RU2003677C1 - Strain of bacterium escherichia coli - a producer of l-histidine - Google Patents
Strain of bacterium escherichia coli - a producer of l-histidineInfo
- Publication number
- RU2003677C1 RU2003677C1 SU5034791A RU2003677C1 RU 2003677 C1 RU2003677 C1 RU 2003677C1 SU 5034791 A SU5034791 A SU 5034791A RU 2003677 C1 RU2003677 C1 RU 2003677C1
- Authority
- RU
- Russia
- Prior art keywords
- histidine
- strain
- producer
- escherichia coli
- bacterium escherichia
- Prior art date
Links
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 title description 16
- 241000588724 Escherichia coli Species 0.000 title description 3
- 229960002885 histidine Drugs 0.000 description 14
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 13
- 239000002609 medium Substances 0.000 description 8
- UCSJYZPVAKXKNQ-HZYVHMACSA-N streptomycin Chemical compound CN[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1O[C@@H]1[C@](C=O)(O)[C@H](C)O[C@H]1O[C@@H]1[C@@H](NC(N)=N)[C@H](O)[C@@H](NC(N)=N)[C@H](O)[C@H]1O UCSJYZPVAKXKNQ-HZYVHMACSA-N 0.000 description 8
- 239000012531 culture fluid Substances 0.000 description 7
- 238000009825 accumulation Methods 0.000 description 6
- 230000035772 mutation Effects 0.000 description 6
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 4
- 108020004566 Transfer RNA Proteins 0.000 description 4
- 238000000855 fermentation Methods 0.000 description 4
- 230000004151 fermentation Effects 0.000 description 4
- 229960005322 streptomycin Drugs 0.000 description 4
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 230000026683 transduction Effects 0.000 description 3
- 238000010361 transduction Methods 0.000 description 3
- 101150017621 truA gene Proteins 0.000 description 3
- MHUWZNTUIIFHAS-XPWSMXQVSA-N 9-octadecenoic acid 1-[(phosphonoxy)methyl]-1,2-ethanediyl ester Chemical compound CCCCCCCC\C=C\CCCCCCCC(=O)OCC(COP(O)(O)=O)OC(=O)CCCCCCC\C=C\CCCCCCCC MHUWZNTUIIFHAS-XPWSMXQVSA-N 0.000 description 2
- QGZKDVFQNNGYKY-UHFFFAOYSA-O Ammonium Chemical compound [NH4+] QGZKDVFQNNGYKY-UHFFFAOYSA-O 0.000 description 2
- DJHGAFSJWGLOIV-UHFFFAOYSA-K Arsenate3- Chemical compound [O-][As]([O-])([O-])=O DJHGAFSJWGLOIV-UHFFFAOYSA-K 0.000 description 2
- CSNNHWWHGAXBCP-UHFFFAOYSA-L Magnesium sulfate Chemical compound [Mg+2].[O-][S+2]([O-])([O-])[O-] CSNNHWWHGAXBCP-UHFFFAOYSA-L 0.000 description 2
- 229940000489 arsenate Drugs 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 239000002207 metabolite Substances 0.000 description 2
- 229910052757 nitrogen Inorganic materials 0.000 description 2
- PTJWIQPHWPFNBW-GBNDHIKLSA-N pseudouridine Chemical compound O[C@@H]1[C@H](O)[C@@H](CO)O[C@H]1C1=CNC(=O)NC1=O PTJWIQPHWPFNBW-GBNDHIKLSA-N 0.000 description 2
- 101150098466 rpsL gene Proteins 0.000 description 2
- 229940047047 sodium arsenate Drugs 0.000 description 2
- 230000002269 spontaneous effect Effects 0.000 description 2
- 238000013518 transcription Methods 0.000 description 2
- 230000035897 transcription Effects 0.000 description 2
- LWIHDJKSTIGBAC-UHFFFAOYSA-K tripotassium phosphate Chemical compound [K+].[K+].[K+].[O-]P([O-])([O-])=O LWIHDJKSTIGBAC-UHFFFAOYSA-K 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- -1 7-aqueous 1.125 Chemical compound 0.000 description 1
- 108010058756 ATP phosphoribosyltransferase Proteins 0.000 description 1
- 108020005098 Anticodon Proteins 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 241000702191 Escherichia virus P1 Species 0.000 description 1
- PWHULOQIROXLJO-UHFFFAOYSA-N Manganese Chemical compound [Mn] PWHULOQIROXLJO-UHFFFAOYSA-N 0.000 description 1
- 108010076504 Protein Sorting Signals Proteins 0.000 description 1
- 229930185560 Pseudouridine Natural products 0.000 description 1
- PTJWIQPHWPFNBW-UHFFFAOYSA-N Pseudouridine C Natural products OC1C(O)C(CO)OC1C1=CNC(=O)NC1=O PTJWIQPHWPFNBW-UHFFFAOYSA-N 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 101100478714 Streptomyces griseus strR gene Proteins 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
- JZRWCGZRTZMZEH-UHFFFAOYSA-N Thiamine Natural products CC1=C(CCO)SC=[N+]1CC1=CN=C(C)N=C1N JZRWCGZRTZMZEH-UHFFFAOYSA-N 0.000 description 1
