SK279915B6 - Dna kódujúca aspartokinázu iii, transformovaný mik - Google Patents
Dna kódujúca aspartokinázu iii, transformovaný mik Download PDFInfo
- Publication number
- SK279915B6 SK279915B6 SK819-94A SK81994A SK279915B6 SK 279915 B6 SK279915 B6 SK 279915B6 SK 81994 A SK81994 A SK 81994A SK 279915 B6 SK279915 B6 SK 279915B6
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- Prior art keywords
- mutation
- lysc
- replaced
- dna
- lysine
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- C12N9/1217—Phosphotransferases with a carboxyl group as acceptor (2.7.2)
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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
- C12N9/10—Transferases (2.)
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-
- 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
- C12P13/04—Alpha- or beta- amino acids
- C12P13/08—Lysine; Diaminopimelic acid; Threonine; Valine
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- Health & Medical Sciences (AREA)
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- Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Genetics & Genomics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Biomedical Technology (AREA)
- Molecular Biology (AREA)
- Medicinal Chemistry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
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Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP30002192 | 1992-11-10 | ||
| PCT/JP1993/001640 WO1994011517A1 (en) | 1992-11-10 | 1993-11-10 | Process for producing l-threonine by fermentation |
| CN94102007A CN1071378C (zh) | 1992-11-10 | 1994-02-15 | 发酵生产l-苏氨酸的方法 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| SK81994A3 SK81994A3 (en) | 1995-05-10 |
| SK279915B6 true SK279915B6 (sk) | 1999-05-07 |
Family
ID=36950107
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| SK819-94A SK279915B6 (sk) | 1992-11-10 | 1993-11-10 | Dna kódujúca aspartokinázu iii, transformovaný mik |
Country Status (12)
| Country | Link |
|---|---|
| US (1) | US5661012A (cs) |
| EP (1) | EP0643135B1 (cs) |
| JP (1) | JP3331472B2 (cs) |
| CN (1) | CN1071378C (cs) |
| AT (1) | ATE203769T1 (cs) |
| CZ (1) | CZ285453B6 (cs) |
| DE (1) | DE69330518T2 (cs) |
| DK (1) | DK0643135T3 (cs) |
| ES (1) | ES2158867T3 (cs) |
| RU (1) | RU2113484C1 (cs) |
| SK (1) | SK279915B6 (cs) |
| WO (1) | WO1994011517A1 (cs) |
Families Citing this family (113)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH07155184A (ja) * | 1993-12-08 | 1995-06-20 | Ajinomoto Co Inc | 発酵法によるｌ−リジンの製造法 |
| US5998178A (en) * | 1994-05-30 | 1999-12-07 | Ajinomoto Co., Ltd. | L-isoleucine-producing bacterium and method for preparing L-isoleucine through fermentation |
| HU224158B1 (hu) * | 1995-06-13 | 2005-06-28 | Ajinomoto Co., Inc. | Eljárás L-lizin előállítására fermentálással |
| JP4088982B2 (ja) * | 1996-10-15 | 2008-05-21 | 味の素株式会社 | 発酵法によるｌ−アミノ酸の製造法 |
