JP2007502124A - 改良ケトレダクターゼポリペプチドおよび関連ポリヌクレオチド - Google Patents
改良ケトレダクターゼポリペプチドおよび関連ポリヌクレオチド Download PDFInfo
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- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0006—Oxidoreductases (1.) acting on CH-OH groups as donors (1.1)
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Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2010539952A (ja) * | 2007-10-01 | 2010-12-24 | コデクシス， インコーポレイテッド | アゼチジノンの生産のためのケトレダクターゼポリペプチド |
| WO2011145211A1 (ja) * | 2010-05-21 | 2011-11-24 | 明治製菓株式会社 | ケトレダクターゼ変異体 |
| JP2022536500A (ja) * | 2019-06-13 | 2022-08-17 | アシムケム ラボラトリーズ （ティエンジン） カンパニー リミテッド | ケトレダクターゼ突然変異体及びキラルアルコールの生産方法 |
Families Citing this family (129)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
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| WO2010135624A2 (en) | 2009-05-22 | 2010-11-25 | Codexis, Inc. | Engineered biosynthesis of fatty alcohols |
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| US9322027B2 (en) | 2010-08-20 | 2016-04-26 | Shell Oil Company | Expression constructs comprising fungal promoters |
| US9074233B2 (en) | 2010-09-01 | 2015-07-07 | Concert Pharmaceuticals, Inc. | Process for preparing an enantiomerically enriched, deuterated secondary alcohol from a corresponding ketone without reducing deuterium incorporation |
| WO2012031072A1 (en) | 2010-09-01 | 2012-03-08 | Concert Pharmaceuticals, Inc. | Process for preparing an enantiomerically enriched, deuterated secondary alcohol from a corresponding ketone without reducing deuterium incorporation |
| WO2012035402A1 (en) * | 2010-09-14 | 2012-03-22 | Council Of Scientific & Industrial Research | High flux hollow fiber ultrafiltration membranes and process for the preparation thereof |
| JP2013541942A (ja) * | 2010-10-08 | 2013-11-21 | カディラ ヘルスケア リミティド | 酵素的変換によるシタグリプチンの中間体を生産する方法 |
| DK2649187T3 (da) | 2010-12-08 | 2018-01-29 | Codexis Inc | Biokatalysatorer og fremgangsmåder til syntesen af armodafinil |
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| EP2753640B1 (en) | 2011-09-08 | 2016-03-09 | Codexis, Inc. | Biocatalysts and methods for the synthesis of substituted lactams |
| EP2768811A1 (en) | 2011-10-19 | 2014-08-27 | Cipla Limited | Process for the preparation of an endothelin receptor antagonist |
| CN106479990B (zh) | 2011-11-18 | 2020-09-18 | 科德克希思公司 | 用于制备羟基取代的氨基甲酸酯的生物催化剂 |
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| EP3578557B1 (en) | 2012-03-23 | 2023-09-20 | Novartis AG | Chemical process for preparing spiroindolones and intermediates thereof |
| WO2013142770A1 (en) | 2012-03-23 | 2013-09-26 | Codexis, Inc. | Biocatalysts and methods for synthesizing derivatives of tryptamine and tryptamine analogs |
| US20150133698A1 (en) | 2012-04-20 | 2015-05-14 | Codexis, Inc. | Production of fatty alcohols from engineered microorganisms |
| WO2013169725A2 (en) | 2012-05-08 | 2013-11-14 | Codexis, Inc. | Biocatalysts and methods for hydroxylation of chemical compounds |