- DRTQHJPVMGBUCF-XVFCMESISA-N Uridine Chemical group O[C@@H]1[C@H](O)[C@@H](CO)O[C@H]1N1C(=O)NC(=O)C=C1 DRTQHJPVMGBUCF-XVFCMESISA-N 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- WGDUUQDYDIIBKT-UHFFFAOYSA-N beta-Pseudouridine Natural products OC1OC(CN2C=CC(=O)NC2=O)C(O)C1O WGDUUQDYDIIBKT-UHFFFAOYSA-N 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 101150032598 hisG gene Proteins 0.000 description 1
- 239000002054 inoculum Substances 0.000 description 1
- 229910052816 inorganic phosphate Inorganic materials 0.000 description 1
- BAUYGSIQEAFULO-UHFFFAOYSA-L iron(2+) sulfate (anhydrous) Chemical compound [Fe+2].[O-]S([O-])(=O)=O BAUYGSIQEAFULO-UHFFFAOYSA-L 0.000 description 1
- 229910000359 iron(II) sulfate Inorganic materials 0.000 description 1
- 239000011777 magnesium Substances 0.000 description 1
- 229910052943 magnesium sulfate Inorganic materials 0.000 description 1
- 235000019341 magnesium sulphate Nutrition 0.000 description 1
- 229910052748 manganese Inorganic materials 0.000 description 1
- 239000011572 manganese Substances 0.000 description 1
- 238000000034 method Methods 0.000 description 1
- 150000002823 nitrates Chemical class 0.000 description 1
- 150000002894 organic compounds Chemical class 0.000 description 1
- 229910000160 potassium phosphate Inorganic materials 0.000 description 1
- 235000011009 potassium phosphates Nutrition 0.000 description 1
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 102100029783 tRNA pseudouridine synthase A Human genes 0.000 description 1
- 101710194143 tRNA pseudouridine synthase A Proteins 0.000 description 1
- KYMBYSLLVAOCFI-UHFFFAOYSA-N thiamine Chemical compound CC1=C(CCO)SCN1CC1=CN=C(C)N=C1N KYMBYSLLVAOCFI-UHFFFAOYSA-N 0.000 description 1
- 229960003495 thiamine Drugs 0.000 description 1
- 235000019157 thiamine Nutrition 0.000 description 1
- 239000011721 thiamine Substances 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
Landscapes
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Description
ретроингибировани первого этапа биосинтеза гистидином.retroinhibition of the first stage of histidine biosynthesis.
Усваивает азот в форме аммони , нитратов , а также азот некоторых органических соединений.Absorbs nitrogen in the form of ammonium, nitrates, and also nitrogen of some organic compounds.
Растет при температуре 43°С и ниже. Оптимальной дл роста вл етс температура 37°С. а дл продукции гистидина 29-30°С.It grows at a temperature of 43 ° C and below. The optimum temperature for growth is 37 ° C. and for histidine production, 29-30 ° C.
Растет нэ жидких средах с рН от 6,0 до 8,0, Оптимальное значение рН 7,0.It grows in non-liquid media with a pH of 6.0 to 8.0. The optimum pH value is 7.0.
Хранение штамма. Посевной материал смешивают с равным объемом 80%-ного глицерина и хран т при -70°С.Strain storage. The seed is mixed with an equal volume of 80% glycerol and stored at -70 ° C.
П р и м е р 1. Введение мутации hfsT.PRI me R 1. Introduction mutations hfsT.
В штамм E.coli(hisG) с нечувствительной к гистидину АТФ-фосфорибозилтранс- феразой трансдукцией ввод т мутантный ген.ЫзТ. Ген hisT кодирует псевдоуридилат- синтазу 1 - фермент, который превращает уридиновые остатки в антикодоновой области тРНК в псевдоуридиновые. Использованна мутаци в гене hisT приводит к накоплению тРНК с пониженным содержанием псевдоуридиновых остатков. Наличие в клетках Е. coll измененной тРНК his вызывает усиление транскрипции гистидинового оперона. Активаци транскрипции происходит , по-видимому, из-за замедлени трансл ции лидерного пептида аттенюаторной области his-оперона.A mutant gene is introduced into the E. coli strain (hisG) with histidine-insensitive ATP-phosphoribosyltransferase transduction. The hisT gene encodes pseudouridylate synthase 1, an enzyme that converts the uridine residues in the anticodon region of tRNA into pseudouridine. The mutation used in the hisT gene leads to the accumulation of tRNA with a reduced content of pseudouridine residues. The presence of altered his tRNA in E. coll cells causes increased transcription of the histidine operon. Transcription activation is apparently due to a slower translation of the leader peptide of the attenuator region of his-operon.