| MXPA01010151A (es) * | 1999-04-09 | 2002-06-21 | Ajinomoto Kk | Bacterianas que producen l-aminoacido y procedimiento para producir l-aminoacido. |
| US6927046B1 (en) | 1999-12-30 | 2005-08-09 | Archer-Daniels-Midland Company | Increased lysine production by gene amplification using coryneform bacteria |
| BR122013017187B1 (pt) | 2001-02-13 | 2016-03-01 | Ajinomoto Kk | bactéria transgênica produtora de l-aminoácido pertencente ao gênero escherichia, e, método para produzir l-aminoácido |
| US7052883B2 (en) | 2001-04-03 | 2006-05-30 | Degussa Ag | Process for the production of L-amino acids using strains of the family Enterobacteriaceae that contain an attenuated fruR gene |
| DE10116518A1 (de) * | 2001-04-03 | 2002-10-17 | Degussa | Verfahren zur fermentativen Herstellung von L-Aminosäuren unter Verwendung von Stämmen der Familie Enterobacteriaceae |
| AU2002321165A1 (en) * | 2001-07-18 | 2003-03-03 | Degussa Ag | Process for the preparation of l-amino acids using strains of the enterobacteriaceae family which contain an enhanced pfkb gene |
| BRPI0214330B1 (pt) | 2001-11-23 | 2015-06-16 | Ajinomoto Kk | Bactéria produtora de l-aminoácido, e, métodos para a produção de um l-aminoácido e de alquil éster inferior de alfa-l-aspartil-l-fenilalanina |
| DE10210960A1 (de) * | 2002-03-13 | 2003-09-25 | Degussa | Verfahren zur fermentativen Hestellung von L-Aminosäuren unter Verwendung von Stämmen der Familie Enterobacteriaceae |
| ATE399863T1 (de) * | 2002-03-13 | 2008-07-15 | Evonik Degussa Gmbh | Verfahren zur herstellung von l-threonin unter verwendung von stämmen der enterobacteriaceae familie |
| EP1483388B1 (en) * | 2002-03-13 | 2008-11-05 | Evonik Degussa GmbH | Process for the preparation of l-amino acids using strains of the enterobacteriaceae family |
| KR100451299B1 (ko) * | 2002-03-21 | 2004-10-06 | 씨제이 주식회사 | Ｌ―쓰레오닌의 제조방법 |
| DE10231115A1 (de) * | 2002-07-10 | 2004-01-22 | Degussa Ag | Verfahren zur Herstellung von L-Aminosäuren unter Verwendung von Stämmen der Familie Enterbacteriaceae |
| KR100505797B1 (ko) * | 2002-10-11 | 2005-08-04 | 씨제이 주식회사 | 염색체 상의 ｆａｄＲ 유전자가 불활성화된 Ｌ-쓰레오닌 생성 변이 미생물과 이를 이용한 Ｌ-쓰레오닌의 제조방법 |
| BR0304860A (pt) * | 2002-11-11 | 2004-08-31 | Ajinomoto Kk | Método para produzir uma substância alvo pela utilização de uma-bactéria pertencente ao gênero escherichia |
| RU2276687C2 (ru) * | 2003-07-16 | 2006-05-20 | Закрытое акционерное общество "Научно-исследовательский институт Аджиномото-Генетика" | Бактерия, принадлежащая к роду escherichia, - продуцент l-гистидина и способ получения l-гистидина |
| EP1650296B1 (en) * | 2003-07-16 | 2012-04-18 | Ajinomoto Co., Inc. | Mutant serine acetyltransferase and process for producing l-cysteine |
| RU2276688C2 (ru) * | 2003-08-29 | 2006-05-20 | Закрытое акционерное общество "Научно-исследовательский институт Аджиномото-Генетика" | БАКТЕРИЯ, ПРИНАДЛЕЖАЩАЯ К РОДУ Escherichia,- ПРОДУЦЕНТ L-ГИСТИДИНА И СПОСОБ ПОЛУЧЕНИЯ L-ГИСТИДИНА |
