CA1248898A - Production of l-amino acids by transamination - Google Patents
Production of l-amino acids by transaminationInfo
- Publication number
- CA1248898A CA1248898A CA000462306A CA462306A CA1248898A CA 1248898 A CA1248898 A CA 1248898A CA 000462306 A CA000462306 A CA 000462306A CA 462306 A CA462306 A CA 462306A CA 1248898 A CA1248898 A CA 1248898A
- Authority
- CA
- Canada
- Prior art keywords
- acid
- transaminase
- oxaloacetate
- enzyme
- amino acid
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired
Links
- 238000005891 transamination reaction Methods 0.000 title claims description 14
- 150000008575 L-amino acids Chemical class 0.000 title abstract description 36
- 238000004519 manufacturing process Methods 0.000 title description 16
- 238000000034 method Methods 0.000 claims abstract description 81
- 102000003929 Transaminases Human genes 0.000 claims abstract description 63
- 108090000340 Transaminases Proteins 0.000 claims abstract description 62
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- 230000008569 process Effects 0.000 claims abstract description 48
- 229960005261 aspartic acid Drugs 0.000 claims abstract description 34
- CKLJMWTZIZZHCS-UHFFFAOYSA-N D-OH-Asp Natural products OC(=O)C(N)CC(O)=O CKLJMWTZIZZHCS-UHFFFAOYSA-N 0.000 claims abstract description 29
- KHPXUQMNIQBQEV-UHFFFAOYSA-N oxaloacetic acid Chemical compound OC(=O)CC(=O)C(O)=O KHPXUQMNIQBQEV-UHFFFAOYSA-N 0.000 claims abstract description 20
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 claims abstract description 8
- 235000008206 alpha-amino acids Nutrition 0.000 claims abstract description 6
- 150000001371 alpha-amino acids Chemical class 0.000 claims abstract description 4
- 150000001412 amines Chemical class 0.000 claims abstract description 3
- 150000004716 alpha keto acids Chemical class 0.000 claims abstract 6
- 230000000911 decarboxylating effect Effects 0.000 claims abstract 5
- 150000001370 alpha-amino acid derivatives Chemical class 0.000 claims abstract 2
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 claims description 44
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- 102100029589 Acylpyruvase FAHD1, mitochondrial Human genes 0.000 claims description 29
- 229960005190 phenylalanine Drugs 0.000 claims description 24
- 150000001413 amino acids Chemical class 0.000 claims description 22
- BTNMPGBKDVTSJY-UHFFFAOYSA-N keto-phenylpyruvic acid Chemical compound OC(=O)C(=O)CC1=CC=CC=C1 BTNMPGBKDVTSJY-UHFFFAOYSA-N 0.000 claims description 17
- 238000002360 preparation method Methods 0.000 claims description 17
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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 claims description 9
- 241000191938 Micrococcus luteus Species 0.000 claims description 9
- PPKAIMDMNWBOKN-UHFFFAOYSA-N 2-Oxo-4-phenylbutyric acid Chemical compound OC(=O)C(=O)CCC1=CC=CC=C1 PPKAIMDMNWBOKN-UHFFFAOYSA-N 0.000 claims description 6
- 239000002245 particle Substances 0.000 claims description 6
- 244000005700 microbiome Species 0.000 claims description 5
- RSTKLPZEZYGQPY-UHFFFAOYSA-N 3-(indol-3-yl)pyruvic acid Chemical compound C1=CC=C2C(CC(=O)C(=O)O)=CNC2=C1 RSTKLPZEZYGQPY-UHFFFAOYSA-N 0.000 claims description 4
- 229910021645 metal ion Inorganic materials 0.000 claims description 4
- 229960001153 serine Drugs 0.000 claims description 4