Трзнсдукцию провод т с помощью фага Р1 так, как рекомендовано в руководстве Миллера. У трансдуктантов определ ют уровень накоплени гистидина в культу- ральной жидкости через 72 ч культивировани . Культивирование провод т так, как описано ниже в примере 3. Среда дл культивировани содержит компоненты, перечисленные в примере 3, за исключением стрептомицина, который в данном случае в среду не добавл етс . Данные по накоплению гистидина в культуральной жидкости исходным штаммом и штаммом с glsT-мута- цией приведены в табл.1.Transduction is carried out using phage P1 as recommended in Miller’s manual. For transductants, histidine accumulation in the culture fluid was determined after 72 hours of cultivation. The cultivation is carried out as described below in Example 3. The culture medium contains the components listed in Example 3, with the exception of streptomycin, which in this case is not added to the medium. Data on histidine accumulation in the culture fluid by the initial strain and the strain with glsT mutation are given in Table 1.
П р и м е р 2. Эффект введени мутации по гену rpsL который придает клеткам устойчивость к стрептомицину (strR),Example 2. The effect of introducing a mutation on the rpsL gene which gives the cells resistance to streptomycin (strR),
В штамм E.coli gfsGr hisT трансдукцией ввод т мутантный ген rpsL. Трансдуктанты станов тс устойчивыми к 1-2 мг/мл стрептомицина . Эффект этой мутации на продукцию гистидина провер ют, культивиру Трансдуктанты так, как описано ниже в примере 3. Данные по накоплению гистидина в культуральной жидкости приведены в табл.2.A mutant rpsL gene is introduced into E. coli gfsGr hisT strain by transduction. Transductants become resistant to 1-2 mg / ml streptomycin. The effect of this mutation on histidine production is checked by culturing the Transductants as described below in Example 3. Data on the accumulation of histidine in the culture fluid are shown in Table 2.
П р и м е р 3. Отбор устойчивых к арсе- нату натри мутантов. Накопление гистидина в культуральной жидкости му антного штамма-продуцента.EXAMPLE 3. Selection of sodium arsenate-resistant mutants. The accumulation of histidine in the culture fluid of the mutant producer strain.
Биосинтез гистидина - энергоемкий процесс, требующий участи АТФ и фосфо- 5 рибозилпирофосфата. Дл стимул ции образовани макроэргических метаболитов, подобных АТФ, используют арсенат натри - токсический аналог неорганического фосфата . Клетки, устойчивые к ( , обрэзу- 0 ют большее количество макроэрготических метаболитов, чем обычные.Histidine biosynthesis is an energy-intensive process that requires the participation of ATP and phospho-5-ribosylpyrophosphate. Sodium arsenate, a toxic analogue of inorganic phosphate, is used to stimulate the formation of macroergic metabolites like ATP. Cells resistant to (form a larger number of macroergotic metabolites than ordinary ones.
Отбирают спонтанные мутации, обеспечивающие устойчивость к 4 мМ арсената Na. Затем среди отобранных спонтанных му- 5 тантов вы вл юттакие, которые при культивировании накапливают в культуральной жидкости гистидина больше, чем родительский штамм.Spontaneous mutations that provide resistance to 4 mM Na arsenate are selected. Then, among the selected spontaneous mutants, 5 are revealed which, upon cultivation, accumulate more histidine in the culture fluid than the parent strain.
Культивирование провод т следующим 0 образом.Cultivation is carried out as follows 0.
Посевную среду инокулируют бактери ми , выращенными на минимальной агаризо- ванной среде при 29°С в течение 48ч. Посевной материал получают выращивани- 5 ем в пробирках объемом 50 мл, содержащих 2 мл среды, помещенных на термостатируе- мую круговую качалку (200-240 об/ мин), при 29°С в течение 20 ч. Состав посевной среды, г/л:The seed medium is inoculated with bacteria grown on minimal agarized medium at 29 ° C for 48 hours. The seed is obtained by growing in 5 50 ml tubes containing 2 ml of medium placed on a thermostatically controlled circular shaker (200-240 rpm), at 29 ° C for 20 hours. The composition of the seed medium, g / l :
0Глюкоза560 Glucose56
АммонийAmmonium
сернокислый28sulfate28
Калий фосфорнокислый одно5 замещенный2,25Potassium phosphate one5 substituted2.25
Магний сернокислый , 7-водный1.125, Железо (II) сернокислое , 7-водное 0,01, 0 Марганец (() сернокислый,Magnesium sulfate, 7-aqueous 1.125, Iron (II) sulfate, 7-aqueous 0.01, 0 Manganese (() sulfate,
4-водный0,01,4-water 0.01,
Тиамин0,001,Thiamine 0.001,
Аатолизэт дрожжей 2,8, 5Пролил0,5Yeast Anatolysis 2.8, 5 Prolyl 0.5
Стрептомицин1,0Streptomycin 1.0
Вода дистиллированна , лДо 1, рН7,0 0 Затем в колбу объемом 250 мл, содержащую 10 мл ферментационной среды, в лос т 5% посевного материала и инкубирую1 нэ круговой качалке (300 об /мин) при 30°С. Ферментационна среда отличаетс от по- 5 севной среды только добавлением 22 г мела на 1 л посевной среды, По окончании ферментации клетки отдел ют центрифугарова- нием, а гистидин определ ют колориметрически в культуральной жидкости после хроматографии на пластинках Силуфол . Через 72 ч ферментации культураль- на жидкость содержит 11,6-11,8 г/л гисти- дина. Данные по накоплению гистидина родительским и арсенат-устойчивым штаммом в культуральной жидкости приведены в табл.3.Distilled water, lDo 1, pH 7.0 0 Then, into a 250 ml flask containing 10 ml of fermentation medium, in a lot of 5% seed and incubate 1 in a circular shaker (300 rpm) at 30 ° C. The fermentation medium differs from the seed medium only by adding 22 g of chalk per 1 liter of inoculum. After the fermentation is complete, the cells are separated by centrifugation, and histidine is determined colorimetrically in the culture liquid after chromatography on Silufol plates. After 72 hours of fermentation, the culture fluid contains 11.6-11.8 g / L histidine. Data on the accumulation of histidine by the parent and arsenate-resistant strain in the culture fluid are shown in table 3.