| WO2013170050A1 (en) | 2012-05-11 | 2013-11-14 | Codexis, Inc. | Engineered imine reductases and methods for the reductive amination of ketone and amine compounds |
| WO2014015278A1 (en) | 2012-07-20 | 2014-01-23 | Codexis, Inc. | Production of fatty alcohols from engineered microorganisms |
| WO2014093070A1 (en) | 2012-12-14 | 2014-06-19 | Codexis, Inc. | Modified native beta-ketoacyl-acp synthases and engineered microorganisms |
| SG11201504752YA (en) | 2012-12-21 | 2015-07-30 | Codexis Inc | Engineered biocatalysts and methods for synthesizing chiral amines |
| CN105051180B (zh) | 2013-01-18 | 2020-06-12 | 科德克希思公司 | 用于碳青霉烯类合成的工程化的生物催化剂 |
| US9617573B2 (en) | 2013-02-28 | 2017-04-11 | Codexis, Inc. | Engineered transaminase polypeptides for industrial biocatalysis |
| US10150959B2 (en) | 2013-03-15 | 2018-12-11 | Merck Sharp & Dohme Corp. | Immobilized ketoreductases and process for making and using immobilized ketoreductase |
| WO2014170917A1 (en) * | 2013-04-17 | 2014-10-23 | Council Of Scientific & Industrial Research | Designer cells for enantioselective reduction of ketones and use thereof in efficient production of enantioenriched alcohols |
| CN106232619B (zh) | 2013-11-13 | 2022-09-09 | 科德克希思公司 | 工程化的亚胺还原酶和用于酮和胺化合物的还原胺化的方法 |
| US9133488B2 (en) | 2013-12-30 | 2015-09-15 | University Of Alaska Fairbanks | Synthetic methods and compounds related thereto |
| CN121203988A (zh) | 2014-04-22 | 2025-12-26 | C-乐克塔股份有限公司 | 酮还原酶 |
| DK3256577T3 (da) | 2015-02-10 | 2020-09-14 | Codexis Inc | Ketoreduktase polypeptider til syntesen af chirale forbindelser |
| CN104659287B (zh) * | 2015-03-12 | 2017-05-31 | 京东方科技集团股份有限公司 | 像素界定层及制备方法、显示基板及制备方法、显示装置 |
| CN107531762A (zh) | 2015-05-07 | 2018-01-02 | 科德克希思公司 | 青霉素g酰化酶 |
| KR102382489B1 (ko) | 2016-05-05 | 2022-04-01 | 코덱시스, 인코포레이티드 | 페니실린 ｇ 아실라제 |
| IL263448B2 (en) | 2016-06-09 | 2023-10-01 | Codexis Inc | Biological catalysts and methods for hydroxylation of chemical compounds |
| EP3471744A4 (en) | 2016-06-15 | 2020-07-29 | Codexis, Inc. | REVISED BETA-GLUCOSIDASES AND GLUCOSYLATION PROCESSES |
| WO2018038906A1 (en) | 2016-08-26 | 2018-03-01 | Codexis, Inc. | Engineered imine reductases and methods for the reductive amination of ketone and amine compounds |
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| KR20260006703A (ko) | 2017-02-03 | 2026-01-13 | 테이트 앤드 라일 솔루션스 유에스에이 엘엘씨 | 조작된 글리코실트랜스퍼라제 및 스테비올 글리코시드 글루코실화 방법 |
| JP7045725B2 (ja) | 2017-04-27 | 2022-04-01 | コデクシス， インコーポレイテッド | ケトレダクターゼポリペプチドおよびポリヌクレオチド |
| CA3062550A1 (en) | 2017-05-08 | 2018-11-15 | Codexis, Inc. | Engineered ligase variants |
| WO2018231462A1 (en) | 2017-06-14 | 2018-12-20 | Codexis, Inc. | Engineered transaminase polypeptides for industrial biocatalysis |
| EP3645713A4 (en) | 2017-06-27 | 2021-06-30 | Codexis, Inc. | PENICILLIN-G ACYLASES |
| KR102773542B1 (ko) | 2017-06-30 | 2025-02-25 | 코덱시스, 인코포레이티드 | T7 rna 폴리머라제 변이체 |
| JP2020530267A (ja) | 2017-06-30 | 2020-10-22 | コデクシス， インコーポレイテッド | Ｔ７ ｒｎａポリメラーゼバリアント |
