HU218139B - Triptofántermelő mikroorganizmusok, eljárás előállításukra és a mikroorganizmusok alkalmazása triptofán előállítására - Google Patents
Triptofántermelő mikroorganizmusok, eljárás előállításukra és a mikroorganizmusok alkalmazása triptofán előállítására Download PDFInfo
- Publication number
- HU218139B HU218139B HU9500884A HU9500884A HU218139B HU 218139 B HU218139 B HU 218139B HU 9500884 A HU9500884 A HU 9500884A HU 9500884 A HU9500884 A HU 9500884A HU 218139 B HU218139 B HU 218139B
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- Prior art keywords
- tryptophan
- leu
- sera
- int
- glu
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- C12P13/22—Tryptophan; Tyrosine; Phenylalanine; 3,4-Dihydroxyphenylalanine
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12R—INDEXING SCHEME ASSOCIATED WITH SUBCLASSES C12C - C12Q, RELATING TO MICROORGANISMS
- C12R2001/00—Microorganisms ; Processes using microorganisms
- C12R2001/01—Bacteria or Actinomycetales ; using bacteria or Actinomycetales
- C12R2001/15—Corynebacterium
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S435/00—Chemistry: molecular biology and microbiology
- Y10S435/8215—Microorganisms
- Y10S435/822—Microorganisms using bacteria or actinomycetales
- Y10S435/843—Corynebacterium
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S435/00—Chemistry: molecular biology and microbiology
- Y10S435/8215—Microorganisms
- Y10S435/822—Microorganisms using bacteria or actinomycetales
- Y10S435/848—Escherichia
- Y10S435/849—Escherichia coli
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Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
DE4232468A DE4232468A1 (de) | 1992-09-28 | 1992-09-28 | Mikroorganismen für die Produktion von Tryptophan und Verfahren zu ihrer Herstellung |
PCT/EP1993/002588 WO1994008031A1 (de) | 1992-09-28 | 1993-09-23 | Mikroorganismen für die produktion von tryptophan und verfahren zu ihrer herstellung |
Publications (3)
Publication Number | Publication Date |
---|---|
HU9500884D0 HU9500884D0 (en) | 1995-05-29 |
HUT72925A HUT72925A (en) | 1996-06-28 |
HU218139B true HU218139B (hu) | 2000-06-28 |
Family
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Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
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HU9500884A HU218139B (hu) | 1992-09-28 | 1993-09-23 | Triptofántermelő mikroorganizmusok, eljárás előállításukra és a mikroorganizmusok alkalmazása triptofán előállítására |
Country Status (18)
Families Citing this family (103)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
HU220773B1 (hu) | 1990-01-22 | 2002-05-28 | Dekalb Genetics Corporation | Eljárás termő transzgenikus kukoricanövények előállítására |
US6329574B1 (en) | 1990-01-22 | 2001-12-11 | Dekalb Genetics Corporation | High lysine fertile transgenic corn plants |
US6326527B1 (en) | 1993-08-25 | 2001-12-04 | Dekalb Genetics Corporation | Method for altering the nutritional content of plant seed |
