HU217795B - Eljárás szerin és szerinszármazékok bioszintézisére - Google Patents
Eljárás szerin és szerinszármazékok bioszintézisére Download PDFInfo
- Publication number
- HU217795B HU217795B HU9400796A HU9400796A HU217795B HU 217795 B HU217795 B HU 217795B HU 9400796 A HU9400796 A HU 9400796A HU 9400796 A HU9400796 A HU 9400796A HU 217795 B HU217795 B HU 217795B
- Authority
- HU
- Hungary
- Prior art keywords
- pgd
- serine
- aeqg
- genetically engineered
- dna
- Prior art date
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- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 title claims abstract description 63
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 title claims abstract description 61
- 238000000034 method Methods 0.000 title claims abstract description 13
- 230000015572 biosynthetic process Effects 0.000 title abstract description 14
- 239000000463 material Substances 0.000 title description 2
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 17
- 108010038555 Phosphoglycerate dehydrogenase Proteins 0.000 claims description 83
- 210000004027 cell Anatomy 0.000 claims description 25
- 230000014509 gene expression Effects 0.000 claims description 14
- 101150002295 serA gene Proteins 0.000 claims description 13
- 150000001413 amino acids Chemical class 0.000 claims description 10
- 238000012217 deletion Methods 0.000 claims description 9
- 230000037430 deletion Effects 0.000 claims description 9
- 238000003780 insertion Methods 0.000 claims description 8
- 230000037431 insertion Effects 0.000 claims description 8
- 125000001433 C-terminal amino-acid group Chemical group 0.000 claims description 7
- 210000004899 c-terminal region Anatomy 0.000 claims description 7
- 239000013604 expression vector Substances 0.000 claims description 6
- 238000012986 modification Methods 0.000 claims description 6
- 230000004048 modification Effects 0.000 claims description 6
- 230000001105 regulatory effect Effects 0.000 claims description 6
- 230000008569 process Effects 0.000 claims description 3
- 125000003275 alpha amino acid group Chemical group 0.000 claims 3
- 241000772991 Aira Species 0.000 claims 1
- 102100034184 Macrophage scavenger receptor types I and II Human genes 0.000 claims 1
- 101710134306 Macrophage scavenger receptor types I and II Proteins 0.000 claims 1
- 238000012258 culturing Methods 0.000 claims 1
- 238000011191 terminal modification Methods 0.000 claims 1
- 230000035945 sensitivity Effects 0.000 abstract description 13
- 238000004519 manufacturing process Methods 0.000 abstract description 7
- 238000010353 genetic engineering Methods 0.000 abstract description 4
- 150000003354 serine derivatives Chemical class 0.000 abstract 1
- 229960001153 serine Drugs 0.000 description 55
- 239000013612 plasmid Substances 0.000 description 21
- 230000000694 effects Effects 0.000 description 19
- 108020004414 DNA Proteins 0.000 description 15
- 239000012634 fragment Substances 0.000 description 15
- 230000003197 catalytic effect Effects 0.000 description 11
- 108700028369 Alleles Proteins 0.000 description 10
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 10
- 229960000723 ampicillin Drugs 0.000 description 9
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 9
- 239000002207 metabolite Substances 0.000 description 8
- 239000013598 vector Substances 0.000 description 8
- 102000004190 Enzymes Human genes 0.000 description 7
- 108090000790 Enzymes Proteins 0.000 description 7
- 150000001875 compounds Chemical class 0.000 description 7