(56) 1. Патент США Мг 3713977, кл. 195-29. 1973.(56) 1. U.S. Patent Mg 3713977, cl. 195-29. 1973.
2. Патент США № 4388405, кл. С 12 N 1/20, 1983.2. US patent No. 4388405, CL. C 12 N 1/20, 1983.
3.Аствацатур нц Г.В.. Лисенков А.Ф., Смирнов Ю.В., Шакулов Р.С. Генетика, т. XXIV.1988, с. 1928-1934.3. Astvatsatur nts G.V. Lisenkov A.F., Smirnov Yu.V., Shakulov R.S. Genetics, vol. XXIV. 1988, p. 1928-1934.
4.Лисенков В.Ф.. Аствацатур нц Г.В., Смирнов Ю.В., Ежель С.А.. Шакулов Р.С.4. Lisenkov V.F. Astvatsatur nts G.V., Smirnov Yu.V., Yezhel S.A. Shakulov R.S.
Молекул рна генетика, микробиологи и вирусологи , 1988, с. 37-43.Molecular Genetics, Microbiologists and Virologists, 1988, p. 37-43.
5.Миллер Дж. Эксперименты в молекул рной генетике. М.: Мир, 1976.5. Miller J. Experiments in molecular genetics. M.: Mir, 1976.
Ф ормула изобретени Штамм бактерий Escherlchla coti ВКПМSUMMARY OF THE INVENTION Escherlchla coti VKPM bacterial strain
Т а б л и ца 1Table 1
Таблица2Table 2
ТаблицаЗTable3
В-5945 - продуцент L-гистидина.B-5945 is a producer of L-histidine.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| SU5034791 RU2003677C1 (en) | 1992-03-30 | 1992-03-30 | Strain of bacterium escherichia coli - a producer of l-histidine |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| SU5034791 RU2003677C1 (en) | 1992-03-30 | 1992-03-30 | Strain of bacterium escherichia coli - a producer of l-histidine |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| RU2003677C1 true RU2003677C1 (en) | 1993-11-30 |
Family
ID=21600571
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| SU5034791 RU2003677C1 (en) | 1992-03-30 | 1992-03-30 | Strain of bacterium escherichia coli - a producer of l-histidine |
Country Status (1)
| Country | Link |
|---|---|
| RU (1) | RU2003677C1 (en) |
Cited By (42)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2119536C1 (en) * | 1997-01-21 | 1998-09-27 | Государственный научно-исследовательский институт генетики и селекции промышленных микроорганизмов | Strain escherichia coli - a producer of l-histidine |
| WO2007100009A1 (en) | 2006-03-03 | 2007-09-07 | Ajinomoto Co., Inc. | Method for production of l-amino acid |
| WO2007125954A1 (en) | 2006-04-28 | 2007-11-08 | Ajinomoto Co., Inc. | Microorganism capable of producing l-amino acid, and process for production of l-amino acid |
| WO2007136133A1 (en) | 2006-05-23 | 2007-11-29 | Ajinomoto Co., Inc. | A method for producing an l-amino acid using a bacterium of the enterobacteriaceae family |
| WO2008090770A1 (en) | 2007-01-22 | 2008-07-31 | Ajinomoto Co., Inc. | Microorganism capable of producing l-amino acid, and method for production of l-amino acid |
| WO2008102861A1 (en) | 2007-02-22 | 2008-08-28 | Ajinomoto Co., Inc. | Method of producing l-amino acid |
| EP2055771A2 (en) | 2006-03-23 | 2009-05-06 | 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 |
| DE102008049533A1 (en) | 2007-09-27 | 2009-06-18 | Ajinomoto Co., Inc. | A method for producing amino acids using a bacterium of the family Enterobacteriaceae |
| WO2009088049A1 (en) | 2008-01-10 | 2009-07-16 | Ajinomoto Co., Inc. | Method for production of desired substance by fermentation process |
| WO2009093703A1 (en) | 2008-01-23 | 2009-07-30 | Ajinomoto Co., Inc. | Method of producing l-amino acid |
| EP2093291A1 (en) | 2008-02-19 | 2009-08-26 | Ajinomoto Co., Inc. | A method for constructing an operon containing translationally coupled genes |
| WO2010027045A1 (en) | 2008-09-08 | 2010-03-11 | 味の素株式会社 | Microorganism capable of producing l-amino acid, and method for producing l-amino acid |
| WO2010084995A2 (en) | 2009-01-23 | 2010-07-29 | Ajinomoto Co.,Inc. | A method for producing an l-amino acid |
| WO2011013707A1 (en) | 2009-07-29 | 2011-02-03 | 味の素株式会社 | Method for producing l-amino acid |