US6118047A (en) * | 1993-08-25 | 2000-09-12 | Dekalb Genetic Corporation | Anthranilate synthase gene and method of use thereof for conferring tryptophan overproduction |
GB2304718B (en) * | 1995-09-05 | 2000-01-19 | Degussa | The production of tryptophan by the bacterium escherichia coli |
JP3997631B2 (ja) * | 1998-01-12 | 2007-10-24 | 味の素株式会社 | 発酵法によるl−セリンの製造法 |
RU2206612C2 (ru) * | 1999-11-03 | 2003-06-20 | Закрытое акционерное общество Научно-исследовательский институт "Аджиномото-Генетика" | Способ получения шикимовой кислоты (варианты), штамм бактерий bacillus subtilis - продуцент шикимовой кислоты (варианты) |
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US7160711B2 (en) * | 2001-08-06 | 2007-01-09 | Degussa Ag | Coryneform bacteria which produce chemical compounds I |
AU2002355022B2 (en) | 2001-11-23 | 2007-09-20 | Ajinomoto Co., Inc. | Process for producing L-amino acid using escherichia |
DE10231297A1 (de) * | 2002-07-10 | 2004-02-05 | Forschungszentrum Jülich GmbH | Nukleotidsequenzen coryneformer Bakterien codierend für an der Biosynthese von L-Serin beteiligte Proteine sowie Verfahren zur Herstellung von L-Serin |
RU2273666C2 (ru) * | 2003-02-26 | 2006-04-10 | Закрытое акционерное общество "Научно-исследовательский институт Аджиномото-Генетика" | Способ получения l-аминокислот методом ферментации смеси глюкозы и пентоз |
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DE10331291A1 (de) | 2003-07-10 | 2005-02-17 | Consortium für elektrochemische Industrie GmbH | Varianten der 3-Phosphoglyceratdehydrogenase mit reduzierter Hemmung durch L-Serin und dafür codierende Gene |
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US7300776B2 (en) * | 2004-04-26 | 2007-11-27 | Ajinomoto Co., Inc. | L-amino acid-producing bacterium and a method for producing L-amino acid |
RU2004137198A (ru) * | 2004-12-21 | 2006-06-10 | Закрытое акционерное общество "Научно-исследовательский институт Аджиномото-Генетика" (ЗАО АГРИ) (RU) | СПОСОБ ПОЛУЧЕНИЯ L-АМИНОКИСЛОТ С ИСПОЛЬЗОВАНИЕМ БАКТЕРИИ СЕМЕЙСТВА Enterobacteriaceae, В КОТОРОЙ ИНАКТИВИРОВАН ГЕН yafA |
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JP2009118740A (ja) | 2006-03-03 | 2009-06-04 | Ajinomoto Co Inc | L−アミノ酸の製造法 |
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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 |
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CN101627110B (zh) | 2007-01-22 | 2014-08-13 | 味之素株式会社 | 生产l-氨基酸的微生物和l-氨基酸的生产方法 |
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EP1975241A1 (de) | 2007-03-29 | 2008-10-01 | Evonik Degussa GmbH | Verfahren zur Herstellung von L-Aminosäuren unter Verwendung von verbesserten Stämmen der Familie Enterobacteriaceae |
US8435769B2 (en) * | 2007-04-13 | 2013-05-07 | Monsanto Technology Llc | Use of glyphosate to produce shikimic acid in microorganisms |
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EP2060636A1 (de) | 2007-11-14 | 2009-05-20 | Evonik Degussa GmbH | Verfahren zur Herstellung von L-Aminosäuren unter Verwendung von verbesserten Stämmen der Familie Enterobacteriaceae |