- JVIPLYCGEZUBIO-UHFFFAOYSA-N 2-(4-fluorophenyl)-1,3-dioxoisoindole-5-carboxylic acid Chemical compound O=C1C2=CC(C(=O)O)=CC=C2C(=O)N1C1=CC=C(F)C=C1 JVIPLYCGEZUBIO-UHFFFAOYSA-N 0.000 claims description 3
- QHKABHOOEWYVLI-UHFFFAOYSA-N 3-methyl-2-oxobutanoic acid Chemical compound CC(C)C(=O)C(O)=O QHKABHOOEWYVLI-UHFFFAOYSA-N 0.000 claims description 3
- 241000590020 Achromobacter Species 0.000 claims description 3
- 108030000991 Aromatic-amino-acid transaminases Proteins 0.000 claims description 3
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- 241000384075 Eurydice Species 0.000 claims description 3
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- JTTHKOPSMAVJFE-VIFPVBQESA-N L-homophenylalanine Chemical compound OC(=O)[C@@H](N)CCC1=CC=CC=C1 JTTHKOPSMAVJFE-VIFPVBQESA-N 0.000 claims description 3
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- BKAJNAXTPSGJCU-UHFFFAOYSA-N 4-methyl-2-oxopentanoic acid Chemical compound CC(C)CC(=O)C(O)=O BKAJNAXTPSGJCU-UHFFFAOYSA-N 0.000 claims description 2
- 239000001903 2-oxo-3-phenylpropanoic acid Substances 0.000 claims 2
- HHDDCCUIIUWNGJ-UHFFFAOYSA-N 3-hydroxypyruvic acid Chemical compound OCC(=O)C(O)=O HHDDCCUIIUWNGJ-UHFFFAOYSA-N 0.000 claims 2
- DEDGUGJNLNLJSR-UHFFFAOYSA-N alpha-hydroxycinnamic acid Natural products OC(=O)C(O)=CC1=CC=CC=C1 DEDGUGJNLNLJSR-UHFFFAOYSA-N 0.000 claims 2
- 239000011148 porous material Substances 0.000 claims 2
- JVQYSWDUAOAHFM-UHFFFAOYSA-N 3-methyl-2-oxovaleric acid Chemical compound CCC(C)C(=O)C(O)=O JVQYSWDUAOAHFM-UHFFFAOYSA-N 0.000 claims 1
- DGKSNMQAIREVEE-UHFFFAOYSA-N 4-(1h-imidazol-5-yl)-2,4-dioxobutanoic acid Chemical compound OC(=O)C(=O)CC(=O)C1=CN=CN1 DGKSNMQAIREVEE-UHFFFAOYSA-N 0.000 claims 1
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- 239000000203 mixture Substances 0.000 abstract description 19
- 108010003989 D-amino-acid oxidase Proteins 0.000 abstract description 18
- 125000003277 amino group Chemical group 0.000 abstract description 2
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- 238000006243 chemical reaction Methods 0.000 description 39
- LCTONWCANYUPML-UHFFFAOYSA-N Pyruvic acid Chemical compound CC(=O)C(O)=O LCTONWCANYUPML-UHFFFAOYSA-N 0.000 description 32
- 239000000243 solution Substances 0.000 description 31
- 102100026908 D-amino-acid oxidase Human genes 0.000 description 16
- -1 alpha-keto acid compounds Chemical class 0.000 description 16
- NGVDGCNFYWLIFO-UHFFFAOYSA-N pyridoxal 5'-phosphate Chemical compound CC1=NC=C(COP(O)(O)=O)C(C=O)=C1O NGVDGCNFYWLIFO-UHFFFAOYSA-N 0.000 description 16
- 229940107700 pyruvic acid Drugs 0.000 description 16
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- 102000016938 Catalase Human genes 0.000 description 13
- 108010053835 Catalase Proteins 0.000 description 13
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 12
- 239000000047 product Substances 0.000 description 11
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 10
- 238000006114 decarboxylation reaction Methods 0.000 description 10
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 9
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 9
- LWIHDJKSTIGBAC-UHFFFAOYSA-K tripotassium phosphate Chemical compound [K+].[K+].[K+].[O-]P([O-])([O-])=O LWIHDJKSTIGBAC-UHFFFAOYSA-K 0.000 description 9
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 8
- 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 8