| EP2345667A2 (en) | 2010-01-15 | 2011-07-20 | Ajinomoto Co., Inc. | A method for producing an L-amino acid using a bacterium of the enterobacteriaceae family |
| WO2011096554A1 (en) | 2010-02-08 | 2011-08-11 | 味の素株式会社 | MANUFACTURING METHOD FOR MUTANT rpsA GENE AND L-AMINO ACID |
| WO2011102305A2 (en) | 2010-02-18 | 2011-08-25 | Ajinomoto Co.,Inc. | A METHOD FOR PRODUCING AN L-AMINO ACID USING A BACTERIUM OF THE Enterobacteriaceae FAMILY HAVING A MUTANT ADENYLATE CYCLASE |
| WO2012011595A1 (en) | 2010-07-21 | 2012-01-26 | Ajinomoto Co.,Inc. | A METHOD FOR PRODUCING AN L-AMINO ACID USING A BACTERIUM OF THE ENTEROBACTERIACEAE FAMILY HAVING ATTENUATED EXPRESSION OF THE astCADBE OPERON |
| WO2012011596A1 (en) | 2010-07-21 | 2012-01-26 | Ajinomoto Co.,Inc. | A method for producing an l- amino acid using a bacterium of the enterobacteriaceae family with enhanced expression of the bssr gene |
| EP2460873A1 (en) | 2006-12-12 | 2012-06-06 | Ajinomoto Co., Inc. | A method for producing an L-amino acid using a bacterium of the Enterobacteriaceae family with attenuated expression of any of the cynT, cynS, cynX or cynR genes or a combination thereof |
| WO2012077739A1 (en) | 2010-12-10 | 2012-06-14 | 味の素株式会社 | Method for producing l-amino acid |
| US8372606B2 (en) | 2006-12-25 | 2013-02-12 | Ajinomoto Co., Inc. | Methods for obtaining crystals of a basic amino acid hydrochloride |
| EP2559754A2 (en) | 2011-08-18 | 2013-02-20 | Ajinomoto Co., Inc. | Method for producing an L-amino acid using a bacterium of the family enterobacteriaceae having enhanced expression of the flagella formation and motility cascade genes |
| WO2014029376A1 (en) | 2012-08-22 | 2014-02-27 | Forschungszentrum Jülich GmbH | Method for producing vectors containing a gene that codes for an enzyme having reduced or switched-off feedback inhibition, and use thereof for producing amino acids and nucleotides |
| EP2796560A1 (en) | 2013-04-23 | 2014-10-29 | Ajinomoto Co., Inc. | A method for producing an L-amino acid using a bacterium of the family Enterobacteriaceae having attenuated expression of the yjjK gene |
| WO2014185430A1 (en) | 2013-05-13 | 2014-11-20 | 味の素株式会社 | Method for manufacturing l-amino acid |
| WO2015030019A1 (en) | 2013-08-30 | 2015-03-05 | Ajinomoto Co.,Inc. | A METHOD FOR PRODUCING AN L-AMINO ACID USING A BACTERIUM OF THE FAMILY ENTEROBACTERIACEAE HAVING ATTENUATED EXPRESSION OF THE znuACB GENE CLUSTER |
| WO2015041265A1 (en) | 2013-09-17 | 2015-03-26 | 味の素株式会社 | Method for producing l-amino acid from seaweed-derived biomass |
| WO2015050276A1 (en) | 2013-10-02 | 2015-04-09 | Ajinomoto Co.,Inc. | A method for producing an l-amino acid using a bacterium of the family enterobacteriaceae having attenuated expression of a phosphate transporter-encoding gene |
| WO2015050234A1 (en) | 2013-10-02 | 2015-04-09 | 味の素株式会社 | Ammonia control apparatus and ammonia control method |
| WO2015060391A1 (en) | 2013-10-23 | 2015-04-30 | 味の素株式会社 | Method for producing target substance |
| WO2015060314A1 (en) | 2013-10-21 | 2015-04-30 | 味の素株式会社 | Method for producing l-amino acid |
| WO2015122544A1 (en) | 2014-02-14 | 2015-08-20 | Ajinomoto Co.,Inc. | A METHOD FOR PRODUCING AN L-AMINO ACID USING A BACTERIUM OF THE FAMILY ENTEROBACTERIACEAE HAVING OVEREXPRESSED THE yajL GENE |
| EP3098319A1 (en) | 2015-05-28 | 2016-11-30 | Ajinomoto Co., Inc. | A method for producing an l-amino acid using a bacterium of the family enterobacteriaceae having an attenuated expression of a gsha gene |
| WO2017146195A1 (en) | 2016-02-25 | 2017-08-31 | Ajinomoto Co., Inc. | A method for producing l-amino acids using a bacterium of the family enterobacteriaceae overexpressing a gene encoding an iron exporter |
| EP3385389A1 (en) | 2017-04-03 | 2018-10-10 | Ajinomoto Co., Inc. | Method for producing l-amino acid from fructose |
| WO2020071538A1 (en) | 2018-10-05 | 2020-04-09 | Ajinomoto Co., Inc. | Method for producing target substance by bacterial fermentation |