| EP3652328A1 (en) | 2017-07-14 | 2020-05-20 | c-LEcta GmbH | Ketoreductases |
| SG11202003094PA (en) | 2017-11-07 | 2020-05-28 | Codexis Inc | Transglutaminase variants |
| AU2018383752B2 (en) | 2017-12-13 | 2025-01-30 | Codexis, Inc. | Carboxyesterase polypeptides for amide coupling |
| CN111465688A (zh) | 2017-12-13 | 2020-07-28 | 葛兰素史密斯克莱知识产权发展有限公司 | 羧酸酯酶催化剂 |
| GB201802383D0 (en) * | 2018-02-14 | 2018-03-28 | Givaudan Sa | Process |
| ES2975412T3 (es) | 2018-06-21 | 2024-07-05 | Fis Fabbrica Italiana Sintetici Spa | Proceso enzimático para la preparación de droxidopa |
| CN112673105A (zh) | 2018-07-09 | 2021-04-16 | 科德克希思公司 | 工程化脱氧核糖磷酸醛缩酶 |
| AU2019304216B2 (en) | 2018-07-16 | 2022-06-02 | Novartis Ag | Chemical process for preparing phenylpiperidinyl indole derivatives |
| IL319918A (en) | 2018-07-30 | 2025-05-01 | Tate & Lyle Solutions Usa Llc | Engineered glycosyltransferases and methods for glycosylation of steviol glycoside |
| CA3114400A1 (en) | 2018-09-26 | 2020-04-02 | Kalamazoo Holdings, Inc. | Enzymatic process for production of modified hop products |
| EP3870694A4 (en) * | 2018-10-26 | 2022-08-17 | Tami Bar | COMPOSITIONS AND METHODS FOR BIODEGRADING ALCOHOL |
| JP7780186B2 (ja) | 2018-10-29 | 2025-12-04 | コデクシス， インコーポレイテッド | 操作されたｄｎａポリメラーゼバリアント |
| AU2019397401A1 (en) | 2018-12-14 | 2021-06-17 | Codexis, Inc. | Engineered tyrosine ammonia lyase |
| CN113396218B (zh) | 2019-01-15 | 2025-02-18 | 科德克希思公司 | 工程化转氨酶多肽 |
| EP3963057A4 (en) | 2019-05-01 | 2023-06-14 | Codexis, Inc. | MANIPULATED IMINE REDUCTASES AND METHODS FOR THE REDUCTIVE AMINATION OF KETONE AND AMINE COMPOUNDS |
| US12215359B2 (en) | 2019-05-01 | 2025-02-04 | Codexis, Inc. | Engineered glucose dehydrogenases and methods for the reductive amination of ketone and amine compounds |
| AU2020300454A1 (en) | 2019-07-02 | 2021-12-23 | Codexis, Inc. | Engineered sucrose phosphorylase variant enzymes |
| BR112022003705A2 (pt) | 2019-08-30 | 2022-05-24 | Codexis Inc | Lipase recombinante, composição, sequência de polinucleotídeo recombinante, vetor de expressão, composição farmacêutica para o tratamento de insuficiência pancreática, célula hospedeira, métodos para produzir uma lipase recombinante e para tratar e/ou prevenir os sintomas de insuficiência pancreática, e, uso |
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| JP7715045B2 (ja) * | 2019-11-22 | 2025-07-30 | Ｕｂｅ株式会社 | カルボニル還元酵素、これをコードする核酸、及びこれらを利用した光学活性化合物の製造方法 |
| IL293038A (en) | 2019-11-26 | 2022-07-01 | Codexis Inc | Biocatalysts and methods for hydroxylation of chemical compounds |
| EP4103711A4 (en) | 2020-02-04 | 2024-02-28 | Codexis, Inc. | Engineered leucine decarboxylases |
| US11788071B2 (en) | 2020-04-10 | 2023-10-17 | Codexis, Inc. | Engineered transaminase polypeptides |
| JP2023539634A (ja) | 2020-08-28 | 2023-09-15 | コデクシス， インコーポレイテッド | 操作されたアミラーゼバリアント |
| AU2021334371A1 (en) | 2020-08-28 | 2023-03-09 | Codexis, Inc. | Engineered protease variants |