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 |
KR20100120663A (ko) | 2008-01-23 | 2010-11-16 | 아지노모토 가부시키가이샤 | L-아미노산의 제조법 |
RU2008105793A (ru) | 2008-02-19 | 2009-08-27 | Закрытое акционерное общество "Научно-исследовательский институт Аджиномото-Генетика" (ЗАО АГРИ) (RU) | Способ конструирования оперонов, содержащих трансляционно сопряженные гены, бактерия, содержащая такой оперон, способ продукции полезного метаболита и способ мониторинга экспрессии гена |
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RU2593957C2 (ru) * | 2012-01-10 | 2016-08-10 | СиДжей ЧЕИЛДЗЕДАНГ КОРПОРЕЙШН | МИКРООРГАНИЗМ ИЗ РОДА Escherichia, ОБЛАДАЮЩИЙ УСИЛЕННОЙ СПОСОБНОСТЬЮ К ПРОДУКЦИИ L-ТРИПТОФАНА, И СПОСОБ ПОЛУЧЕНИЯ L-ТРИПТОФАНА С ЕГО ИСПОЛЬЗОВАНИЕМ |
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PE20150681A1 (es) | 2013-05-13 | 2015-05-15 | Ajinomoto Kk | Metodo para producir l-aminoacidos |
JP2016165225A (ja) | 2013-07-09 | 2016-09-15 | 味の素株式会社 | 有用物質の製造方法 |
RU2013140115A (ru) | 2013-08-30 | 2015-03-10 | Закрытое акционерное общество "Научно-исследовательский институт Аджиномото-Генетика" (ЗАО "АГРИ") | СПОСОБ ПОЛУЧЕНИЯ L-АМИНОКИСЛОТ С ИСПОЛЬЗОВАНИЕМ БАКТЕРИИ СЕМЕЙСТВА Enterobacteriaceae, В КОТОРОЙ НАРУШЕНА ЭКСПРЕССИЯ КЛАСТЕРА ГЕНОВ znuACB |
JP2016192903A (ja) | 2013-09-17 | 2016-11-17 | 味の素株式会社 | 海藻由来バイオマスからのl−アミノ酸の製造方法 |
WO2015050234A1 (ja) | 2013-10-02 | 2015-04-09 | 味の素株式会社 | アンモニア制御装置およびアンモニア制御方法 |
RU2013144250A (ru) | 2013-10-02 | 2015-04-10 | Закрытое акционерное общество "Научно-исследовательский институт Аджиномото-Генетика" (ЗАО "АГРИ") | СПОСОБ ПОЛУЧЕНИЯ L-АМИНОКИСЛОТ С ИСПОЛЬЗОВАНИЕМ БАКТЕРИИ СЕМЕЙСТВА Enterobacteriaceae, В КОТОРОЙ ОСЛАБЛЕНА ЭКСПРЕССИЯ ГЕНА, КОДИРУЮЩЕГО ФОСФАТНЫЙ ТРАНСПОРТЕР |
PL2886651T3 (pl) | 2013-10-21 | 2018-11-30 | Ajinomoto Co., Inc. | Sposób wytwarzania l-aminokwasu |
BR112016008830B1 (pt) | 2013-10-23 | 2023-02-23 | Ajinomoto Co., Inc | Método para produzir uma substância alvo |
RU2014105547A (ru) | 2014-02-14 | 2015-08-20 | Адзиномото Ко., Инк. | СПОСОБ ПОЛУЧЕНИЯ L-АМИНОКИСЛОТ С ИСПОЛЬЗОВАНИЕМ БАКТЕРИИ СЕМЕЙСТВА ENTEROBACTERIACEAE, ИМЕЮЩЕЙ СВЕРХЭКСПРЕССИРУЕМЫЙ ГЕН yajL |
RU2015120052A (ru) | 2015-05-28 | 2016-12-20 | Аджиномото Ко., Инк. | Способ получения L-аминокислоты с использованием бактерии семейства Enterobacteriaceae, в которой ослаблена экспрессия гена gshA |
WO2017136795A1 (en) * | 2016-02-04 | 2017-08-10 | Synlogic, Inc. | Bacteria engineered to treat diseases associated with tryptophan metabolism |
CN109121422B (zh) | 2016-02-25 | 2021-12-21 | 味之素株式会社 | 使用过表达编码铁输出蛋白基因的肠杆菌科的细菌生产l-氨基酸的方法 |
KR20190003939A (ko) | 2016-03-02 | 2019-01-10 | 피티티지씨 이노베이션 아메리카 코포레이션 | 유전자 조작된 미생물로부터 개선된 뮤콘산 생산 |
JP7066977B2 (ja) | 2017-04-03 | 2022-05-16 | 味の素株式会社 | L-アミノ酸の製造法 |
EP3385275B1 (de) | 2017-04-07 | 2019-10-23 | Evonik Degussa GmbH | Verfahren zur herstellung von aromatischen l-aminosäuren unter verwendung von verbesserten stämmen der familie enterobacteriaceae |