| WO2020138178A1 (en) | 2018-12-27 | 2020-07-02 | Ajinomoto Co., Inc. | Method for producing basic l-amino acids or salts thereof by fermentation of an enterobacteriaceae bacterium |
| WO2020171227A1 (en) | 2019-02-22 | 2020-08-27 | Ajinomoto Co., Inc. | METHOD FOR PRODUCING L-AMINO ACIDS USING A BACTERIUM BELONGING TO THE FAMILY Enterobacteriaceae HAVING OVEREXPRESSED ydiJ GENE |
| WO2020204179A1 (en) | 2019-04-05 | 2020-10-08 | Ajinomoto Co., Inc. | Method of producing l-amino acids |
| JP2020530771A (en) * | 2017-08-02 | 2020-10-29 | シージェイ チェイルジェダン コーポレーション | ATP phosphoribosyltransferase variant and method for producing L-histidine using it |
| WO2021060438A1 (en) | 2019-09-25 | 2021-04-01 | Ajinomoto Co., Inc. | Method for producing l-amino acids by bacterial fermentation |
-
1992
- 1992-03-30 RU SU5034791 patent/RU2003677C1/en active
Cited By (48)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2119536C1 (en) * | 1997-01-21 | 1998-09-27 | Государственный научно-исследовательский институт генетики и селекции промышленных микроорганизмов | Strain escherichia coli - a producer of l-histidine |
| WO2007100009A1 (en) | 2006-03-03 | 2007-09-07 | Ajinomoto Co., Inc. | Method for production of l-amino acid |
| EP2351830A1 (en) | 2006-03-23 | 2011-08-03 | 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 |
| EP2055771A2 (en) | 2006-03-23 | 2009-05-06 | 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 |
| WO2007125954A1 (en) | 2006-04-28 | 2007-11-08 | Ajinomoto Co., Inc. | Microorganism capable of producing l-amino acid, and process for production of l-amino acid |
| WO2007136133A1 (en) | 2006-05-23 | 2007-11-29 | Ajinomoto Co., Inc. | A method for producing an l-amino acid using a bacterium of the enterobacteriaceae family |
| EP2460873A1 (en) | 2006-12-12 | 2012-06-06 | Ajinomoto Co., Inc. | A method for producing an L-amino acid using a bacterium of the Enterobacteriaceae family with attenuated expression of any of the cynT, cynS, cynX or cynR genes or a combination thereof |
| US8372606B2 (en) | 2006-12-25 | 2013-02-12 | Ajinomoto Co., Inc. | Methods for obtaining crystals of a basic amino acid hydrochloride |
| WO2008090770A1 (en) | 2007-01-22 | 2008-07-31 | Ajinomoto Co., Inc. | Microorganism capable of producing l-amino acid, and method for production of l-amino acid |
| WO2008102861A1 (en) | 2007-02-22 | 2008-08-28 | Ajinomoto Co., Inc. | Method of producing l-amino acid |
| DE102008049533A1 (en) | 2007-09-27 | 2009-06-18 | Ajinomoto Co., Inc. | A method for producing amino acids using a bacterium of the family Enterobacteriaceae |
| WO2009088049A1 (en) | 2008-01-10 | 2009-07-16 | Ajinomoto Co., Inc. | Method for production of desired substance by fermentation process |
| EP2749652A2 (en) | 2008-01-10 | 2014-07-02 | Ajinomoto Co., Inc. | A method for producing a target substance by fermentation |
| WO2009093703A1 (en) | 2008-01-23 | 2009-07-30 | Ajinomoto Co., Inc. | Method of producing l-amino acid |
| EP2093291A1 (en) | 2008-02-19 | 2009-08-26 | Ajinomoto Co., Inc. | A method for constructing an operon containing translationally coupled genes |
| WO2010027045A1 (en) | 2008-09-08 | 2010-03-11 | 味の素株式会社 | Microorganism capable of producing l-amino acid, and method for producing l-amino acid |
| WO2010084995A2 (en) | 2009-01-23 | 2010-07-29 | Ajinomoto Co.,Inc. | A method for producing an l-amino acid |
| WO2011013707A1 (en) | 2009-07-29 | 2011-02-03 | 味の素株式会社 | Method for producing l-amino acid |
| EP2345667A2 (en) | 2010-01-15 | 2011-07-20 | Ajinomoto Co., Inc. | A method for producing an L-amino acid using a bacterium of the enterobacteriaceae family |
| WO2011096554A1 (en) | 2010-02-08 | 2011-08-11 | 味の素株式会社 | MANUFACTURING METHOD FOR MUTANT rpsA GENE AND L-AMINO ACID |