- 229940088598 enzyme Drugs 0.000 description 7
- 230000010354 integration Effects 0.000 description 6
- 239000004471 Glycine Substances 0.000 description 5
- 229940024606 amino acid Drugs 0.000 description 5
- 235000001014 amino acid Nutrition 0.000 description 5
- 230000002759 chromosomal effect Effects 0.000 description 5
- 210000000349 chromosome Anatomy 0.000 description 5
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- 230000002068 genetic effect Effects 0.000 description 5
- 230000010076 replication Effects 0.000 description 5
- 230000007017 scission Effects 0.000 description 5
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 4
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 4
- IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 4
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 4
- 230000001413 cellular effect Effects 0.000 description 4
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- 229930182817 methionine Natural products 0.000 description 4
- 150000003212 purines Chemical class 0.000 description 4
- 230000009466 transformation Effects 0.000 description 4
- OSJPPGNTCRNQQC-UWTATZPHSA-N 3-phospho-D-glyceric acid Chemical compound OC(=O)[C@H](O)COP(O)(O)=O OSJPPGNTCRNQQC-UWTATZPHSA-N 0.000 description 3
- 241000894006 Bacteria Species 0.000 description 3
- 102000004594 DNA Polymerase I Human genes 0.000 description 3
- 108010017826 DNA Polymerase I Proteins 0.000 description 3
- 241000588724 Escherichia coli Species 0.000 description 3
- GRSZFWQUAKGDAV-KQYNXXCUSA-N IMP Chemical compound O[C@@H]1[C@H](O)[C@@H](COP(O)(O)=O)O[C@H]1N1C(NC=NC2=O)=C2N=C1 GRSZFWQUAKGDAV-KQYNXXCUSA-N 0.000 description 3
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 3
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 3
- 230000006696 biosynthetic metabolic pathway Effects 0.000 description 3
- OEYIOHPDSNJKLS-UHFFFAOYSA-N choline Chemical compound C[N+](C)(C)CCO OEYIOHPDSNJKLS-UHFFFAOYSA-N 0.000 description 3
- 229960001231 choline Drugs 0.000 description 3
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 3
- 235000018417 cysteine Nutrition 0.000 description 3
- 235000013902 inosinic acid Nutrition 0.000 description 3
- 230000036961 partial effect Effects 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- 150000003230 pyrimidines Chemical class 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- 239000005460 tetrahydrofolate Substances 0.000 description 3
- 238000010361 transduction Methods 0.000 description 3
- MSTNYGQPCMXVAQ-RYUDHWBXSA-N (6S)-5,6,7,8-tetrahydrofolic acid Chemical compound C([C@H]1CNC=2N=C(NC(=O)C=2N1)N)NC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 MSTNYGQPCMXVAQ-RYUDHWBXSA-N 0.000 description 2
- 108020005544 Antisense RNA Proteins 0.000 description 2
- DWRXFEITVBNRMK-UHFFFAOYSA-N Beta-D-1-Arabinofuranosylthymine Natural products O=C1NC(=O)C(C)=CN1C1C(O)C(O)C(CO)O1 DWRXFEITVBNRMK-UHFFFAOYSA-N 0.000 description 2
- 241000206602 Eukaryota Species 0.000 description 2
- 101150020741 Hpgds gene Proteins 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
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- 229930027917 kanamycin Natural products 0.000 description 2
- 229960000318 kanamycin Drugs 0.000 description 2
- SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 2
- 229930182823 kanamycin A Natural products 0.000 description 2
- 244000005700 microbiome Species 0.000 description 2
- 238000012261 overproduction Methods 0.000 description 2
- 235000018102 proteins Nutrition 0.000 description 2
