AU2004288134B2 - Improved glucose dehydrogenase polypeptides and related polynucleotides - Google Patents
Improved glucose dehydrogenase polypeptides and related polynucleotides Download PDFInfo
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- AU2004288134B2 AU2004288134B2 AU2004288134A AU2004288134A AU2004288134B2 AU 2004288134 B2 AU2004288134 B2 AU 2004288134B2 AU 2004288134 A AU2004288134 A AU 2004288134A AU 2004288134 A AU2004288134 A AU 2004288134A AU 2004288134 B2 AU2004288134 B2 AU 2004288134B2
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- polypeptide
- seq
- gdh
- naturally occurring
- acid sequence
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Classifications
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- 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
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0006—Oxidoreductases (1.) acting on CH-OH groups as donors (1.1)
-
- 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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/52—Genes encoding for enzymes or proenzymes
-
- 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
- C12N9/14—Hydrolases (3)
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- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
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- Engineering & Computer Science (AREA)
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- Medicinal Chemistry (AREA)
- Physics & Mathematics (AREA)
- Biophysics (AREA)
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| US54565704P | 2004-02-18 | 2004-02-18 | |
| US60/545,657 | 2004-02-18 | ||
| PCT/US2004/026194 WO2005045016A2 (en) | 2003-08-11 | 2004-08-11 | Improved glucose dehydrogenase polypeptides and related polynucleotides |
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| EP1537222B1 (en) * | 2002-08-09 | 2011-03-09 | Codexis, Inc. | Enzymatic processes for the production of 4-substituted 3-hydroxybutyric acid derivatives |
| US7132267B2 (en) | 2002-08-09 | 2006-11-07 | Codexis, Inc. | Enzymatic processes for the production of 4-substituted 3-hydroxybutyric acid derivatives and vicinal cyano, hydroxy substituted carboxylic acid esters |
| JP4494978B2 (ja) | 2002-12-24 | 2010-06-30 | 池田食研株式会社 | 補酵素結合型グルコース脱水素酵素 |
| GB0330016D0 (en) * | 2003-12-24 | 2004-01-28 | Danisco | Method |
| MXPA06001719A (es) | 2003-08-11 | 2006-05-19 | Codexis Inc | Polipeptidos de glucosa deshidrogenasa mejorados, y polinucleotidos relacionados. |
| CA2550800A1 (en) * | 2003-12-24 | 2005-07-21 | Danisco A/S | Methods to produce variant glycolipid acyltransferases and variant glycolipid acyltransferases with enhanced activity towards glycolipids. |
| DE102004059376A1 (de) * | 2004-12-09 | 2006-06-22 | Consortium für elektrochemische Industrie GmbH | GDH-Mutante mit verbesserter chemischer Stabilität |
| WO2006101239A1 (ja) * | 2005-03-25 | 2006-09-28 | Ikeda Food Research Co., Ltd. | 補酵素結合型グルコース脱水素酵素及びこれをコードするポリヌクレオチド |
| DE102005036880A1 (de) * | 2005-08-02 | 2007-02-08 | Julich Chiral Solutions Gmbh | Stereoselektive Synthese von chiralen Diolen |
| EP2066788B1 (en) * | 2006-10-02 | 2014-07-23 | Codexis, Inc. | Compositions and methods for producing stereoisomerically pure statins and synthetic intermediates therefor |
| ATE496124T1 (de) * | 2006-11-14 | 2011-02-15 | Toyo Boseki | Modifizierte flavin-adenin-dinucleotid-abhängige glucose-dehydrogenase |
| JP2009034063A (ja) * | 2007-08-03 | 2009-02-19 | Kao Corp | アルカリプロテアーゼの安定性向上方法 |