| WO2011102305A2 (en) | 2010-02-18 | 2011-08-25 | Ajinomoto Co.,Inc. | A METHOD FOR PRODUCING AN L-AMINO ACID USING A BACTERIUM OF THE Enterobacteriaceae FAMILY HAVING A MUTANT ADENYLATE CYCLASE |
| WO2012011595A1 (en) | 2010-07-21 | 2012-01-26 | Ajinomoto Co.,Inc. | A METHOD FOR PRODUCING AN L-AMINO ACID USING A BACTERIUM OF THE ENTEROBACTERIACEAE FAMILY HAVING ATTENUATED EXPRESSION OF THE astCADBE OPERON |
| WO2012011596A1 (en) | 2010-07-21 | 2012-01-26 | Ajinomoto Co.,Inc. | A method for producing an l- amino acid using a bacterium of the enterobacteriaceae family with enhanced expression of the bssr gene |
| WO2012077739A1 (en) | 2010-12-10 | 2012-06-14 | 味の素株式会社 | Method for producing l-amino acid |
| WO2013024904A1 (en) | 2011-08-18 | 2013-02-21 | Ajinomoto Co.,Inc. | A method for producing an l-amino acid using a bacterium of the family enterobacteriaceae having enhanced expression of the flagella formation and motility cascade genes |
| EP2559754A2 (en) | 2011-08-18 | 2013-02-20 | Ajinomoto Co., Inc. | Method for producing an L-amino acid using a bacterium of the family enterobacteriaceae having enhanced expression of the flagella formation and motility cascade genes |
| WO2014029376A1 (en) | 2012-08-22 | 2014-02-27 | Forschungszentrum Jülich GmbH | Method for producing vectors containing a gene that codes for an enzyme having reduced or switched-off feedback inhibition, and use thereof for producing amino acids and nucleotides |
| DE102012016716A1 (en) | 2012-08-22 | 2014-02-27 | Forschungszentrum Jülich GmbH | A process for the preparation of vectors comprising a gene coding for an enzyme which has been reduced or eliminated in its feedback inhibition and the use thereof for the production of amino acids and nucleotides |
| US9644226B2 (en) | 2012-08-22 | 2017-05-09 | Forschungszentrum Juelich Gmbh | Method for producing vectors containing a gene coding for an enzyme having reduced or deactivated feedback inhibition and the use thereof for producing amino acids and nucleotides |
| EP2796560A1 (en) | 2013-04-23 | 2014-10-29 | Ajinomoto Co., Inc. | A method for producing an L-amino acid using a bacterium of the family Enterobacteriaceae having attenuated expression of the yjjK gene |
| WO2014185430A1 (en) | 2013-05-13 | 2014-11-20 | 味の素株式会社 | Method for manufacturing l-amino acid |
| WO2015030019A1 (en) | 2013-08-30 | 2015-03-05 | Ajinomoto Co.,Inc. | A METHOD FOR PRODUCING AN L-AMINO ACID USING A BACTERIUM OF THE FAMILY ENTEROBACTERIACEAE HAVING ATTENUATED EXPRESSION OF THE znuACB GENE CLUSTER |
| WO2015041265A1 (en) | 2013-09-17 | 2015-03-26 | 味の素株式会社 | Method for producing l-amino acid from seaweed-derived biomass |
| WO2015050276A1 (en) | 2013-10-02 | 2015-04-09 | Ajinomoto Co.,Inc. | A method for producing an l-amino acid using a bacterium of the family enterobacteriaceae having attenuated expression of a phosphate transporter-encoding gene |
| WO2015050234A1 (en) | 2013-10-02 | 2015-04-09 | 味の素株式会社 | Ammonia control apparatus and ammonia control method |
| WO2015060314A1 (en) | 2013-10-21 | 2015-04-30 | 味の素株式会社 | Method for producing l-amino acid |
| WO2015060391A1 (en) | 2013-10-23 | 2015-04-30 | 味の素株式会社 | Method for producing target substance |
| WO2015122544A1 (en) | 2014-02-14 | 2015-08-20 | Ajinomoto Co.,Inc. | A METHOD FOR PRODUCING AN L-AMINO ACID USING A BACTERIUM OF THE FAMILY ENTEROBACTERIACEAE HAVING OVEREXPRESSED THE yajL GENE |
| EP3098319A1 (en) | 2015-05-28 | 2016-11-30 | Ajinomoto Co., Inc. | A method for producing an l-amino acid using a bacterium of the family enterobacteriaceae having an attenuated expression of a gsha gene |
| WO2017146195A1 (en) | 2016-02-25 | 2017-08-31 | Ajinomoto Co., Inc. | A method for producing l-amino acids using a bacterium of the family enterobacteriaceae overexpressing a gene encoding an iron exporter |