| WO2022066155A1 (en) | 2020-09-24 | 2022-03-31 | Kalamazoo Holdings, Inc. | Enzymatic process for production of modified hop products |
| CN116209754A (zh) | 2020-09-28 | 2023-06-02 | 科德克希思公司 | 用于合成手性胺的工程化生物催化剂及方法 |
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| WO2022133289A2 (en) | 2020-12-18 | 2022-06-23 | Codexis, Inc. | Engineered uridine phosphorylase variant enzymes |
| AU2022279241A1 (en) | 2021-05-21 | 2023-11-30 | Syntis Bio, Inc. | Engineered methionine gamma lyase variants |
| US20250136954A1 (en) * | 2021-08-13 | 2025-05-01 | Codexis, Inc. | Engineered nucleoside deoxyribosyltransferase variant enzymes |
| WO2023064938A1 (en) | 2021-10-15 | 2023-04-20 | Codexis, Inc. | Engineered dna polymerase variants |
| WO2023069865A1 (en) | 2021-10-15 | 2023-04-27 | Codexis, Inc. | Engineered terminal deoxynucleotidyl transferase variants |
| JP2024540358A (ja) | 2021-11-01 | 2024-10-31 | シンティス バイオ，インコーポレイティド | 工学操作ロイシン脱炭酸酵素 |
| EP4577644A1 (en) | 2022-08-26 | 2025-07-02 | Tesaro, Inc. | Biocatalysts and methods thereof |
| TW202440911A (zh) | 2022-12-20 | 2024-10-16 | 瑞士商諾華公司 | 工程化連接酶及其用途 |
| TW202440941A (zh) | 2022-12-20 | 2024-10-16 | 瑞士商諾華公司 | 核酸連接方法 |
| IL322082A (en) | 2023-01-12 | 2025-09-01 | Novartis Ag | Engineered ketoreductase polypeptides |
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| WO2026093943A1 (en) | 2024-10-31 | 2026-05-07 | Novartis Ag | Chemical process for preparing phenylpiperidinyl indole derivatives |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1998035025A1 (en) * | 1997-02-07 | 1998-08-13 | Kaneka Corporation | Novel carbonyl reductase, gene that encodes the same, and method of utilizing these |
| WO1999023242A1 (en) * | 1997-11-04 | 1999-05-14 | Eli Lilly And Company | Ketoreductase gene and protein from yeast |
| WO2003004653A1 (en) * | 2001-07-02 | 2003-01-16 | Kaneka Corporation | Method of modifying enzyme and oxidoreductase variant |
Family Cites Families (13)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB9512837D0 (en) * | 1995-06-23 | 1995-08-23 | Zeneca Ltd | reduction of ketone groups |
| US6531308B2 (en) | 1997-11-04 | 2003-03-11 | Eli Lilly And Company | Ketoreductase gene and protein from yeast |
| AU755543B2 (en) * | 1997-12-19 | 2002-12-12 | Warner-Lambert Export Limited | Process for the synthesis of 1,3-diols |
| WO1999057109A1 (en) * | 1998-04-30 | 1999-11-11 | Kaneka Corporation | Process for producing 6-cyanomethyl-1,3-dioxane-4-acetic acid derivatives |
| HUP0101122A3 (en) * | 1998-08-05 | 2006-02-28 | Kaneka Corp | Process for the preparation of optically active 2-[6-(hydroxymethyl)-1,3-dioxan-4-yl]acetic acid derivatives |
| MXPA01004786A (es) | 1998-11-12 | 2002-09-18 | Larry Kirn | Amplificador de conmutacion de alta exactitud, con referencia multiple. |
| JP2003504070A (ja) * | 1999-07-09 | 2003-02-04 | フォルシュングスツェントルム ユーリッヒ ゲゼルシャフト ミット ベシュレンクテル ハフツング | ケトカルボン酸及びそのエステルの還元のための方法 |
| AU1551701A (en) * | 1999-12-03 | 2001-06-12 | Kaneka Corporation | Novel carbonyl reductase, gene thereof and method of using the same |