| JP2009034062A (ja) * | 2007-08-03 | 2009-02-19 | Kao Corp | アルカリプロテアーゼ |
| WO2009029554A2 (en) | 2007-08-24 | 2009-03-05 | Codexis, Inc. | Improved ketoreductase polypeptides for the stereoselective production of (r)-3-hydroxythiolane |
| EP2093284A1 (de) | 2008-02-19 | 2009-08-26 | F.Hoffmann-La Roche Ag | Stabilisierung von Dehydrogenasen mit stabilen Coenzymen |
| WO2010027710A2 (en) * | 2008-08-27 | 2010-03-11 | Codexis, Inc. | Ketoreductase polypeptides and uses thereof |
| HUE026181T2 (en) | 2008-08-27 | 2016-05-30 | Codexis Inc | Ketoreductase polypeptide for the preparation of 3-aryl-3-hydroxypropanamine from 3-aryl-3-ketopropanamine |
| WO2010025287A2 (en) * | 2008-08-27 | 2010-03-04 | Codexis, Inc. | Ketoreductase polypeptides for the production of 3-aryl-3-hydroxypropanamine from a 3-aryl-3-ketopropanamine |
| SI2329014T1 (sl) | 2008-08-29 | 2015-01-30 | Codexis, Inc. | Polipeptidi ketoreduktaze za stereoselektivno produkcijo (4s)-3(5s)-5(4-fluorofenil)-5-hidroksipentanoil)-4-fenil-1,3-oksazolidin -2-ona |
| CA2750474C (en) | 2009-02-19 | 2017-07-25 | F. Hoffmann-La Roche Ag | Fast reaction kinetics of enzymes having low activity in dry chemistry layers |
| EP2398909B1 (de) | 2009-02-19 | 2015-07-22 | F. Hoffmann-La Roche AG | Schnelle reaktionskinetik von enzymen mit niedriger aktivität in trockenen chemieschichten |
| WO2011005527A2 (en) | 2009-06-22 | 2011-01-13 | Codexis, Inc. | Ketoreductase-mediated stereoselective route to alpha chloroalcohols |
| WO2011022548A2 (en) | 2009-08-19 | 2011-02-24 | Codexis, Inc. | Ketoreductase polypeptides for the preparation of phenylephrine |
| EP2292751A1 (de) | 2009-08-20 | 2011-03-09 | Roche Diagnostics GmbH | Stabilisierung von Enzymen mit stabilen Coenzymen |
| CN102770536B (zh) * | 2009-12-05 | 2014-04-30 | 天野酶株式会社 | 突变酶及其用途 |
| WO2011071982A2 (en) | 2009-12-08 | 2011-06-16 | Codexis, Inc. | Synthesis of prazole compounds |
| PL2513648T3 (pl) | 2009-12-16 | 2015-11-30 | Hoffmann La Roche | Wykrywanie rozkładu enzymów w elemencie testującym przy pomocy kontrolowanego uwalniania chronionego analitu |
| WO2011140219A1 (en) | 2010-05-04 | 2011-11-10 | Codexis, Inc. | Biocatalysts for ezetimibe synthesis |
| HUE037616T2 (hu) | 2010-12-08 | 2018-09-28 | Codexis Inc | Biokatalizátorok és eljárások armodafinil szintéziséhez |
| EP2695939B1 (en) * | 2011-03-30 | 2017-11-01 | Nipro Corporation | Modified glucose dehydrogenase |
| HUE038800T2 (hu) | 2011-04-13 | 2018-11-28 | Codexis Inc | Biokatalitikus eljárás eszlikarbazepin és ennek analógjai elõállítására |
| CN104053771B (zh) | 2011-11-18 | 2016-11-09 | 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 |
| EP2636750A1 (en) | 2012-03-06 | 2013-09-11 | Roche Diagniostics GmbH | Compatible solute ectoine as well as derivatives thereof for enzyme stabilization |
| DK2847214T3 (en) | 2012-05-11 | 2018-03-12 | Codexis Inc | CONSTRUCTED IMINE REDUCTIONS AND PROCEDURES FOR THE REDUCED AMINING OF KETON AND AMINE COMPOUNDS |
| EP2770064A1 (de) | 2013-02-22 | 2014-08-27 | F. Hoffmann-La Roche AG | Hocheffiziente Herstellung von Blutglucose-Teststreifen |
| WO2014150633A1 (en) | 2013-03-15 | 2014-09-25 | Merck Sharp & Dohme Corp. | Immobilized ketoreductases and process for making and using immobilized ketoreductase |
| JP6330028B2 (ja) | 2013-04-17 | 2018-05-23 | カウンシル オブ サイエンティフィック アンド インダストリアル リサーチ | ケトンのエナンチオ選択性還元のためのデザイナー細胞及びエナンチオ濃縮アルコールの効率的製造におけるその使用 |
| EP2994536B1 (en) | 2013-05-08 | 2017-06-14 | Roche Diabetes Care GmbH | Stabilization of enzymes by nicotinic acid |