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- 238000011084 recovery Methods 0.000 description 2
- 238000012216 screening Methods 0.000 description 2
- 229940104230 thymidine Drugs 0.000 description 2
- 231100000331 toxic Toxicity 0.000 description 2
- 230000002588 toxic effect Effects 0.000 description 2
- 230000026683 transduction Effects 0.000 description 2
- LELJBJGDDGUFRP-REOHCLBHSA-N (2s)-2-amino-n,3-dihydroxypropanamide Chemical compound OC[C@H](N)C(=O)NO LELJBJGDDGUFRP-REOHCLBHSA-N 0.000 description 1
- QYNUQALWYRSVHF-OLZOCXBDSA-N (6R)-5,10-methylenetetrahydrofolic acid Chemical compound C([C@H]1CNC=2N=C(NC(=O)C=2N1C1)N)N1C1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 QYNUQALWYRSVHF-OLZOCXBDSA-N 0.000 description 1
- MJEQLGCFPLHMNV-UHFFFAOYSA-N 4-amino-1-(hydroxymethyl)pyrimidin-2-one Chemical compound NC=1C=CN(CO)C(=O)N=1 MJEQLGCFPLHMNV-UHFFFAOYSA-N 0.000 description 1
- PFJBDCNEHIXTLU-VPCXQMTMSA-N 4-amino-1-[(2r,3r,4s,5r)-3,4-dihydroxy-2,5-bis(hydroxymethyl)oxolan-2-yl]pyrimidin-2-one Chemical compound O=C1N=C(N)C=CN1[C@@]1(CO)[C@H](O)[C@H](O)[C@@H](CO)O1 PFJBDCNEHIXTLU-VPCXQMTMSA-N 0.000 description 1
- -1 5 , N 10 -methylene Chemical group 0.000 description 1
- 241000193738 Bacillus anthracis Species 0.000 description 1
- 102000005367 Carboxypeptidases Human genes 0.000 description 1
- 108010006303 Carboxypeptidases Proteins 0.000 description 1
- 102000005572 Cathepsin A Human genes 0.000 description 1
- 108010059081 Cathepsin A Proteins 0.000 description 1
- 108020004638 Circular DNA Proteins 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 102100037579 D-3-phosphoglycerate dehydrogenase Human genes 0.000 description 1
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 1
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 1
- 108090000204 Dipeptidase 1 Proteins 0.000 description 1
- 108700039887 Essential Genes Proteins 0.000 description 1
- 108010046914 Exodeoxyribonuclease V Proteins 0.000 description 1
- 102000019236 Exonuclease V Human genes 0.000 description 1
- 230000005526 G1 to G0 transition Effects 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- 229930010555 Inosine Natural products 0.000 description 1
- UGQMRVRMYYASKQ-KQYNXXCUSA-N Inosine Chemical compound O[C@@H]1[C@H](O)[C@@H](CO)O[C@H]1N1C2=NC=NC(O)=C2N=C1 UGQMRVRMYYASKQ-KQYNXXCUSA-N 0.000 description 1
- 102100038609 Lactoperoxidase Human genes 0.000 description 1
- 108010023244 Lactoperoxidase Proteins 0.000 description 1
- 102000003960 Ligases Human genes 0.000 description 1
- 108090000364 Ligases Proteins 0.000 description 1
- 108091028043 Nucleic acid sequence Proteins 0.000 description 1
- 108091000080 Phosphotransferase Proteins 0.000 description 1
- 108020005091 Replication Origin Proteins 0.000 description 1
- 108700008625 Reporter Genes Proteins 0.000 description 1
- 239000004098 Tetracycline Substances 0.000 description 1
- 230000003281 allosteric effect Effects 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 101150072344 argA gene Proteins 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 102000006635 beta-lactamase Human genes 0.000 description 1
- 238000002306 biochemical method Methods 0.000 description 1
- 230000001851 biosynthetic effect Effects 0.000 description 1
- 125000004432 carbon atom Chemical group C* 0.000 description 1
- 230000003833 cell viability Effects 0.000 description 1
- 238000007385 chemical modification Methods 0.000 description 1
- 229960005091 chloramphenicol Drugs 0.000 description 1
- WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 1