| EP3385389A1 (en) | 2017-04-03 | 2018-10-10 | Ajinomoto Co., Inc. | Method for producing l-amino acid from fructose |
| JP2020530771A (en) * | 2017-08-02 | 2020-10-29 | シージェイ チェイルジェダン コーポレーション | ATP phosphoribosyltransferase variant and method for producing L-histidine using it |
| WO2020071538A1 (en) | 2018-10-05 | 2020-04-09 | Ajinomoto Co., Inc. | Method for producing target substance by bacterial fermentation |
| WO2020138178A1 (en) | 2018-12-27 | 2020-07-02 | Ajinomoto Co., Inc. | Method for producing basic l-amino acids or salts thereof by fermentation of an enterobacteriaceae bacterium |
| US11999983B2 (en) | 2018-12-27 | 2024-06-04 | Ajinomoto Co., Inc. | Method for producing basic L-amino acids or salts thereof by fermentation of an Enterobacteriaceae bacterium |
| WO2020171227A1 (en) | 2019-02-22 | 2020-08-27 | Ajinomoto Co., Inc. | METHOD FOR PRODUCING L-AMINO ACIDS USING A BACTERIUM BELONGING TO THE FAMILY Enterobacteriaceae HAVING OVEREXPRESSED ydiJ GENE |
| WO2020204179A1 (en) | 2019-04-05 | 2020-10-08 | Ajinomoto Co., Inc. | Method of producing l-amino acids |
| WO2021060438A1 (en) | 2019-09-25 | 2021-04-01 | Ajinomoto Co., Inc. | Method for producing l-amino acids by bacterial fermentation |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| RU2003677C1 (en) | Strain of bacterium escherichia coli - a producer of l-histidine | |
| US4681852A (en) | Novel microorganism and method | |
| RU2119536C1 (en) | Strain escherichia coli - a producer of l-histidine | |
| JP3032013B2 (en) | Strain of microorganism producing tryptophan, method for producing the same, and method for producing tryptophan | |
| US5538873A (en) | Bacterial strain of escherichia coli BKIIM B-3996 as the producer of l-threonine | |
| AU712821B2 (en) | Production of tryptophan by the bacterium Escherichia coli | |
| US5658766A (en) | Strains of Escherichia coli which produce isoleucine or valine and a method for their production | |
| RU2207376C2 (en) | Method for preparing l-amino acid by fermentation method, strain of bacterium escherichia coli as producer of l-amino acid (variants) | |
| US7011961B2 (en) | Method for L-threonine production | |
| Sias et al. | Isolation and analysis of mutants of Pseudomonas aeruginosa unable to assimilate nitrate | |
| Ravnikar et al. | Genetic characterization of a highly efficient alternate pathway of serine biosynthesis in Escherichia coli | |
| RU2245919C2 (en) | Method for producing l-amino acid, strain escherichia coli tdh7δmlc::cat/pprt614 as producer of l-threonine | |
| FR2680178A1 (en) | Process for producing L-glutamic acid by fermentation | |
| US7582460B2 (en) | 3-phosphoglycerate dehydrogenase variants whose inhibition by L-serine is reduced, and genes encoding them | |
| Özbas et al. | Comparative study of riboflavin production from two microorganisms: Eremothecium ashbyii and Ashbya gossypii | |
| CS273163B2 (en) | Method of l-carnitine production | |
| FI115636B (en) | Quinic acid synthesis from glucose | |
| GB2130216A (en) | Enzymatic synthesis of L-serine | |
| US6893860B1 (en) | Microorganisms and methods for producing threonine | |
| Ely et al. | Ammonia assimilation and glutamate formation in Caulobacter crescentus | |
| Yokota et al. | Conversion of pyruvic acid fermentation to tryptophan production by the combination of pyruvic acid-producing microorganisms and Enterobacter aerogenes having high tryptophanase activity | |
| RU2728251C1 (en) | Escherichia coli strain with inactivated yche gene - l-threonine producer | |
| Bubnov et al. | Glutamyl-and Glutaminyl-tRNA synthetases are a promising target for the design of an L-Threonine–producing strain | |
| RYU et al. | Stringent factor regulates antibiotics production and morphological differentiation of Streptomyces clavuligerus | |
| US5151353A (en) | Process of using bacteria that metabolize phenylacetate through mandelate |