| US20050176033A1 (en) * | 2003-11-10 | 2005-08-11 | Klyachko Elena V. | Mutant phosphoribosylpyrophosphate synthetase and method for producing L-histidine |
| RU2275424C2 (ru) * | 2003-12-05 | 2006-04-27 | Закрытое акционерное общество "Научно-исследовательский институт Аджиномото-Генетика" (ЗАО АГРИ) | Способ получения l-треонина с использованием бактерий, принадлежащих к роду escherichia |
| KR100608085B1 (ko) * | 2004-02-05 | 2006-08-02 | 씨제이 주식회사 | ｔｙｒＲ 유전자가 불활성화된 Ｌ-쓰레오닌 생성 미생물,그를 제조하는 방법 및 상기 미생물을 이용한Ｌ-쓰레오닌의 제조방법 |
| US20050181488A1 (en) * | 2004-02-12 | 2005-08-18 | Akhverdian Valery Z. | Method for producing L-threonine using bacteria belonging to the genus Escherichia |
| US7915018B2 (en) * | 2004-10-22 | 2011-03-29 | Ajinomoto Co., Inc. | Method for producing L-amino acids using bacteria of the Enterobacteriaceae family |
| US20070212764A1 (en) * | 2005-01-19 | 2007-09-13 | Ptitsyn Leonid R | Method for producing l-amino acids using bacterium of the enterobacteriaceae family |
| JP2007037533A (ja) * | 2005-06-29 | 2007-02-15 | Ajinomoto Co Inc | Ｌ−スレオニンの製造法 |
| RU2304615C2 (ru) * | 2005-10-12 | 2007-08-20 | Закрытое акционерное общество "Научно-исследовательский институт Аджиномото-Генетика" (ЗАО АГРИ) | Способ получения l-аминокислот с использованием бактерий, принадлежащих к роду escherichia |
| JP2007185184A (ja) * | 2005-12-16 | 2007-07-26 | Ajinomoto Co Inc | Ｌ−アミノ酸生産菌及びｌ−アミノ酸の製造法 |
| RU2312893C2 (ru) * | 2006-01-17 | 2007-12-20 | Закрытое акционерное общество "Научно-исследовательский институт Аджиномото-Генетика" (ЗАО АГРИ) | СПОСОБ ПОЛУЧЕНИЯ L-АМИНОКИСЛОТ С ИСПОЛЬЗОВАНИЕМ БАКТЕРИИ, ПРИНАДЛЕЖАЩЕЙ К РОДУ Escherichia |
| EP1976994A1 (en) * | 2006-01-26 | 2008-10-08 | Ajinomoto Co., Inc. | A method for producing an l-amino acid using a bacterium of enterobacteriaceae family with attenuated expression of the aldh gene |
| WO2007086618A1 (en) | 2006-01-30 | 2007-08-02 | Ajinomoto Co., Inc. | L-amino acid producing bacterium and method of producing l-amino acid |
| JP2009095237A (ja) * | 2006-02-02 | 2009-05-07 | Ajinomoto Co Inc | Ｌ−アミノ酸の製造法 |
| JP2009118740A (ja) * | 2006-03-03 | 2009-06-04 | Ajinomoto Co Inc | Ｌ−アミノ酸の製造法 |
| EP2184348B1 (en) | 2006-03-23 | 2013-11-27 | Ajinomoto Co., Inc. | A method for producing an L-amino acid using bacterium of the Enterobacteriaceae family with attenuated expression of a gene coding for small RNA |
| 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 |
| RU2338782C2 (ru) * | 2006-04-13 | 2008-11-20 | Закрытое акционерное общество "Научно-исследовательский институт Аджиномото-Генетика" (ЗАО АГРИ) | Способ получения l-треонина с использованием бактерии, принадлежащей к роду escherichia, модифицированной таким образом, что в ней нарушена способность к образованию ворсинок типа "керли" |