- 239000013611 chromosomal DNA Substances 0.000 description 1
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- 239000008103 glucose Substances 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 229960003786 inosine Drugs 0.000 description 1
- 230000026045 iodination Effects 0.000 description 1
- 238000006192 iodination reaction Methods 0.000 description 1
- 229940057428 lactoperoxidase Drugs 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- KCRZDTROFIOPBP-UHFFFAOYSA-N phosphono 2,3-dihydroxypropanoate Chemical compound OCC(O)C(=O)OP(O)(O)=O KCRZDTROFIOPBP-UHFFFAOYSA-N 0.000 description 1
- 102000020233 phosphotransferase Human genes 0.000 description 1
- 239000013600 plasmid vector Substances 0.000 description 1
- 230000035755 proliferation Effects 0.000 description 1
- 230000003252 repetitive effect Effects 0.000 description 1
- 108091008146 restriction endonucleases Proteins 0.000 description 1
- 210000003705 ribosome Anatomy 0.000 description 1
- 150000003355 serines Chemical class 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 229960002180 tetracycline Drugs 0.000 description 1
- 229930101283 tetracycline Natural products 0.000 description 1
- 235000019364 tetracycline Nutrition 0.000 description 1
- 150000003522 tetracyclines Chemical class 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
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- 230000001131 transforming effect Effects 0.000 description 1
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Classifications
-
- 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
- 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
- C12P13/06—Alanine; Leucine; Isoleucine; Serine; Homoserine
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Engineering & Computer Science (AREA)
- Health & Medical Sciences (AREA)
- Wood Science & Technology (AREA)
- Genetics & Genomics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Microbiology (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Biotechnology (AREA)
- General Engineering & Computer Science (AREA)
- Biomedical Technology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- General Chemical & Material Sciences (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Enzymes And Modification Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Transition And Organic Metals Composition Catalysts For Addition Polymerization (AREA)
- Tires In General (AREA)
- Epoxy Resins (AREA)
- Ceramic Products (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP91121385 | 1991-12-12 |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| HU9400796D0 HU9400796D0 (en) | 1994-06-28 |
| HUT69802A HUT69802A (en) | 1995-09-28 |
| HU217795B true HU217795B (hu) | 2000-04-28 |
Family
ID=8207424
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| HU9400796A HU217795B (hu) | 1991-12-12 | 1992-08-17 | Eljárás szerin és szerinszármazékok bioszintézisére |
Country Status (19)
Families Citing this family (33)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE4232468A1 (de) * | 1992-09-28 | 1994-03-31 | Consortium Elektrochem Ind | Mikroorganismen für die Produktion von Tryptophan und Verfahren zu ihrer Herstellung |
| JP4066543B2 (ja) * | 1998-01-12 | 2008-03-26 | 味の素株式会社 | 発酵法によるｌ−セリンの製造法 |
| 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 |
| US6431870B1 (en) | 1999-11-30 | 2002-08-13 | Ora Metrix, Inc. | Method and apparatus for generating a desired three-dimensional digital model of an orthodontic structure |
