RU2557411C2 - Модифицированный полипептид, обдадающий гомосеринацетилтрансферазной активностью, и экспрессирующий его микроорганизм - Google Patents
Модифицированный полипептид, обдадающий гомосеринацетилтрансферазной активностью, и экспрессирующий его микроорганизм Download PDFInfo
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- RU2557411C2 RU2557411C2 RU2013133626/10A RU2013133626A RU2557411C2 RU 2557411 C2 RU2557411 C2 RU 2557411C2 RU 2013133626/10 A RU2013133626/10 A RU 2013133626/10A RU 2013133626 A RU2013133626 A RU 2013133626A RU 2557411 C2 RU2557411 C2 RU 2557411C2
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Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2733426C1 (ru) * | 2018-05-28 | 2020-10-01 | СиДжей ЧеилДжеданг Корпорейшн | Модифицированная гомосериндегидрогеназа и способ получения гомосерина или l-аминокислоты, имеющей происхождение от гомосерина, с использованием такой гомосериндегидрогеназы |
| RU2747493C1 (ru) * | 2017-06-30 | 2021-05-05 | СиДжей ЧеилДжеданг Корпорейшн | Новый вариант О-сукцинилгомосеринтрансферазы и способ получения О-сукцинилгомосерина с использованием этого варианта |
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| WO2012135651A1 (en) | 2011-03-31 | 2012-10-04 | The Procter & Gamble Company | Systems, models and methods for identifying and evaluating skin-active agents effective for treating dandruff/seborrheic dermatitis |
| MX2014014898A (es) | 2012-06-06 | 2015-03-04 | Procter & Gamble | Sistemas y metodos de identificacion de agentes cosmeticos para composiciones para el cuidado del cabello/cuero cabelludo. |
| US9834491B2 (en) | 2013-03-20 | 2017-12-05 | Cj Cheiljedang Corporation | Method for producing bio-based homoserine lactone and bio-based organic acid from O-acyl homoserine produced by microorganisms |
| KR101565213B1 (ko) * | 2013-10-23 | 2015-11-03 | 씨제이제일제당 (주) | Ｏ-숙시닐호모세린 생산 미생물 및 이를 이용한 ｏ-숙시닐호모세린의 생산방법 |
| KR101555749B1 (ko) * | 2013-10-23 | 2015-09-25 | 씨제이제일제당 (주) | O-숙시닐호모세린 생산 미생물 및 이를 이용한 o-숙시닐호모세린의 생산방법 |
| AU2014386892B2 (en) * | 2014-03-20 | 2017-11-23 | Cj Cheiljedang Corporation | Method for preparing biobased homoserine lactone hydrochloride and biobased organic acid from microorganism-derived O-acyl homoserine |
| KR101825777B1 (ko) * | 2014-06-05 | 2018-02-07 | 씨제이제일제당 (주) | O-아세틸-호모세린을 생산하는 미생물 및 이를 이용하여 o-아세틸-호모세린을 생산하는 방법 |
| KR101641770B1 (ko) * | 2014-06-23 | 2016-07-22 | 씨제이제일제당 (주) | O-아세틸 호모세린을 생산하는 미생물 및 상기 미생물을 이용하여 o-아세틸 호모세린을 생산하는 방법 |
| PL3305808T3 (pl) | 2015-06-04 | 2022-04-04 | Cj Cheiljedang Corporation | Mikroorganizm wytwarzający o-acetylohomoserynę i sposób wytwarzania o-acetylohomoseryny z jego zastosowaniem |
| US11034985B2 (en) | 2015-11-27 | 2021-06-15 | Evonik Operations Gmbh | Method for producing L-methionine |
| KR20200026874A (ko) * | 2017-06-06 | 2020-03-11 | 지머젠 인코포레이티드 | 대장균 개량을 위한 htp 게놈 공학 플랫폼 |
| EP3647415B1 (en) * | 2017-06-30 | 2025-12-03 | CJ Cheiljedang Corporation | Novel o-succinyl homoserine transferase mutant and method for producing o-succinyl homoserine using same |