| RU2333953C2 (ru) * | 2006-04-18 | 2008-09-20 | Закрытое акционерное общество "Научно-исследовательский институт Аджиномото-Генетика" (ЗАО АГРИ) | СПОСОБ ПОЛУЧЕНИЯ L-ТРЕОНИНА С ИСПОЛЬЗОВАНИЕМ БАКТЕРИИ, ПРИНАДЛЕЖАЩЕЙ К РОДУ Escherichia, В КОТОРОЙ ИНАКТИВИРОВАН КЛАСТЕР ГЕНОВ sfmACDFH-fimZ ИЛИ ГЕН fimZ |
| WO2007119890A1 (en) | 2006-04-18 | 2007-10-25 | Ajinomoto Co., Inc. | A METHOD FOR PRODUCING AN L-AMINO ACID USING A BACTERIUM OF THE ENTEROBACTERIACEAE FAMILY WITH ATTENUATED EXPRESSION OF THE sfmACDFH-fimZ CLUSTER OR THE fimZ GENE |
| JP2009165355A (ja) * | 2006-04-28 | 2009-07-30 | Ajinomoto Co Inc | Ｌ−アミノ酸を生産する微生物及びｌ−アミノ酸の製造法 |
| RU2337960C2 (ru) * | 2006-06-01 | 2008-11-10 | Закрытое акционерное общество "Научно-исследовательский институт Аджиномото-Генетика" (ЗАО АГРИ) | СПОСОБ ПОЛУЧЕНИЯ L-ТРЕОНИНА И L-АРГИНИНА С ИСПОЛЬЗОВАНИЕМ БАКТЕРИИ, ПРИНАДЛЕЖАЩЕЙ К РОДУ Escherichia, В КОТОРОЙ ИНАКТИВИРОВАН КЛАСТЕР ГЕНОВ yehABCDE |
| RU2337961C2 (ru) * | 2006-07-04 | 2008-11-10 | Закрытое акционерное общество "Научно-исследовательский институт Аджиномото-Генетика" (ЗАО АГРИ) | СПОСОБ ПОЛУЧЕНИЯ L-ТРЕОНИНА С ИСПОЛЬЗОВАНИЕМ БАКТЕРИИ, ПРИНАДЛЕЖАЩЕЙ К РОДУ Escherichia, В КОТОРОЙ ИНАКТИВИРОВАН ОПЕРОН rspAB |
| RU2337962C2 (ru) * | 2006-07-04 | 2008-11-10 | Закрытое акционерное общество "Научно-исследовательский институт Аджиномото-Генетика" (ЗАО АГРИ) | СПОСОБ ПОЛУЧЕНИЯ L-ТРЕОНИНА С ИСПОЛЬЗОВАНИЕМ БАКТЕРИИ, ПРИНАДЛЕЖАЩЕЙ К РОДУ Escherichia, В КОТОРОЙ ИНАКТИВИРОВАН КЛАСТЕР ГЕНОВ yraH-R |
| BRPI0715584B8 (pt) * | 2006-07-19 | 2017-02-21 | Ajinomoto Kk | método para produzir um l-aminoácido |
| RU2355763C2 (ru) | 2006-09-13 | 2009-05-20 | Закрытое акционерное общество "Научно-исследовательский институт Аджиномото-Генетика" (ЗАО АГРИ) | Мутантная ацетолактатсинтаза и способ продукции разветвленных l-аминокислот |
| JP2010017081A (ja) * | 2006-10-10 | 2010-01-28 | Ajinomoto Co Inc | Ｌ−アミノ酸の製造法 |
| WO2008072761A2 (en) * | 2006-12-11 | 2008-06-19 | Ajinomoto Co., Inc. | Method for producing an l-amino acid |
| RU2006143864A (ru) | 2006-12-12 | 2008-06-20 | Закрытое акционерное общество "Научно-исследовательский институт Аджиномото-Генетика" (ЗАО АГРИ) (RU) | СПОСОБ ПОЛУЧЕНИЯ L-АМИНОКИСЛОТ С ИСПОЛЬЗОВАНИЕМ БАКТЕРИИ СЕМЕЙСТВА ENTEROBACTERIACEAE, В КОТОРОЙ ОСЛАБЛЕНА ЭКСПРЕССИЯ ГЕНОВ cynT, cynS, cynX, ИЛИ cynR, ИЛИ ИХ КОМБИНАЦИИ |
| RU2006145712A (ru) * | 2006-12-22 | 2008-06-27 | Закрытое акционерное общество "Научно-исследовательский институт Аджиномото-Генетика" (ЗАО АГРИ) (RU) | Способ получения l-аминокислот методом ферментации с использованием бактерий, обладающих повышенной способностью к утилизации глицерина |
| JP2010088301A (ja) | 2007-02-01 | 2010-04-22 | Ajinomoto Co Inc | Ｌ−アミノ酸の製造法 |
| KR100868330B1 (ko) | 2007-02-01 | 2008-11-12 | 씨제이제일제당 (주) | 엘-쓰레오닌의 제조방법 |