| US6250918B1 (en) | 1999-11-30 | 2001-06-26 | Orametrix, Inc. | Method and apparatus for simulating tooth movement for an orthodontic patient |
| US6350120B1 (en) | 1999-11-30 | 2002-02-26 | Orametrix, Inc. | Method and apparatus for designing an orthodontic apparatus to provide tooth movement |
| US6471512B1 (en) | 1999-11-30 | 2002-10-29 | Ora Metrix, Inc. | Method and apparatus for determining and monitoring orthodontic treatment |
| US6540512B1 (en) | 1999-11-30 | 2003-04-01 | Orametrix, Inc. | Method and apparatus for treating an orthodontic patient |
| AU2001259263A1 (en) * | 2000-05-02 | 2001-11-12 | Agrinomics, Llc | Identification and characterization of a pagoda phenotype (pgd) in plants |
| DE10232930A1 (de) * | 2002-07-19 | 2004-02-05 | Consortium für elektrochemische Industrie GmbH | Verfahren zur fermentativen Herstellung von Aminosäuren und Aminosäure-Derivaten der Phosphoglycerat-Familie |
| 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 |
| WO2006096558A2 (en) | 2005-03-07 | 2006-09-14 | Orthoclear Holdings, Inc. | Variations of dental aligners |
| US20060275731A1 (en) | 2005-04-29 | 2006-12-07 | Orthoclear Holdings, Inc. | Treatment of teeth by aligners |
| DE102005049527B4 (de) * | 2005-10-17 | 2013-05-08 | Forschungszentrum Jülich GmbH | Verfahren zur Herstellung von L-Serin, Gensequenz, Vektoren sowie Mikroorganismus |
| RU2006129690A (ru) | 2006-08-16 | 2008-02-27 | Закрытое акционерное общество "Научно-исследовательский институт Аджиномото-Генетика" (ЗАО АГРИ) (RU) | СПОСОБ ПОЛУЧЕНИЯ L-АМИНОКИСЛОТЫ С ИСПОЛЬЗОВАНИЕМ БАКТЕРИЙ СЕМЕЙСТВА Enterobacteriaceae, В КОТОРОЙ ОСЛАБЛЕНА ЭКСПРЕССИЯ ГЕНА ydiN, ГЕНА ydiB ИЛИ ИХ КОМБИНАЦИИ |
| JP2010017082A (ja) * | 2006-10-10 | 2010-01-28 | Ajinomoto Co Inc | Ｌ−アミノ酸の製造法 |
| JP2010017081A (ja) * | 2006-10-10 | 2010-01-28 | Ajinomoto Co Inc | Ｌ−アミノ酸の製造法 |
| CN101939412B (zh) | 2007-09-04 | 2016-01-20 | 味之素株式会社 | 生产氨基酸的微生物以及氨基酸的生产方法 |
| US8383372B2 (en) * | 2008-03-06 | 2013-02-26 | Ajinomoto Co., Inc. | L-cysteine producing bacterium and a method for producing L-cysteine |
| JP5332237B2 (ja) * | 2008-03-06 | 2013-11-06 | 味の素株式会社 | Ｌ−システイン生産菌及びｌ−システインの製造法 |
| EP2379730B1 (en) | 2008-12-31 | 2015-07-22 | Metabolic Explorer | Method for the preparation of diols |
| EP2508594B1 (en) * | 2009-11-30 | 2017-08-16 | Ajinomoto Co., Inc. | L-cysteine-producing bacterium, and process for production of l-cysteine |
| EP2588598B1 (en) | 2010-07-02 | 2016-03-09 | Metabolic Explorer | Method for the preparation of hydroxy acids |
| DE102011075656A1 (de) | 2011-05-11 | 2012-03-29 | Wacker Chemie Ag | Verfahren zur fermentativen Produktion von L-Cystin |
| DE102011078481A1 (de) | 2011-06-30 | 2013-01-03 | Wacker Chemie Ag | Verfahren zur fermentativen Produktion von natürlichem L-Cystein |
| DE102012208359A1 (de) | 2012-05-18 | 2013-11-21 | Wacker Chemie Ag | Verfahren zur fermentativen Produktion von L-Cystein und Derivaten dieser Aminosäure |
| DE102012216527A1 (de) | 2012-09-17 | 2014-03-20 | Wacker Chemie Ag | Verfahren zur fermentativen Produktion von L-Cystein und Derivaten dieser Aminosäure |
| WO2014049382A2 (en) | 2012-09-26 | 2014-04-03 | Metabolic Explorer | Ethylenediamine fermentative production by a recombinant microorganism |
| DE102013209274A1 (de) | 2013-05-17 | 2014-11-20 | Wacker Chemie Ag | Mikroorganismus und Verfahren zur fermentativen Überproduktion von Gamma-Glutamylcystein und Derivaten dieses Dipeptids |
| JP7463388B2 (ja) | 2019-02-20 | 2024-04-08 | ブラスケム エス．エー． | ペントース糖およびヘキソース糖のための分解経路 |
| CN113710807B (zh) | 2019-02-20 | 2025-05-30 | 布拉斯科公司 | 用于由己糖生产含氧化合物的微生物和方法 |
