SK402002A3 - Method for the production of l-amino acids from their racemic n-acetyl-d,l-derivatives by enzymatic racemate cleavage by means of isolated recombinant enzymes - Google Patents
Method for the production of l-amino acids from their racemic n-acetyl-d,l-derivatives by enzymatic racemate cleavage by means of isolated recombinant enzymes Download PDFInfo
- Publication number
- SK402002A3 SK402002A3 SK40-2002A SK402002A SK402002A3 SK 402002 A3 SK402002 A3 SK 402002A3 SK 402002 A SK402002 A SK 402002A SK 402002 A3 SK402002 A3 SK 402002A3
- Authority
- SK
- Slovakia
- Prior art keywords
- acetyl
- derivatives
- amino acids
- deac
- production
- Prior art date
Links
- 108090000790 Enzymes Proteins 0.000 title claims abstract description 37
- 102000004190 Enzymes Human genes 0.000 title claims abstract description 37
- 238000000034 method Methods 0.000 title claims abstract description 26
- 238000004519 manufacturing process Methods 0.000 title claims abstract description 20
- 150000008575 L-amino acids Chemical class 0.000 title claims abstract description 18
- 230000002255 enzymatic effect Effects 0.000 title claims abstract description 9
- 238000003776 cleavage reaction Methods 0.000 title abstract description 11
- 230000007017 scission Effects 0.000 title abstract description 10
- IAJOBQBIJHVGMQ-BYPYZUCNSA-N glufosinate-P Chemical compound CP(O)(=O)CC[C@H](N)C(O)=O IAJOBQBIJHVGMQ-BYPYZUCNSA-N 0.000 claims abstract description 42
- 150000008574 D-amino acids Chemical class 0.000 claims abstract description 3
- 239000000758 substrate Substances 0.000 claims description 38
- 238000006243 chemical reaction Methods 0.000 claims description 24
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 claims description 14
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 claims description 11
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 claims description 10
- 239000004395 L-leucine Substances 0.000 claims description 9
- 229960003136 leucine Drugs 0.000 claims description 9
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 claims description 8
- 229960002989 glutamic acid Drugs 0.000 claims description 8
- 241001600125 Delftia acidovorans Species 0.000 claims description 7
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 claims description 7
- 235000019454 L-leucine Nutrition 0.000 claims description 7
- 241000983364 Stenotrophomonas sp. Species 0.000 claims description 7
- 229960002885 histidine Drugs 0.000 claims description 7
- 229930182816 L-glutamine Natural products 0.000 claims description 6
- 239000002253 acid Substances 0.000 claims description 6
- 229960005190 phenylalanine Drugs 0.000 claims description 6
- 108010093701 hippurate hydrolase Proteins 0.000 claims description 5
- -1 Lhistidine Chemical compound 0.000 claims description 4
- 150000007513 acids Chemical class 0.000 claims description 4
- 229960002743 glutamine Drugs 0.000 claims description 4
- 108090000604 Hydrolases Proteins 0.000 claims description 3
- 108090000623 proteins and genes Proteins 0.000 description 18
- 235000018102 proteins Nutrition 0.000 description 16
- 102000004169 proteins and genes Human genes 0.000 description 16
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 12
- 230000000694 effects Effects 0.000 description 12
- 239000000243 solution Substances 0.000 description 11
- QIAFMBKCNZACKA-UHFFFAOYSA-N N-benzoylglycine Chemical compound OC(=O)CNC(=O)C1=CC=CC=C1 QIAFMBKCNZACKA-UHFFFAOYSA-N 0.000 description 10
- 150000001413 amino acids Chemical class 0.000 description 10
- 239000011942 biocatalyst Substances 0.000 description 10
- 239000001488 sodium phosphate Substances 0.000 description 10
- 229910000162 sodium phosphate Inorganic materials 0.000 description 10
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 10
- 229940024606 amino acid Drugs 0.000 description 9
- 235000001014 amino acid Nutrition 0.000 description 9
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 6
- VZVQOWUYAAWBCP-LURJTMIESA-N N-acetyl-L-phosphinothricin Chemical compound CC(=O)N[C@H](C(O)=O)CCP(C)(O)=O VZVQOWUYAAWBCP-LURJTMIESA-N 0.000 description 6
- 239000011780 sodium chloride Substances 0.000 description 6
- QXNVGIXVLWOKEQ-UHFFFAOYSA-N Disodium Chemical class [Na][Na] QXNVGIXVLWOKEQ-UHFFFAOYSA-N 0.000 description 5
- 230000014509 gene expression Effects 0.000 description 5