| CN110129294B (zh) * | 2018-02-02 | 2021-12-24 | 中国科学院天津工业生物技术研究所 | 高丝氨酸乙酰基转移酶突变体及其宿主细胞和应用 |
| CN112673091B (zh) * | 2018-07-09 | 2025-04-25 | 科德克希思公司 | 工程化泛酸激酶变体酶 |
| KR101996769B1 (ko) | 2018-12-21 | 2019-10-01 | 씨제이제일제당 (주) | 변이형 호모세린 디하이드로게나제 및 이를 이용한 호모세린 또는 호모세린 유래 l-아미노산의 생산 방법 |
| US12146167B2 (en) | 2021-04-01 | 2024-11-19 | Evonik Operations Gmbh | Enzymatic method for producing L-glufosinate and its phosphoesters |
| JP2025531377A (ja) | 2022-09-21 | 2025-09-19 | エボニック オペレーションズ ゲーエムベーハー | Ｌ－グルホシネート及びそのホスホエステルを製造するための酵素法 |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7195897B2 (en) * | 2002-10-24 | 2007-03-27 | Consortium für elektrochemische Industrie GmbH | Feedback-resistant homoserine transsuccinylases having a modified c-terminus |
| RU2008105480A (ru) * | 2005-07-18 | 2009-08-27 | Эвоник Дегусса ГмБх (DE) | Рекомбинантные микроорганизмы, продуцирующие метионин |
| EP2108693A2 (en) * | 2008-04-04 | 2009-10-14 | CJ Cheiljedang Corporation | Microorganism producing L-methionine precursor and the method of producing L-methionone precursor using the microorganism |
Family Cites Families (15)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP4110641B2 (ja) | 1998-11-17 | 2008-07-02 | 味の素株式会社 | 発酵法によるｌ−メチオニンの製造法 |
| DE10239073A1 (de) * | 2002-08-26 | 2004-03-11 | Basf Ag | Verfahren zur fermentativen Herstellung schwefelhaltiger Feinchemikalien |
| MXPA05008857A (es) | 2003-02-18 | 2006-03-09 | Metabolic Explorer Sa | Procedimiento de preparacion de microorganismos evolucionados que permite la creacion o la modificacion de vias metabolicas. |
| US20040199941A1 (en) * | 2003-03-24 | 2004-10-07 | Rice University | Increased bacterial CoA and acetyl-CoA pools |
| BRPI0410861A (pt) | 2003-05-30 | 2006-05-23 | Microbia Inc | métodos e composições para a produção de aminoácidos |
| WO2005111202A1 (en) | 2004-05-12 | 2005-11-24 | Metabolic Explorer | Recombinant enzyme with altered feedback sensitivity |
| KR100620092B1 (ko) | 2004-12-16 | 2006-09-08 | 씨제이 주식회사 | 코리네박테리움 속 세포로부터 유래된 신규한 프로모터서열, 그를 포함하는 발현 카세트 및 벡터, 상기 벡터를포함하는 숙주 세포 및 그를 이용하여 유전자를 발현하는방법 |
| ATE427414T1 (de) | 2005-06-30 | 2009-04-15 | Muhr & Bender Kg | Ventilfederteller mit radialer stutzkraftverstarkung |
| JP2009060791A (ja) * | 2006-03-30 | 2009-03-26 | Ajinomoto Co Inc | Ｌ−アミノ酸生産菌及びｌ−アミノ酸の製造法 |
| PL2808382T3 (pl) * | 2007-04-11 | 2016-09-30 | Kompozycje i sposoby wytwarzania metioniny | |
| KR101136248B1 (ko) * | 2008-04-04 | 2012-04-20 | 씨제이제일제당 (주) | Ｌ-메치오닌 전구체 생산 균주 및 이를 이용한 ｌ-메치오닌 전구체의 생산 방법 |
| US7851180B2 (en) * | 2008-04-04 | 2010-12-14 | Cj Cheiljedang Corporation | Microorganism producing L-methionine precursor and the method of producing L-methionine precursor using the microorganism |
| US8609396B2 (en) * | 2009-08-28 | 2013-12-17 | Cj Cheiljedang Corporation | Microorganism producing O-acetyl-homoserine and the method of producing O-acetyl-homoserine using the microorganism |
| US8283152B2 (en) | 2009-08-28 | 2012-10-09 | Cj Cheiljedang Corporation | Microorganism producing O-acetyl-homoserine and the method of producing O-acetyl-homoserine using the microorganism |