- 235000007682 pyridoxal 5'-phosphate Nutrition 0.000 description 8
- 239000011589 pyridoxal 5'-phosphate Substances 0.000 description 8
- 229960001327 pyridoxal phosphate Drugs 0.000 description 8
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- 239000000872 buffer Substances 0.000 description 7
- 239000006227 byproduct Substances 0.000 description 7
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- 210000003734 kidney Anatomy 0.000 description 7
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 7
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 description 6
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- 238000002835 absorbance Methods 0.000 description 6
- 125000000217 alkyl group Chemical group 0.000 description 6
- 238000003556 assay Methods 0.000 description 6
- KKADPXVIOXHVKN-UHFFFAOYSA-N 4-hydroxyphenylpyruvic acid Chemical compound OC(=O)C(=O)CC1=CC=C(O)C=C1 KKADPXVIOXHVKN-UHFFFAOYSA-N 0.000 description 5
- 150000008574 D-amino acids Chemical class 0.000 description 5
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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
- C12P41/00—Processes using enzymes or microorganisms to separate optical isomers from a racemic mixture
- C12P41/006—Processes using enzymes or microorganisms to separate optical isomers from a racemic mixture by reactions involving C-N bonds, e.g. nitriles, amides, hydantoins, carbamates, lactames, transamination reactions, or keto group formation from racemic mixtures
-
- 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
- C12N11/00—Carrier-bound or immobilised enzymes; Carrier-bound or immobilised microbial cells; Preparation thereof
- C12N11/18—Multi-enzyme systems
-
- 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.)
- C12N9/1096—Transferases (2.) transferring nitrogenous groups (2.6)
-
- 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
-
- 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
-
- 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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- 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
- C12P13/12—Methionine; Cysteine; Cystine
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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
- C12P13/22—Tryptophan; Tyrosine; Phenylalanine; 3,4-Dihydroxyphenylalanine
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Zoology (AREA)
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- Biotechnology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Biomedical Technology (AREA)
- Analytical Chemistry (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
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Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US528,730 | 1983-09-01 | ||
| US06/528,730 US4518692A (en) | 1983-09-01 | 1983-09-01 | Production of L-amino acids by transamination |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA1248898A true CA1248898A (en) | 1989-01-17 |
Family
ID=24106925
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA000462306A Expired CA1248898A (en) | 1983-09-01 | 1984-08-31 | Production of l-amino acids by transamination |
Country Status (3)
| Country | Link |
|---|---|
| US (1) | US4518692A (https=) |
| JP (1) | JPS6091993A (https=) |
| CA (1) | CA1248898A (https=) |
Families Citing this family (42)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS59146595A (ja) * | 1983-02-10 | 1984-08-22 | Nippon Zeon Co Ltd | Ｓ−アデノシル−ｌ−ホモシステインの製造法 |
