims description 14
- 102000039446 nucleic acids Human genes 0.000 claims description 14
- QTBSBXVTEAMEQO-UHFFFAOYSA-N acetic acid Substances CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 claims description 8
- 229920001184 polypeptide Polymers 0.000 claims description 8
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 8
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 8
- 108090000790 Enzymes Proteins 0.000 claims description 7
- 102000004190 Enzymes Human genes 0.000 claims description 7
- 239000012141 concentrate Substances 0.000 claims description 7
- 239000002773 nucleotide Substances 0.000 claims description 4
- 125000003729 nucleotide group Chemical group 0.000 claims description 4
- -1 1,1-dimethylethoxy Chemical group 0.000 claims description 2
- UDKIRRNUAXWHTO-UHFFFAOYSA-N 2-(3-hydroxy-1-adamantyl)-2-oxoacetic acid Chemical compound C1C(C2)CC3CC2(O)CC1(C(=O)C(=O)O)C3 UDKIRRNUAXWHTO-UHFFFAOYSA-N 0.000 claims description 2
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims description 2
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 2
- 230000015572 biosynthetic process Effects 0.000 claims description 2
- 238000004519 manufacturing process Methods 0.000 claims description 2
- 210000004027 cell Anatomy 0.000 claims 3
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 claims 2
- 238000012258 culturing Methods 0.000 claims 2
- DYHSDKLCOJIUFX-UHFFFAOYSA-N tert-butoxycarbonyl anhydride Chemical compound CC(C)(C)OC(=O)OC(=O)OC(C)(C)C DYHSDKLCOJIUFX-UHFFFAOYSA-N 0.000 claims 2
- 108700039691 Genetic Promoter Regions Proteins 0.000 claims 1
- 210000001236 prokaryotic cell Anatomy 0.000 claims 1
- 108090000698 Formate Dehydrogenases Proteins 0.000 description 30
- 108010078226 phenylalanine oxidase Proteins 0.000 description 16
- 239000012634 fragment Substances 0.000 description 8
- 230000000694 effects Effects 0.000 description 5
- 150000001875 compounds Chemical class 0.000 description 4
- 238000000855 fermentation Methods 0.000 description 4
- 230000004151 fermentation Effects 0.000 description 4
- 108020004414 DNA Proteins 0.000 description 3
- 230000001580 bacterial effect Effects 0.000 description 3
- 238000001914 filtration Methods 0.000 description 3
- QGJUIPDUBHWZPV-SGTAVMJGSA-N saxagliptin Chemical compound C1C(C2)CC(C3)CC2(O)CC13[C@H](N)C(=O)N1[C@H](C#N)C[C@@H]2C[C@@H]21 QGJUIPDUBHWZPV-SGTAVMJGSA-N 0.000 description 3
- 229960004937 saxagliptin Drugs 0.000 description 3
- 108010033693 saxagliptin Proteins 0.000 description 3
- 239000013598 vector Substances 0.000 description 3
- 241000588724 Escherichia coli Species 0.000 description 2
- 101000684208 Homo sapiens Prolyl endopeptidase FAP Proteins 0.000 description 2
- 239000005909 Kieselgur Substances 0.000 description 2
- 102100023832 Prolyl endopeptidase FAP Human genes 0.000 description 2
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 2
- 150000001412 amines Chemical class 0.000 description 2
- 230000036983 biotransformation Effects 0.000 description 2
- 101150086278 fdh gene Proteins 0.000 description 2
- 239000000706 filtrate Substances 0.000 description 2
- 239000003112 inhibitor Substances 0.000 description 2
- 229930027917 kanamycin Natural products 0.000 description 2
- SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 2
- 229960000318 kanamycin Drugs 0.000 description 2
- 229930182823 kanamycin A Natural products 0.000 description 2
- 239000002243 precursor Substances 0.000 description 2
- 108090000623 proteins and genes Proteins 0.000 description 2
- 102000004169 proteins and genes Human genes 0.000 description 2
- 108091008146 restriction endonucleases Proteins 0.000 description 2
- 241000894007 species Species 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 241000982822 Ficus obtusifolia Species 0.000 description 1
- 229930194542 Keto Natural products 0.000 description 1
- 241000235058 Komagataella pastoris Species 0.000 description 1
- 241000203773 Thermoactinomyces intermedius Species 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- 230000004931 aggregating effect Effects 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 125000002915 carbonyl group Chemical group [*:2]C([*:1])=O 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 238000012790 confirmation Methods 0.000 description 1
- UOQACRNTVQWTFF-UHFFFAOYSA-N decane-1,10-dithiol Chemical compound SCCCCCCCCCCS UOQACRNTVQWTFF-UHFFFAOYSA-N 0.000 description 1