| US8563313B2 (en) * | 2007-02-13 | 2013-10-22 | Washington State University Research Foundation | Macrophage cell-lines for propagation of porcine reproductive and respiratory syndrome virus |
| JP2010110217A (ja) * | 2007-02-22 | 2010-05-20 | Ajinomoto Co Inc | Ｌ−アミノ酸生産菌及びｌ−アミノ酸の製造法 |
| JP2010263790A (ja) * | 2007-09-04 | 2010-11-25 | Ajinomoto Co Inc | アミノ酸生産微生物及びアミノ酸の製造法 |
| RU2395579C2 (ru) * | 2007-12-21 | 2010-07-27 | Закрытое акционерное общество "Научно-исследовательский институт Аджиномото-Генетика" (ЗАО АГРИ) | СПОСОБ ПОЛУЧЕНИЯ L-АМИНОКИСЛОТЫ С ИСПОЛЬЗОВАНИЕМ БАКТЕРИИ, ПРИНАДЛЕЖАЩЕЙ К РОДУ Escherichia |
| RU2396336C2 (ru) | 2007-09-27 | 2010-08-10 | Закрытое акционерное общество "Научно-исследовательский институт Аджиномото-Генетика" (ЗАО АГРИ) | СПОСОБ ПОЛУЧЕНИЯ АМИНОКИСЛОТ С ИСПОЛЬЗОВАНИЕМ БАКТЕРИИ, ПРИНАДЛЕЖАЩЕЙ К РОДУ Escherichia |
| JP2011067095A (ja) | 2008-01-10 | 2011-04-07 | Ajinomoto Co Inc | 発酵法による目的物質の製造法 |
| BRPI0906795A2 (pt) | 2008-01-23 | 2015-08-18 | Ajinomoto Kk | Método para produzir um l-aminoácido |
| RU2408731C2 (ru) * | 2008-06-17 | 2011-01-10 | Закрытое акционерное общество "Научно-исследовательский институт Аджиномото-Генетика" (ЗАО АГРИ) | Способ продукции полезного метаболита |
| CN102076856B (zh) * | 2008-06-30 | 2014-12-31 | 孟山都技术公司 | 用于提高植物中的氨基酸含量的组合物和方法 |
| KR101627095B1 (ko) | 2008-09-08 | 2016-06-03 | 아지노모토 가부시키가이샤 | Ｌ-아미노산을 생산하는 미생물 및 ｌ-아미노산의 제조법 |
| JP5504608B2 (ja) * | 2008-10-23 | 2014-05-28 | 東レ株式会社 | １，５−ペンタンジアミンの製造方法 |
| JP2012029565A (ja) | 2008-11-27 | 2012-02-16 | Ajinomoto Co Inc | Ｌ−アミノ酸の製造法 |
| RU2008148283A (ru) | 2008-12-09 | 2010-06-20 | Закрытое акционерное общество "Научно-исследовательский институт Аджиномото-Генетика" (ЗАО АГРИ) (RU) | СПОСОБ ПОЛУЧЕНИЯ L-АРГИНИНА С ИСПОЛЬЗОВАНИЕМ БАКТЕРИИ СЕМЕЙСТВА ENTEROBACTERIACEAE, В КОТОРОЙ ОСЛАБЛЕНА ЭКСПРЕССИЯ ГЕНА artI |
| JP2010142200A (ja) | 2008-12-22 | 2010-07-01 | Ajinomoto Co Inc | Ｌ−リジンの製造法 |
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| JP5521347B2 (ja) | 2009-02-16 | 2014-06-11 | 味の素株式会社 | Ｌ−アミノ酸生産菌及びｌ−アミノ酸の製造法 |
| WO2011013707A1 (ja) | 2009-07-29 | 2011-02-03 | 味の素株式会社 | Ｌ-アミノ酸の製造法 |
| JP2012196144A (ja) | 2009-08-03 | 2012-10-18 | Ajinomoto Co Inc | ビブリオ属細菌を用いたｌ−リジンの製造法 |
| JP2012223092A (ja) | 2009-08-28 | 2012-11-15 | Ajinomoto Co Inc | Ｌ−アミノ酸の製造法 |
| RU2009136544A (ru) | 2009-10-05 | 2011-04-10 | Закрытое акционерное общество "Научно-исследовательский институт "Аджиномото-Генетика" (ЗАО АГРИ) (RU) | Способ получения l-цистеина с использованием бактерии семейства enterobacteriaceae |
| JP2013013329A (ja) | 2009-11-06 | 2013-01-24 | Ajinomoto Co Inc | Ｌ−アミノ酸の製造法 |
| KR101270149B1 (ko) | 2009-11-25 | 2013-06-04 | 한국과학기술원 | Ｌ이소루신 고생성능을 가지는 변이미생물 및 이의 제조방법 |
| RU2010101135A (ru) | 2010-01-15 | 2011-07-20 | Закрытое акционерное общество "Научно-исследовательский институт "Аджиномото-Генетика" (ЗАО АГРИ) (RU) | Бактерия семейства enterobacteriaceae - продуцент l-аспартата или метаболитов, производных l-аспартата, и способ получения l-аспартата или метаболитов, производных l-аспартата |