- 238000002360 preparation method Methods 0.000 description 5
- 238000010367 cloning Methods 0.000 description 4
- 238000005859 coupling reaction Methods 0.000 description 4
- 239000000047 product Substances 0.000 description 4
- 238000000746 purification Methods 0.000 description 4
- 230000002285 radioactive effect Effects 0.000 description 4
- 238000012360 testing method Methods 0.000 description 4
- YXFVVABEGXRONW-UHFFFAOYSA-N Toluene Chemical compound CC1=CC=CC=C1 YXFVVABEGXRONW-UHFFFAOYSA-N 0.000 description 3
- 238000001042 affinity chromatography Methods 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 230000036983 biotransformation Effects 0.000 description 3
- 239000007795 chemical reaction product Substances 0.000 description 3
- 230000008878 coupling Effects 0.000 description 3
- 238000010168 coupling process Methods 0.000 description 3
- 238000006911 enzymatic reaction Methods 0.000 description 3
- 238000002474 experimental method Methods 0.000 description 3
- 239000011159 matrix material Substances 0.000 description 3
- 150000007523 nucleic acids Chemical group 0.000 description 3
- 239000012071 phase Substances 0.000 description 3
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 description 2
- 241000588724 Escherichia coli Species 0.000 description 2
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 239000004471 Glycine Substances 0.000 description 2
- 102000004157 Hydrolases Human genes 0.000 description 2
- 125000003047 N-acetyl group Chemical group 0.000 description 2
- 108010073038 Penicillin Amidase Proteins 0.000 description 2
- IAJOBQBIJHVGMQ-UHFFFAOYSA-N Phosphinothricin Natural products CP(O)(=O)CCC(N)C(O)=O IAJOBQBIJHVGMQ-UHFFFAOYSA-N 0.000 description 2
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 2
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 2
- PXIPVTKHYLBLMZ-UHFFFAOYSA-N Sodium azide Chemical compound [Na+].[N-]=[N+]=[N-] PXIPVTKHYLBLMZ-UHFFFAOYSA-N 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 238000004296 chiral HPLC Methods 0.000 description 2
- 230000002363 herbicidal effect Effects 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- 230000000813 microbial effect Effects 0.000 description 2
- 229960003104 ornithine Drugs 0.000 description 2
- 239000008188 pellet Substances 0.000 description 2
- 239000012460 protein solution Substances 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 238000007086 side reaction Methods 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 239000013598 vector Substances 0.000 description 2
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 2
- IVWWFWFVSWOTLP-YVZVNANGSA-N (3'as,4r,7'as)-2,2,2',2'-tetramethylspiro[1,3-dioxolane-4,6'-4,7a-dihydro-3ah-[1,3]dioxolo[4,5-c]pyran]-7'-one Chemical compound C([C@@H]1OC(O[C@@H]1C1=O)(C)C)O[C@]21COC(C)(C)O2 IVWWFWFVSWOTLP-YVZVNANGSA-N 0.000 description 1
- HBAQYPYDRFILMT-UHFFFAOYSA-N 8-[3-(1-cyclopropylpyrazol-4-yl)-1H-pyrazolo[4,3-d]pyrimidin-5-yl]-3-methyl-3,8-diazabicyclo[3.2.1]octan-2-one Chemical class C1(CC1)N1N=CC(=C1)C1=NNC2=C1N=C(N=C2)N1C2C(N(CC1CC2)C)=O HBAQYPYDRFILMT-UHFFFAOYSA-N 0.000 description 1
- 108700023418 Amidases Proteins 0.000 description 1
- 238000009010 Bradford assay Methods 0.000 description 1
- 239000004593 Epoxy Substances 0.000 description 1
- 241001596967 Escherichia coli M15 Species 0.000 description 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
- NTIZESTWPVYFNL-UHFFFAOYSA-N Methyl isobutyl ketone Chemical compound CC(C)CC(C)=O NTIZESTWPVYFNL-UHFFFAOYSA-N 0.000 description 1
- UIHCLUNTQKBZGK-UHFFFAOYSA-N Methyl isobutyl ketone Natural products CCC(C)C(C)=O UIHCLUNTQKBZGK-UHFFFAOYSA-N 0.000 description 1
- 108091028043 Nucleic acid sequence Proteins 0.000 description 1
- 101710136728 Probable UDP-arabinopyranose mutase 1 Proteins 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 239000004480 active ingredient Substances 0.000 description 1
- 238000001261 affinity purification Methods 0.000 description 1
- 102000005922 amidase Human genes 0.000 description 1
- 150000003862 amino acid derivatives Chemical class 0.000 description 1
- 108010003977 aminoacylase I Proteins 0.000 description 1
- 229910021529 ammonia Inorganic materials 0.000 description 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 1
- 235000011130 ammonium sulphate Nutrition 0.000 description 1
- 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 1