| US6492868B2 (en) * | 2000-08-14 | 2002-12-10 | Larry Kirn | Dynamic range enhancement technique |
| CA2474905A1 (en) | 2002-03-18 | 2003-09-25 | Ciba Specialty Chemicals Holding Inc. | Alcohol dehydrogenases with high solvent and temperature stability |
| AU2003258187A1 (en) | 2002-08-09 | 2004-02-25 | Codexis, Inc. | Enzymatic processes for the production of 4-substituted 3-hydroxybutyric acid derivatives |
| WO2005018579A2 (en) * | 2003-08-11 | 2005-03-03 | Codexis, Inc. | Enzymatic processes for the production of 4-substituted 3-hydroxybutyric acid derivatives and vicinal cyano, hydroxy substituted carboxylic acid esters |
| DE102004029112B4 (de) | 2004-06-11 | 2007-06-21 | Julich Chiral Solutions Gmbh | Alkoholdehydrogenase zur stereoselektiven Gewinnung von Hydroxyverbindungen |
-
2004
- 2004-08-11 US US10/916,311 patent/US7629157B2/en active Active
- 2004-08-11 WO PCT/US2004/026655 patent/WO2005017135A1/en not_active Ceased
- 2004-08-11 JP JP2006523448A patent/JP2007502124A/ja active Pending
- 2004-08-11 EP EP04781365A patent/EP1654354A1/en not_active Withdrawn
- 2004-08-11 CA CA002533838A patent/CA2533838A1/en not_active Abandoned
-
2006
- 2006-01-17 IL IL173191A patent/IL173191A/en not_active IP Right Cessation
-
2009
- 2009-10-08 US US12/576,195 patent/US7833767B2/en not_active Expired - Lifetime
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1998035025A1 (en) * | 1997-02-07 | 1998-08-13 | Kaneka Corporation | Novel carbonyl reductase, gene that encodes the same, and method of utilizing these |
| WO1999023242A1 (en) * | 1997-11-04 | 1999-05-14 | Eli Lilly And Company | Ketoreductase gene and protein from yeast |
| WO2003004653A1 (en) * | 2001-07-02 | 2003-01-16 | Kaneka Corporation | Method of modifying enzyme and oxidoreductase variant |
Cited By (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2010539952A (ja) * | 2007-10-01 | 2010-12-24 | コデクシス， インコーポレイテッド | アゼチジノンの生産のためのケトレダクターゼポリペプチド |
| WO2011145211A1 (ja) * | 2010-05-21 | 2011-11-24 | 明治製菓株式会社 | ケトレダクターゼ変異体 |
| US8697409B2 (en) | 2010-05-21 | 2014-04-15 | Meiji Seika Pharma Co., Ltd. | Ketoreductase mutant |
| JP2022536500A (ja) * | 2019-06-13 | 2022-08-17 | アシムケム ラボラトリーズ （ティエンジン） カンパニー リミテッド | ケトレダクターゼ突然変異体及びキラルアルコールの生産方法 |
| JP7375052B2 (ja) | 2019-06-13 | 2023-11-07 | アシムケム ラボラトリーズ （ティエンジン） カンパニー リミテッド | ケトレダクターゼ突然変異体及びキラルアルコールの生産方法 |
| US12173345B2 (en) | 2019-06-13 | 2024-12-24 | Asymchem Laboratories (Tianjin) Co., Ltd. | Ketoreductase mutant and method for producing chiral alcohols |
Also Published As
| Publication number | Publication date |
|---|---|
| WO2005017135A1 (en) | 2005-02-24 |
| US20100028972A1 (en) | 2010-02-04 |
| EP1654354A1 (en) | 2006-05-10 |
| CA2533838A1 (en) | 2005-02-24 |
| US20060195947A1 (en) | 2006-08-31 |
| US7833767B2 (en) | 2010-11-16 |
| IL173191A (en) | 2010-12-30 |
| WO2005017135A8 (en) | 2012-06-14 |
| US7629157B2 (en) | 2009-12-08 |
| IL173191A0 (en) | 2006-06-11 |
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