| RU2460793C2 (ru) | 2010-01-15 | 2012-09-10 | Закрытое акционерное общество "Научно-исследовательский институт "Аджиномото-Генетика" (ЗАО АГРИ) | Способ получения l-аминокислот с использованием бактерий семейства enterobacteriaceae |
| JP2013074795A (ja) | 2010-02-08 | 2013-04-25 | Ajinomoto Co Inc | 変異型ｒｐｓＡ遺伝子及びＬ−アミノ酸の製造法 |
| RU2471868C2 (ru) | 2010-02-18 | 2013-01-10 | Закрытое акционерное общество "Научно-исследовательский институт "Аджиномото-Генетика" (ЗАО АГРИ) | Мутантная аденилатциклаза, днк, кодирующая ее, бактерия семейства enterobacteriaceae, содержащая указанную днк, и способ получения l-аминокислот |
| EP2363489A1 (en) * | 2010-03-03 | 2011-09-07 | Technische Universität Hamburg-Harburg | Enzyme Aspartokinase III having a reduced L-lysine feedback inhibition |
| RU2471870C2 (ru) | 2010-06-03 | 2013-01-10 | Закрытое акционерное общество "Научно-исследовательский институт "Аджиномото-Генетика" (ЗАО АГРИ) | СПОСОБ ПОЛУЧЕНИЯ L-АРГИНИНА И L-ЦИТРУЛЛИНА С ИСПОЛЬЗОВАНИЕМ БАКТЕРИИ СЕМЕЙСТВА ENTEROBACTERIACEAE, В КОТОРОЙ ОСЛАБЛЕНА ЭКСПРЕССИЯ ГЕНА pepA |
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| JP2014036576A (ja) | 2010-12-10 | 2014-02-27 | Ajinomoto Co Inc | Ｌ−アミノ酸の製造法 |
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| JP2015013812A (ja) | 2011-11-01 | 2015-01-22 | 味の素株式会社 | 植物ウイルスの感染抑制剤およびそれを用いた植物ウイルス感染抑制方法 |
| RU2012112651A (ru) | 2012-04-02 | 2013-10-10 | Закрытое акционерное общество "Научно-исследовательский институт Аджиномото-Генетика" (ЗАО "АГРИ") | САМОИНДУЦИРУЕМАЯ ЭКСПРЕССИОННАЯ СИСТЕМА И ЕЕ ПРИМЕНЕНИЕ ДЛЯ ПОЛУЧЕНИЯ ПОЛЕЗНЫХ МЕТАБОЛИТОВ С ПОМОЩЬЮ БАКТЕРИИ СЕМЕЙСТВА Enterobacteriaceae |
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| CN103667165B (zh) * | 2012-09-12 | 2017-05-31 | 中国科学院上海生命科学研究院 | 高产l‑赖氨酸的生产菌株及其应用 |
| CN108486082A (zh) | 2012-10-18 | 2018-09-04 | 中粮生物化学（安徽）股份有限公司 | 天冬氨酸激酶iii突变体及其宿主细胞和应用 |
| CN103215286B (zh) * | 2012-11-12 | 2015-11-25 | 江南大学 | 用于发酵生产l-赖氨酸的重组dna、菌株及其应用 |
| RU2013118637A (ru) | 2013-04-23 | 2014-10-27 | Закрытое акционерное общество "Научно-исследовательский институт Аджиномото-Генетика" (ЗАО "АГРИ") | СПОСОБ ПОЛУЧЕНИЯ L-АМИНОКИСЛОТ С ИСПОЛЬЗОВАНИЕМ БАКТЕРИИ СЕМЕЙСТВА ENTEROBACTERIACEAE, В КОТОРОЙ РАЗРЕГУЛИРОВАН ГЕН yjjK |
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| JP7066977B2 (ja) | 2017-04-03 | 2022-05-16 | 味の素株式会社 | Ｌ－アミノ酸の製造法 |
| KR102011994B1 (ko) * | 2017-06-30 | 2019-08-20 | 씨제이제일제당 주식회사 | 신규한 아스파토키나제 변이체 및 이를 이용한 l-아미노산의 제조방법 |
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| WO2020204179A1 (en) | 2019-04-05 | 2020-10-08 | Ajinomoto Co., Inc. | Method of producing l-amino acids |
| JP7655312B2 (ja) | 2019-09-25 | 2025-04-02 | 味の素株式会社 | 細菌の発酵によるｌ－アミノ酸の製造方法 |
| IL316086A (en) | 2022-04-04 | 2024-12-01 | Ajinomoto Kk | Method for controlling parasitic plants |