| DK3068793T3 (da) | 2013-11-13 | 2021-03-22 | Codexis Inc | Manipulerede iminreductaser og fremgangsmåder til den reduktive aminering af keton- og aminforbindelser |
| EP3074524B1 (en) | 2013-11-27 | 2019-11-06 | Roche Diabetes Care GmbH | Composition comprising up-converting phosphors for detecting an analyte |
| EP2927319A1 (en) | 2014-03-31 | 2015-10-07 | Roche Diagnostics GmbH | High load enzyme immobilization by crosslinking |
| EP3131882B1 (en) | 2014-04-14 | 2020-07-15 | Roche Diagnostics GmbH | Phenazinium mediators |
| CN111848578B (zh) | 2014-08-22 | 2023-10-31 | 豪夫迈·罗氏有限公司 | 氧化还原指示剂 |
| SG11201703258PA (en) | 2014-11-25 | 2017-05-30 | Codexis Inc | Engineered imine reductases and methods for the reductive amination of ketone and amine compounds |
| EP3256577B1 (en) | 2015-02-10 | 2020-08-26 | Codexis, Inc. | Ketoreductase polypeptides for the synthesis of chiral compounds |
| PL3523639T3 (pl) | 2016-10-05 | 2025-03-17 | F. Hoffmann-La Roche Ag | Odczynniki wykrywające i układy elektrod do elementów diagnostycznych testów wieloanalitowych oraz sposoby ich zastosowania |
| EP3339431A1 (en) * | 2016-12-22 | 2018-06-27 | Roche Diabetes Care GmbH | Glucose dehydrogenase variants with improved properties |
| SG11202004185PA (en) | 2017-12-13 | 2020-06-29 | Codexis Inc | Carboxyesterase polypeptides for amide coupling |
| EP3587393B1 (en) | 2018-06-21 | 2024-01-17 | F.I.S.- Fabbrica Italiana Sintetici S.p.A. | Enzymatic process for the preparation of droxidopa |
| JP6480629B1 (ja) * | 2018-08-07 | 2019-03-13 | キッコーマン株式会社 | グルコースデヒドロゲナーゼの組換え製造方法 |
| WO2020123563A1 (en) * | 2018-12-10 | 2020-06-18 | The Regents Of The University Of California | Engineered polypeptides that exhibit increased catalytic efficiency for unnatural cofactors and uses thereof |
| JP7677630B2 (ja) * | 2019-05-01 | 2025-05-15 | コデクシス， インコーポレイテッド | 操作されたグルコースデヒドロゲナーゼ、ならびにケトンおよびアミン化合物の還元的アミノ化を行うための方法 |
| EP4649143A1 (en) | 2023-01-12 | 2025-11-19 | Novartis AG | Engineered ketoreductase polypeptides |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2004015132A2 (en) * | 2002-08-09 | 2004-02-19 | Codexis, Inc. | Enzymatic processes for the production of 4-substituted 3-hydroxybutyric acid derivatives |
| US7132267B2 (en) * | 2002-08-09 | 2006-11-07 | Codexis, Inc. | Enzymatic processes for the production of 4-substituted 3-hydroxybutyric acid derivatives and vicinal cyano, hydroxy substituted carboxylic acid esters |
Family Cites Families (17)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE3019450A1 (de) * | 1980-05-21 | 1981-11-26 | Boehringer Mannheim Gmbh, 6800 Mannheim | Verfahren zur gewinnung von glucosedehydrogenase und hierfuer geeigneter mikroorganismus |
| US4542098A (en) * | 1983-05-06 | 1985-09-17 | Institut Francais Du Petrole | Production of glucose dehydrogenase and use of the resultant enzyme in the enzymatic synthesis of L-carnitine |
| US4877733A (en) * | 1986-05-02 | 1989-10-31 | Toyo Jozo Kabushiki Kaisha | Glucose dehydrogenase and its production |
| DE3711881A1 (de) * | 1987-04-08 | 1988-10-27 | Merck Patent Gmbh | Verfahren zur herstellung von glucosedehydrogenase aus bacillus megaterium |
| DE3808531C1 (enExample) * | 1988-03-15 | 1989-07-13 | Eppendorf - Netheler - Hinz Gmbh, 2000 Hamburg, De | |
| JPH0286779A (ja) * | 1988-09-22 | 1990-03-27 | Amano Pharmaceut Co Ltd | 改良型組換えｄｎａ、それを含む形質転換体及びそれを用いた耐熱性グルコースデヒドロゲナーゼの製造法 |
| JP2850515B2 (ja) * | 1990-09-25 | 1999-01-27 | 東洋紡績株式会社 | グルコースデヒドロゲナーゼおよびその製造法 |