| US4600692A (en) * | 1983-02-10 | 1986-07-15 | Purification Engineering, Inc. | Immobilized cells for preparing phenylalanine |
| US4728611A (en) * | 1983-07-29 | 1988-03-01 | Purification Engineering, Inc. | Production of phenylalanine with immobilized cells |
| US4710467A (en) * | 1983-07-29 | 1987-12-01 | Purification Engineering, Inc. | Process for preparing phenylalanine |
| US4783403A (en) * | 1984-02-08 | 1988-11-08 | Kyowa Hakko Kogyo Co., Ltd. | Process for producing l-phenylalanine |
| DE3423936A1 (de) * | 1984-06-29 | 1986-01-02 | Hoechst Ag, 6230 Frankfurt | Verfahren zur herstellung von l-phenylalanin |
| US4859591A (en) * | 1984-07-05 | 1989-08-22 | W. R. Grace & Co.-Conn. | Transamination process for producing amino acids |
| US4652452A (en) * | 1985-02-11 | 1987-03-24 | Calgene, Inc. | Oxalic acid removal in beer production |
| US4826766A (en) * | 1985-09-23 | 1989-05-02 | Genetics Institute, Inc. | Production of amino acids using coupled aminotransferases |
| JPS62143691A (ja) * | 1985-12-17 | 1987-06-26 | Kyowa Hakko Kogyo Co Ltd | アミノ酸の製造法 |
| EP0533216B1 (de) * | 1986-06-04 | 2000-03-22 | Hoechst Schering AgrEvo GmbH | Verfahren zur Herstellung von L-tertiär-Leucin durch Transaminierung |
| US4880738A (en) * | 1986-06-13 | 1989-11-14 | Genetics Institute, Inc. | Production of amino acids using coupled enzyme systems |
| US5316943A (en) * | 1988-06-14 | 1994-05-31 | Kidman Gene E | Racemic conversion of using a transaminase |
| DE3842025A1 (de) * | 1988-12-14 | 1990-07-05 | Hoechst Ag | Verfahren zur herstellung von l-phosphinothricin |
| JPH0553580A (ja) * | 1991-08-23 | 1993-03-05 | Kawai Musical Instr Mfg Co Ltd | 電子楽器の楽音制御装置 |
| US6197558B1 (en) | 1997-05-19 | 2001-03-06 | Nsc Technologies | Transaminase biotransformation process |
| US7202070B2 (en) * | 2000-10-31 | 2007-04-10 | Biocatalytics, Inc. | Method for reductive amination of a ketone using a mutated enzyme |
| US7297800B2 (en) * | 2001-12-27 | 2007-11-20 | Ajinomoto Co., Inc. | Process of producing glutamate derivatives |
| US7572607B2 (en) * | 2002-04-23 | 2009-08-11 | Cargill, Incorporated | Polypeptides and biosynthetic pathways for the production of monatin and its precursors |
| US8372989B2 (en) | 2002-04-23 | 2013-02-12 | Cargill, Incorporated | Polypeptides and biosynthetic pathways for the production of monatin and its precursors |
| RU2307871C2 (ru) | 2002-08-26 | 2007-10-10 | Адзиномото Ко., Инк. | НОВАЯ АЛЬДОЛАЗА И СПОСОБ ПОЛУЧЕНИЯ ЗАМЕЩЕННЫХ α-КЕТОКИСЛОТ |
| AU2003289264A1 (en) | 2002-12-09 | 2004-06-30 | Ajinomoto Co., Inc. | Mutant d-aminotransferase and process for producing optically active glutamic acid derivative using the same |
| US20050009151A1 (en) * | 2003-07-10 | 2005-01-13 | Pharmacia Corporation | Methods for the stereospecific and enantiomeric enrichment of beta-amino acids |
| US7180370B2 (en) * | 2004-09-01 | 2007-02-20 | Micron Technology, Inc. | CMOS amplifiers with frequency compensating capacitors |
| EP2132322A4 (en) * | 2007-03-02 | 2013-02-20 | Richmond Chemical Corp | METHOD FOR INCREASING YIELD AND IMPROVING PURIFICATION OF PRODUCTS FROM REACTIONS WITH TRANSAMINASE |
| CN104651381A (zh) | 2008-01-03 | 2015-05-27 | 巴斯夫酶有限责任公司 | 转移酶和氧化还原酶、编码它们的核酸以及其制备和应用方法 |
| HUE052297T2 (hu) | 2009-01-08 | 2021-04-28 | Codexis Inc | Transzamináz polipeptidek |