Family Cites Families (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| SU943282A1 (ru) * | 1979-07-13 | 1982-07-15 | Всесоюзный научно-исследовательский институт генетики и селекции промышленных микроорганизмов | Способ получени L-треонина |
| JPS55131397A (en) * | 1979-04-02 | 1980-10-13 | Ajinomoto Co Inc | Preparation of l-threonine by fermentation |
| JPS5931691A (ja) * | 1982-08-16 | 1984-02-20 | Ajinomoto Co Inc | 発酵法によるｌ−スレオニンの製造法 |
| DE243496T1 (de) * | 1985-08-26 | 1988-06-30 | Toray Industries, Inc., Tokio/Tokyo | Verfahren zur herstellung von l-threonin durch gaerung. |
| FR2627508B1 (fr) | 1988-02-22 | 1990-10-05 | Eurolysine | Procede pour l'integration d'un gene choisi sur le chromosome d'une bacterie et bacterie obtenue par ledit procede |
| DE3891417C5 (de) * | 1988-10-25 | 2006-01-05 | Ajinomoto Co., Inc. | Verfahren zur Veränderung eines L-Threonin produzierenden Mikroorganismus und Verwendung eines so erhaltenen Mikroorganismus zur Herstellung von L-Threonin |
| CA2132414C (en) * | 1992-03-19 | 2009-01-27 | Saverio Carl Falco | Nucleic acid fragments and methods for increasing the lysine and threonine content of the seeds of plants |
-
1993
- 1993-11-10 EP EP93924805A patent/EP0643135B1/en not_active Expired - Lifetime
- 1993-11-10 JP JP51192494A patent/JP3331472B2/ja not_active Expired - Fee Related
- 1993-11-10 DE DE69330518T patent/DE69330518T2/de not_active Expired - Lifetime
- 1993-11-10 CZ CZ941658A patent/CZ285453B6/cs not_active IP Right Cessation
- 1993-11-10 ES ES93924805T patent/ES2158867T3/es not_active Expired - Lifetime
- 1993-11-10 SK SK819-94A patent/SK279915B6/sk not_active IP Right Cessation
- 1993-11-10 WO PCT/JP1993/001640 patent/WO1994011517A1/ja active IP Right Grant
- 1993-11-10 DK DK93924805T patent/DK0643135T3/da active
- 1993-11-10 RU RU94035744A patent/RU2113484C1/ru not_active IP Right Cessation
- 1993-11-10 US US08/256,136 patent/US5661012A/en not_active Expired - Lifetime
- 1993-11-10 AT AT93924805T patent/ATE203769T1/de not_active IP Right Cessation
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Also Published As
| Publication number | Publication date |
|---|---|
| SK81994A3 (en) | 1995-05-10 |
| EP0643135A1 (en) | 1995-03-15 |
| ES2158867T3 (es) | 2001-09-16 |
| DE69330518D1 (de) | 2001-09-06 |
| CN1071378C (zh) | 2001-09-19 |
| ATE203769T1 (de) | 2001-08-15 |
| RU94035744A (ru) | 1996-10-20 |
| EP0643135A4 (en) | 1997-04-09 |
| WO1994011517A1 (en) | 1994-05-26 |
| JP3331472B2 (ja) | 2002-10-07 |
| EP0643135B1 (en) | 2001-08-01 |
| CZ165894A3 (en) | 1994-12-15 |
| DK0643135T3 (da) | 2001-10-15 |
| DE69330518T2 (de) | 2002-05-08 |
| CZ285453B6 (cs) | 1999-08-11 |
| RU2113484C1 (ru) | 1998-06-20 |
| CN1107179A (zh) | 1995-08-23 |
| US5661012A (en) | 1997-08-26 |
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