US10858676B2 (en) | 2017-05-22 | 2020-12-08 | Ajinomoto Co., Inc. | Method for producing objective substance |
WO2019110101A1 (de) | 2017-12-06 | 2019-06-13 | Wacker Chemie Ag | Mikroorganismen-stamm und verfahren zur fermentativen herstellung von methylanthranilat |
US11053526B2 (en) | 2018-08-09 | 2021-07-06 | Evonik Operations Gmbh | Process for preparing L amino acids using improved strains of the enterobacteriaceae family |
JP7094494B2 (ja) * | 2018-09-07 | 2022-07-04 | 味の素株式会社 | キョウチクトウ科ニチニチソウ属の形質転換植物体 |
WO2020071538A1 (en) | 2018-10-05 | 2020-04-09 | Ajinomoto Co., Inc. | Method for producing target substance by bacterial fermentation |
JP7491314B2 (ja) | 2019-02-22 | 2024-05-28 | 味の素株式会社 | ydiJ遺伝子を過剰発現する腸内細菌科に属する細菌を用いたL-アミノ酸の製造方法 |
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 |
CN111926002B (zh) * | 2020-09-16 | 2021-01-05 | 中国科学院天津工业生物技术研究所 | TrpE的突变体及其在产L-色氨酸的基因工程菌中的应用 |
WO2023195475A1 (ja) | 2022-04-04 | 2023-10-12 | 味の素株式会社 | 寄生植物を防除する方法 |
Family Cites Families (16)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US3385762A (en) | 1964-06-29 | 1968-05-28 | Chugai Pharmaceutical Co Ltd | Process for the production of l-tryptophan by fermentation |
FR2000641A1 (GUID-C5D7CC26-194C-43D0-91A1-9AE8C70A9BFF.html) | 1968-01-24 | 1969-09-12 | Kyowa Hakko Kogyo Kk | |
JPS5119037B2 (GUID-C5D7CC26-194C-43D0-91A1-9AE8C70A9BFF.html) | 1972-11-16 | 1976-06-14 | ||
JPS575694A (en) | 1980-06-10 | 1982-01-12 | Showa Denko Kk | Production of l-tryptophane |
US4371614A (en) * | 1980-08-22 | 1983-02-01 | Ajinomoto Co., Inc. | E.Coli bacteria carrying recombinant plasmids and their use in the fermentative production of L-tryptophan |
JPS5780398A (en) | 1980-11-05 | 1982-05-19 | Sanraku Inc | Plasmid produced by genetic manipulation, coliform bacillus having the same and preparation of tryptophan with said bacillus |
SU990814A1 (ru) * | 1981-08-12 | 1983-01-23 | Всесоюзный Научно-Исследовательский Институт Генетики И Селекции Промышленных Микроорганизмов "Вниигенетика" | Способ получени L-триптофана |
JPS5889194A (ja) * | 1981-11-24 | 1983-05-27 | Ajinomoto Co Inc | 微生物によるl−トリプトフアンの製造法 |
CA1226541A (en) | 1984-01-13 | 1987-09-08 | Stauffer Chemical Company | Mutant strain deficient in l-serine deaminase activity |
EP0232262A4 (en) * | 1985-08-15 | 1989-09-19 | Stauffer Chemical Co | TRYPTOPHANE GENERATING MICROORGANISM. |
EP0293207A3 (en) * | 1987-05-29 | 1989-11-02 | The Standard Oil Company | Eschericia coli carrying recombinant plasmid for the production of tryptophan |
US4965191A (en) | 1988-02-12 | 1990-10-23 | Eastman Kodak Company | Lower alcohol sulfate wash solution, test kit and method for the determination of an immunological ligand |
JP2656300B2 (ja) * | 1988-04-18 | 1997-09-24 | 協和醗酵工業株式会社 | L−トリプトファンの製造法 |
JP2967996B2 (ja) * | 1989-06-06 | 1999-10-25 | 協和醗酵工業株式会社 | L―トリプトファンの製造法 |