| WO2011005477A1 (en) | 2009-06-22 | 2011-01-13 | Codexis, Inc. | Transaminase reactions |
| WO2011031147A1 (en) * | 2009-09-11 | 2011-03-17 | Dsm Ip Assets B.V. | Preparation of a compound comprising an amine group from an alpha-keto acid |
| HUE038434T2 (hu) | 2010-06-17 | 2018-10-29 | Codexis Inc | Biokatalizátorok és módszerek (S)-3(1-aminoetil)-fenol szintéziséhez |
| EP2479272A4 (en) * | 2010-10-14 | 2013-11-20 | Ajinomoto Kk | PROCESS FOR THE PRODUCTION OF MONATIN |
| US8771997B2 (en) | 2011-04-20 | 2014-07-08 | Ajinomoto Co., Inc. | Method for producing monatin using an L-amino acid aminotransferase |
| WO2012147674A1 (ja) * | 2011-04-25 | 2012-11-01 | 味の素株式会社 | モナティンの製造方法 |
| EP2828256B1 (en) * | 2012-03-23 | 2019-07-03 | Novartis AG | Chemical process for preparing spiroindolones and intermediates thereof |
| SG11201504752YA (en) | 2012-12-21 | 2015-07-30 | Codexis Inc | Engineered biocatalysts and methods for synthesizing chiral amines |
| US9617573B2 (en) | 2013-02-28 | 2017-04-11 | Codexis, Inc. | Engineered transaminase polypeptides for industrial biocatalysis |
| EP3638688A4 (en) | 2017-06-14 | 2021-07-07 | Codexis, Inc. | MODIFIED TRANSAMINASE POLYPEPTIDES INTENDED FOR INDUSTRIAL BIOCATALYSIS |
| CA3126671A1 (en) | 2019-01-15 | 2020-07-23 | Codexis, Inc. | Engineered transaminase polypeptides |
| US20230025239A1 (en) * | 2019-12-02 | 2023-01-26 | Jilin Asymchem Laboratories Co., Ltd. | Co-immobilized enzyme, preparation method and use thereof |
| EP4133064A4 (en) | 2020-04-10 | 2024-07-24 | Codexis, Inc. | Engineered transaminase polypeptides |
| EP4217502A4 (en) | 2020-09-28 | 2024-12-11 | Codexis, Inc. | Engineered biocatalysts and methods for synthesizing chiral amines |
| CN118599802B (zh) * | 2024-08-08 | 2024-10-18 | 爱斯特（成都）生物制药股份有限公司 | 一种转氨酶、其制备方法、其应用，编码转氨酶的基因，重组质粒，重组菌，制备(s)-3-氨基丁酸的方法 |
Family Cites Families (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3036958A (en) * | 1959-03-17 | 1962-05-29 | Ajinomoto Kk | Process for producing l-tryptophan from 3-indolepyruvic acid |
| US3183170A (en) * | 1961-10-03 | 1965-05-11 | Sanraku Ocean Kabushiki Kaisha | Method of l-amino acid manufacture |
| DE1493442A1 (de) * | 1964-11-09 | 1969-11-06 | Ajinomoto Kk | Verfahren zur Herstellung von Alanin auf enzymatischem Wege |
| GB1059668A (en) * | 1964-11-24 | 1967-02-22 | Tanabe Seiyaku Co | Process for the preparation of l-alanine |
| JPS4818475B1 (https=) * | 1970-09-30 | 1973-06-06 | ||
| JPS4938839A (https=) * | 1972-08-19 | 1974-04-11 | ||
| JPS531831B2 (https=) * | 1972-11-20 | 1978-01-23 | ||
| JPS561076A (en) * | 1979-06-19 | 1981-01-08 | Ricoh Co Ltd | Correcting method for light source fluctuation in pattern generator |
| DE2930070A1 (de) * | 1979-07-25 | 1981-02-19 | Biotechnolog Forschung Gmbh | Verfahren zur kontinuierlichen enzymatischen umwandlung von wasserloeslichen alpha -ketocarbonsaeuren in die entsprechenden aminosaeuren |
-
1983
- 1983-09-01 US US06/528,730 patent/US4518692A/en not_active Expired - Lifetime
-
1984
- 1984-08-31 CA CA000462306A patent/CA1248898A/en not_active Expired
- 1984-09-01 JP JP59183611A patent/JPS6091993A/ja active Granted
Also Published As
| Publication number | Publication date |
|---|---|
| JPS6338193B2 (https=) | 1988-07-28 |
| JPS6091993A (ja) | 1985-05-23 |
| US4518692A (en) | 1985-05-21 |
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