- 238000010586 diagram Methods 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 238000001976 enzyme digestion Methods 0.000 description 1
- 239000013604 expression vector Substances 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 125000000468 ketone group Chemical group 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 150000002994 phenylalanines Chemical class 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 238000003259 recombinant expression Methods 0.000 description 1
- 238000006268 reductive amination reaction Methods 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US16767609P | 2009-04-08 | 2009-04-08 | |
| US61/167,676 | 2009-04-08 | ||
| PCT/US2010/030404 WO2010118240A1 (en) | 2009-04-08 | 2010-04-08 | A genetically stable plasmid expressing pdh and fdh enzymes |
Related Child Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2014041887A Division JP2014128281A (ja) | 2009-04-08 | 2014-03-04 | Ｐｄｈおよびｆｄｈ酵素を発現する遺伝学的に安定なプラスミド |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2012523235A JP2012523235A (ja) | 2012-10-04 |
| JP2012523235A5 true JP2012523235A5 (https=) | 2013-11-07 |
Family
ID=42200623
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2012504868A Pending JP2012523235A (ja) | 2009-04-08 | 2010-04-08 | Ｐｄｈおよびｆｄｈ酵素を発現する遺伝学的に安定なプラスミド |
| JP2014041887A Pending JP2014128281A (ja) | 2009-04-08 | 2014-03-04 | Ｐｄｈおよびｆｄｈ酵素を発現する遺伝学的に安定なプラスミド |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2014041887A Pending JP2014128281A (ja) | 2009-04-08 | 2014-03-04 | Ｐｄｈおよびｆｄｈ酵素を発現する遺伝学的に安定なプラスミド |
Country Status (7)
| Country | Link |
|---|---|
| US (1) | US8158394B2 (https=) |
| EP (1) | EP2417260A1 (https=) |
| JP (2) | JP2012523235A (https=) |
| KR (1) | KR101292379B1 (https=) |
| CN (1) | CN102459610B (https=) |
| SG (1) | SG175054A1 (https=) |
| WO (1) | WO2010118240A1 (https=) |
Families Citing this family (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN103965065B (zh) * | 2013-02-01 | 2016-02-17 | 上海现代制药股份有限公司 | 沙格列汀中间体、其盐、其制备方法及其用途 |
| WO2014134281A1 (en) * | 2013-02-28 | 2014-09-04 | Full Spectrum Laboratories Limited | Biosynthesis of cannabinoids |
| CN103555683B (zh) * | 2013-11-19 | 2015-11-18 | 南京博优康远生物医药科技有限公司 | 一种沙格列汀手性中间体的合成方法 |
| WO2015087262A1 (en) | 2013-12-11 | 2015-06-18 | Ranbaxy Laboratories Limited | Process for the preparation of saxagliptin and its intermediates |
| CN103951588B (zh) * | 2014-04-30 | 2016-10-05 | 淮海工学院 | 一种合成沙格列汀中间体n-叔丁氧羰基-3-羟基-1-金刚烷基-d-甘氨酸的方法 |
| US9394510B2 (en) | 2014-08-25 | 2016-07-19 | Full Spectrum Laboratories Limited | Apparatus and methods for the simultaneous production of compounds |
| CN108795893B (zh) * | 2018-06-27 | 2021-10-08 | 凯莱英医药集团（天津）股份有限公司 | 一种氨基酸脱氢酶突变体及其制备方法和应用 |
| CN112391363B (zh) * | 2021-01-21 | 2021-04-06 | 凯莱英生命科学技术(天津)有限公司 | 氨基酸脱氢酶突变体及其应用 |
Family Cites Families (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6068991A (en) * | 1997-12-16 | 2000-05-30 | Bristol-Myers Squibb Company | High expression Escherichia coli expression vector |
| US6395767B2 (en) * | 2000-03-10 | 2002-05-28 | Bristol-Myers Squibb Company | Cyclopropyl-fused pyrrolidine-based inhibitors of dipeptidyl peptidase IV and method |
| US7087418B2 (en) * | 2001-12-19 | 2006-08-08 | Bristol-Myers Squibb Company | Pichia pastoris formate dehydrogenase and uses therefor |
| US7420079B2 (en) * | 2002-12-09 | 2008-09-02 | Bristol-Myers Squibb Company | Methods and compounds for producing dipeptidyl peptidase IV inhibitors and intermediates thereof |
| US7741082B2 (en) * | 2004-04-14 | 2010-06-22 | Bristol-Myers Squibb Company | Process for preparing dipeptidyl peptidase IV inhibitors and intermediates therefor |
| US8227228B2 (en) | 2005-08-02 | 2012-07-24 | Kaneka Corporation | D-amino acid oxidase, and method for production of L-amino acid, 2-oxo acid, or cyclic imine |
-
2010
- 2010-04-08 US US12/756,700 patent/US8158394B2/en active Active
- 2010-04-08 CN CN201080025346.7A patent/CN102459610B/zh active Active
- 2010-04-08 SG SG2011072261A patent/SG175054A1/en unknown
- 2010-04-08 JP JP2012504868A patent/JP2012523235A/ja active Pending
- 2010-04-08 WO PCT/US2010/030404 patent/WO2010118240A1/en not_active Ceased
- 2010-04-08 KR KR1020117026447A patent/KR101292379B1/ko not_active Expired - Fee Related
- 2010-04-08 EP EP10713773A patent/EP2417260A1/en not_active Withdrawn
-
2014
- 2014-03-04 JP JP2014041887A patent/JP2014128281A/ja active Pending
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