| DK2634193T3 (en) * | 2012-02-29 | 2015-03-02 | Enzypep B V | Condensation of the side-chain protected oligopeptidfragmenter using subtilisins in organic solvents |
-
2011
- 2011-12-21 NO NO11852010A patent/NO2657250T3/no unknown
- 2011-12-21 RU RU2013133626/10A patent/RU2557411C2/ru active
- 2011-12-21 MY MYPI2013002375A patent/MY173933A/en unknown
- 2011-12-21 DK DK11852010.5T patent/DK2657250T3/en active
- 2011-12-21 ES ES11852010.5T patent/ES2650451T3/es active Active
- 2011-12-21 WO PCT/KR2011/009966 patent/WO2012087039A2/ko not_active Ceased
- 2011-12-21 EP EP11852010.5A patent/EP2657250B1/en active Active
- 2011-12-21 KR KR1020110139228A patent/KR101335841B1/ko active Active
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Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7195897B2 (en) * | 2002-10-24 | 2007-03-27 | Consortium für elektrochemische Industrie GmbH | Feedback-resistant homoserine transsuccinylases having a modified c-terminus |
| RU2008105480A (ru) * | 2005-07-18 | 2009-08-27 | Эвоник Дегусса ГмБх (DE) | Рекомбинантные микроорганизмы, продуцирующие метионин |
| EP2108693A2 (en) * | 2008-04-04 | 2009-10-14 | CJ Cheiljedang Corporation | Microorganism producing L-methionine precursor and the method of producing L-methionone precursor using the microorganism |
Non-Patent Citations (1)
| Title |
|---|
| HWANG BJ Corynebacterium glutamicum utilizes both transsulfuration and direct sulfhydrylation pathways for methionine biosynthesis, J Bacteriol. 2002 Mar;184(5):1277-86. КОВАЛЕВА Г.Ю. Регуляция биосинтеза метионина/цистеина в Corynebacterium glutamicum и родственных организмах, Молекулярная биология, т.41, N1, стр.139-150 * |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2747493C1 (ru) * | 2017-06-30 | 2021-05-05 | СиДжей ЧеилДжеданг Корпорейшн | Новый вариант О-сукцинилгомосеринтрансферазы и способ получения О-сукцинилгомосерина с использованием этого варианта |
| RU2733426C1 (ru) * | 2018-05-28 | 2020-10-01 | СиДжей ЧеилДжеданг Корпорейшн | Модифицированная гомосериндегидрогеназа и способ получения гомосерина или l-аминокислоты, имеющей происхождение от гомосерина, с использованием такой гомосериндегидрогеназы |
Also Published As
| Publication number | Publication date |
|---|---|
| EP2657250A4 (en) | 2015-02-18 |
| KR20120070531A (ko) | 2012-06-29 |
| WO2012087039A3 (ko) | 2012-08-23 |
| ES2650451T3 (es) | 2018-01-18 |
| BR112013015991A2 (pt) | 2018-07-10 |
| JP2014502843A (ja) | 2014-02-06 |
| NO2657250T3 (enExample) | 2018-02-03 |
| CN103797027A (zh) | 2014-05-14 |
| WO2012087039A2 (ko) | 2012-06-28 |
| US20130273615A1 (en) | 2013-10-17 |
| EP2657250A2 (en) | 2013-10-30 |
| KR101335841B1 (ko) | 2013-12-02 |
| MY173933A (en) | 2020-02-27 |
| PL2657250T3 (pl) | 2018-02-28 |
| EP2657250B1 (en) | 2017-09-06 |
| DK2657250T3 (en) | 2017-12-11 |
| CN103797027B (zh) | 2017-05-17 |
| JP5758499B2 (ja) | 2015-08-05 |
| RU2013133626A (ru) | 2015-01-27 |
| US9127257B2 (en) | 2015-09-08 |
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