| JP2023532871A (ja) | 2020-06-26 | 2023-08-01 | ワッカー ケミー アクチエンゲゼルシャフト | 改良されたシステイン産生株 |
| CN118742558A (zh) | 2022-03-01 | 2024-10-01 | 瓦克化学股份公司 | 改良的半胱氨酸生产菌株 |
Family Cites Families (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0190921A3 (en) * | 1985-02-04 | 1988-01-13 | Engenics, Inc. | Method for the overproduction of amino acids |
| US4743546A (en) * | 1985-02-13 | 1988-05-10 | Biotechnica International, Inc. | Controlled gene excision |
| US4753883A (en) * | 1986-05-07 | 1988-06-28 | Biotechnica International, Inc. | Enzyme deregulation |
| US4753833A (en) * | 1986-09-26 | 1988-06-28 | Fishgal Semyon I | Hollow article with zigzag projections |
| GB8828806D0 (en) * | 1988-12-09 | 1989-01-18 | Beecham Group Plc | Novel compounds |
| 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 |
| US5120837A (en) * | 1989-09-20 | 1992-06-09 | The Nutrasweet Company | Dna encoding phe a feedback inhibition resistant enzyme analogues |
-
1992
- 1992-03-24 TW TW081102201A patent/TW313589B/zh active
- 1992-08-17 UA UA94005362A patent/UA39861C2/uk unknown
- 1992-08-17 SK SK700-94A patent/SK279805B6/sk not_active IP Right Cessation
- 1992-08-17 EP EP92917826A patent/EP0620853B1/en not_active Expired - Lifetime
- 1992-08-17 CA CA002124214A patent/CA2124214C/en not_active Expired - Lifetime
- 1992-08-17 HU HU9400796A patent/HU217795B/hu unknown
- 1992-08-17 RU RU94030817/13A patent/RU2154671C1/ru active
- 1992-08-17 ES ES92917826T patent/ES2084373T3/es not_active Expired - Lifetime
- 1992-08-17 CZ CZ941406A patent/CZ285915B6/cs not_active IP Right Cessation
- 1992-08-17 JP JP5510540A patent/JP2584409B2/ja not_active Expired - Lifetime
- 1992-08-17 AU AU24268/92A patent/AU668359B2/en not_active Expired
- 1992-08-17 WO PCT/EP1992/001873 patent/WO1993012235A1/en active IP Right Grant
- 1992-08-17 DE DE69208894T patent/DE69208894T2/de not_active Expired - Lifetime
- 1992-08-17 US US08/244,491 patent/US5618716A/en not_active Expired - Lifetime
- 1992-08-17 BR BR9206902A patent/BR9206902A/pt not_active Application Discontinuation
- 1992-08-17 KR KR1019940701948A patent/KR0132258B1/ko not_active Expired - Lifetime
- 1992-08-25 ZA ZA926405A patent/ZA926405B/xx unknown
- 1992-10-10 CN CN92112014A patent/CN1065914C/zh not_active Expired - Lifetime
-
1994
- 1994-06-09 FI FI942711A patent/FI113665B/fi not_active IP Right Cessation
Also Published As
| Publication number | Publication date |
|---|---|
| RU2154671C1 (ru) | 2000-08-20 |
| US5618716A (en) | 1997-04-08 |
| DE69208894D1 (de) | 1996-04-11 |
| AU2426892A (en) | 1993-07-19 |
| SK70094A3 (en) | 1995-03-08 |
| FI942711A0 (fi) | 1994-06-09 |
| CZ140694A3 (en) | 1995-01-18 |
| ZA926405B (en) | 1993-04-28 |
| HUT69802A (en) | 1995-09-28 |
| CA2124214C (en) | 2002-04-02 |
| TW313589B (GUID-C5D7CC26-194C-43D0-91A1-9AE8C70A9BFF.html) | 1997-08-21 |
| ES2084373T3 (es) | 1996-05-01 |
| CN1065914C (zh) | 2001-05-16 |
| WO1993012235A1 (en) | 1993-06-24 |
| CN1073209A (zh) | 1993-06-16 |
| EP0620853B1 (en) | 1996-03-06 |
| FI942711L (fi) | 1994-06-09 |
| UA39861C2 (uk) | 2001-07-16 |
| JP2584409B2 (ja) | 1997-02-26 |
| SK279805B6 (sk) | 1999-04-13 |
| EP0620853A1 (en) | 1994-10-26 |
| DE69208894T2 (de) | 1996-07-18 |
| CA2124214A1 (en) | 1993-06-24 |
| JPH06510911A (ja) | 1994-12-08 |
| AU668359B2 (en) | 1996-05-02 |
| HU9400796D0 (en) | 1994-06-28 |
| KR0132258B1 (ko) | 1998-04-11 |
| CZ285915B6 (cs) | 1999-11-17 |
| FI113665B (fi) | 2004-05-31 |
| BR9206902A (pt) | 1995-11-21 |
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