| GB9512837D0 (en) * | 1995-06-23 | 1995-08-23 | Zeneca Ltd | reduction of ketone groups |
| WO1999032434A1 (en) * | 1997-12-19 | 1999-07-01 | Warner-Lambert Export Limited | Process for the synthesis of 1,3-diols |
| DE69910562T2 (de) * | 1998-04-30 | 2004-06-17 | Kaneka Corp. | Verfahren zur herstellung von derivaten der 6-cyanomethyl-1,3-dioxan-4-essigsäure |
| CA2305564C (en) * | 1998-08-05 | 2008-06-17 | Kaneka Corporation | Process for the preparation of optically active 2-[6-(hydroxymethyl)-1,3-dioxan-4-yl]acetic acid derivatives |
| KR20010103017A (ko) | 1999-02-19 | 2001-11-17 | 플레믹 크리스티안 | 글루코스 데히드로게나제 융합 단백질 및 발현계에서의그의 용도 |
| WO2001004336A1 (de) * | 1999-07-09 | 2001-01-18 | Forschungszentrum Jülich GmbH | Verfahren zur reduktion von keto-carbonsäuren und deren estern |
| JP4510351B2 (ja) * | 1999-12-03 | 2010-07-21 | 株式会社カネカ | 新規カルボニル還元酵素、その遺伝子、およびその利用法 |
| US6884607B2 (en) | 2000-12-07 | 2005-04-26 | Sumitomo Chemical Company, Limited | Process for producing optically active 4-halo-3-hydroxybutanoate |
| JP4039037B2 (ja) * | 2001-06-11 | 2008-01-30 | 住友化学株式会社 | 還元酵素遺伝子及びその利用 |
| MXPA06001719A (es) | 2003-08-11 | 2006-05-19 | Codexis Inc | Polipeptidos de glucosa deshidrogenasa mejorados, y polinucleotidos relacionados. |
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- 2004-08-11 KR KR1020067002919A patent/KR20060064620A/ko not_active Ceased
- 2004-08-11 JP JP2006523377A patent/JP2007502114A/ja active Pending
- 2004-08-11 US US10/915,927 patent/US7816111B2/en not_active Expired - Lifetime
- 2004-08-11 EP EP04816807.4A patent/EP1660648B1/en not_active Expired - Lifetime
- 2004-08-11 BR BRPI0413492-3A patent/BRPI0413492A/pt not_active IP Right Cessation
- 2004-08-11 AU AU2004288134A patent/AU2004288134B2/en not_active Expired
- 2004-08-11 CA CA002535147A patent/CA2535147A1/en not_active Abandoned
- 2004-08-11 WO PCT/US2004/026194 patent/WO2005045016A2/en not_active Ceased
-
2006
- 2006-01-19 IL IL173260A patent/IL173260A0/en unknown
- 2006-02-02 NO NO20060543A patent/NO20060543L/no not_active Application Discontinuation
-
2010
- 2010-05-28 US US12/790,784 patent/US7939309B2/en not_active Expired - Lifetime
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2004015132A2 (en) * | 2002-08-09 | 2004-02-19 | Codexis, Inc. | Enzymatic processes for the production of 4-substituted 3-hydroxybutyric acid derivatives |
| US7132267B2 (en) * | 2002-08-09 | 2006-11-07 | Codexis, Inc. | Enzymatic processes for the production of 4-substituted 3-hydroxybutyric acid derivatives and vicinal cyano, hydroxy substituted carboxylic acid esters |
Non-Patent Citations (1)
| Title |
|---|
| Manjon et al Biotechnology Letters 2002 Vol 24 pp 1227-32 * |
Also Published As
| Publication number | Publication date |
|---|---|
| NO20060543L (no) | 2006-03-13 |
| AU2004288134A1 (en) | 2005-05-19 |
| WO2005045016A2 (en) | 2005-05-19 |
| US7816111B2 (en) | 2010-10-19 |
| EP1660648B1 (en) | 2013-10-09 |
| US20100304459A1 (en) | 2010-12-02 |
| IL173260A0 (en) | 2006-06-11 |
| KR20060064620A (ko) | 2006-06-13 |
| MXPA06001719A (es) | 2006-05-19 |
| US7939309B2 (en) | 2011-05-10 |
| EP1660648A2 (en) | 2006-05-31 |
| US20050095619A1 (en) | 2005-05-05 |
| CA2535147A1 (en) | 2005-05-19 |
| WO2005045016A3 (en) | 2005-11-10 |
| JP2007502114A (ja) | 2007-02-08 |
| BRPI0413492A (pt) | 2006-10-17 |
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| FGA | Letters patent sealed or granted (standard patent) | ||
| MK14 | Patent ceased section 143(a) (annual fees not paid) or expired |