EP0488424B1 (en) | 1990-11-30 | 1997-03-05 | Ajinomoto Co., Inc. | Recombinant DNA sequences encoding feedback inhibition released enzymes, plasmids comprising the recombinant DNA sequences, transformed microorganisms useful in the production of aromatic amino acids, and a process for preparing aromatic amino acids by fermentation |
TW313589B (GUID-C5D7CC26-194C-43D0-91A1-9AE8C70A9BFF.html) * | 1991-12-12 | 1997-08-21 | Wacker Chemie Gmbh |
-
1992
- 1992-09-28 DE DE4232468A patent/DE4232468A1/de not_active Withdrawn
-
1993
- 1993-05-03 TW TW082103438A patent/TW241303B/zh not_active IP Right Cessation
- 1993-09-21 CN CN93117586A patent/CN1065909C/zh not_active Expired - Lifetime
- 1993-09-23 CA CA002145630A patent/CA2145630C/en not_active Expired - Lifetime
- 1993-09-23 HU HU9500884A patent/HU218139B/hu unknown
- 1993-09-23 DE DE59303039T patent/DE59303039D1/de not_active Expired - Lifetime
- 1993-09-23 JP JP6508668A patent/JP3032013B2/ja not_active Expired - Lifetime
- 1993-09-23 BR BR9307125A patent/BR9307125A/pt not_active Application Discontinuation
- 1993-09-23 UA UA95038286A patent/UA32566C2/uk unknown
- 1993-09-23 EP EP93920811A patent/EP0662143B1/de not_active Expired - Lifetime
- 1993-09-23 ES ES93920811T patent/ES2089846T3/es not_active Expired - Lifetime
- 1993-09-23 US US08/411,760 patent/US6180373B1/en not_active Expired - Lifetime
- 1993-09-23 AU AU48190/93A patent/AU673374B2/en not_active Expired
- 1993-09-23 RU RU95113171A patent/RU2111247C1/ru active
- 1993-09-23 SK SK341-95A patent/SK279854B6/sk not_active IP Right Cessation
- 1993-09-23 CZ CZ95667A patent/CZ282396B6/cs not_active IP Right Cessation
- 1993-09-23 WO PCT/EP1993/002588 patent/WO1994008031A1/de active IP Right Grant
- 1993-09-23 KR KR1019950701153A patent/KR950703653A/ko not_active Ceased
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1995
- 1995-03-27 FI FI951439A patent/FI106727B/fi not_active IP Right Cessation
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EP0662143B1 (de) | 1996-06-19 |
FI106727B (fi) | 2001-03-30 |
BR9307125A (pt) | 1999-03-30 |
HU9500884D0 (en) | 1995-05-29 |
JPH07507693A (ja) | 1995-08-31 |
HUT72925A (en) | 1996-06-28 |
CZ66795A3 (en) | 1997-03-12 |
RU2111247C1 (ru) | 1998-05-20 |
WO1994008031A1 (de) | 1994-04-14 |
EP0662143A1 (de) | 1995-07-12 |
CN1065909C (zh) | 2001-05-16 |
KR950703653A (ko) | 1995-09-20 |
UA32566C2 (uk) | 2001-02-15 |
SK34195A3 (en) | 1996-05-08 |
AU673374B2 (en) | 1996-11-07 |
JP3032013B2 (ja) | 2000-04-10 |
CZ282396B6 (cs) | 1997-07-16 |
DE59303039D1 (de) | 1996-07-25 |
SK279854B6 (sk) | 1999-04-13 |
CA2145630A1 (en) | 1994-04-14 |
CN1085950A (zh) | 1994-04-27 |
ES2089846T3 (es) | 1996-10-01 |
DE4232468A1 (de) | 1994-03-31 |
FI951439A0 (fi) | 1995-03-27 |
CA2145630C (en) | 2003-09-09 |
TW241303B (GUID-C5D7CC26-194C-43D0-91A1-9AE8C70A9BFF.html) | 1995-02-21 |
FI951439L (fi) | 1995-03-27 |
US6180373B1 (en) | 2001-01-30 |
AU4819093A (en) | 1994-04-26 |
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