- 229960000723 ampicillin Drugs 0.000 description 1
- 239000008346 aqueous phase Substances 0.000 description 1
- 125000003118 aryl group Chemical group 0.000 description 1
- 238000000376 autoradiography Methods 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 150000001735 carboxylic acids Chemical class 0.000 description 1
- 230000006037 cell lysis Effects 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 238000012790 confirmation Methods 0.000 description 1
- 239000000287 crude extract Substances 0.000 description 1
- KCWUWVDASLBBOZ-UHFFFAOYSA-L cyanoformate;nickel(2+) Chemical compound [Ni+2].[O-]C(=O)C#N.[O-]C(=O)C#N KCWUWVDASLBBOZ-UHFFFAOYSA-L 0.000 description 1
- 230000000850 deacetylating effect Effects 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 239000012149 elution buffer Substances 0.000 description 1
- 238000007824 enzymatic assay Methods 0.000 description 1
- 238000001952 enzyme assay Methods 0.000 description 1
- 125000003700 epoxy group Chemical group 0.000 description 1
- 230000032050 esterification Effects 0.000 description 1
- 238000005886 esterification reaction Methods 0.000 description 1
- 235000019441 ethanol Nutrition 0.000 description 1
- 239000013604 expression vector Substances 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 230000003100 immobilizing effect Effects 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 229930027917 kanamycin Natural products 0.000 description 1
- 229960000318 kanamycin Drugs 0.000 description 1
- 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 1
- 229930182823 kanamycin A Natural products 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 239000012139 lysis buffer Substances 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 229960004452 methionine Drugs 0.000 description 1
- 239000006225 natural substrate Substances 0.000 description 1
- 238000005457 optimization Methods 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 230000002018 overexpression Effects 0.000 description 1
- 238000012261 overproduction Methods 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 229960002429 proline Drugs 0.000 description 1
- 239000003531 protein hydrolysate Substances 0.000 description 1
- 230000020978 protein processing Effects 0.000 description 1
- 229930182852 proteinogenic amino acid Natural products 0.000 description 1
- 238000004445 quantitative analysis Methods 0.000 description 1
- 239000011535 reaction buffer Substances 0.000 description 1
- 230000035484 reaction time Effects 0.000 description 1
- 239000012088 reference solution Substances 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 238000012206 semi-quantitative assay Methods 0.000 description 1
- 229960001153 serine Drugs 0.000 description 1
- 239000002689 soil Substances 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000004809 thin layer chromatography Methods 0.000 description 1
- 229960004799 tryptophan Drugs 0.000 description 1
- 229960004441 tyrosine Drugs 0.000 description 1
- 238000002604 ultrasonography Methods 0.000 description 1
- 229960004295 valine Drugs 0.000 description 1
- 239000011534 wash buffer Substances 0.000 description 1
Classifications
-
- 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
-
- 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
- C12P41/007—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 by reactions involving acyl derivatives of racemic amines
-
- 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
- C12N9/14—Hydrolases (3)
- C12N9/78—Hydrolases (3) acting on carbon to nitrogen bonds other than peptide bonds (3.5)
- C12N9/80—Hydrolases (3) acting on carbon to nitrogen bonds other than peptide bonds (3.5) acting on amide bonds in linear amides (3.5.1)
-
- 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
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Analytical Chemistry (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Biomedical Technology (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Enzymes And Modification Thereof (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DE19933362A DE19933362A1 (de) | 1999-07-20 | 1999-07-20 | Verfahren zur Herstellung von L-Aminosäuren aus ihren racemischen N-Acetyl-D,L-Derivaten durch enzymatische Racemat-Spaltung mittels isolierter, rekombinanter Enzyme |
| PCT/EP2000/005586 WO2001005982A1 (de) | 1999-07-20 | 2000-06-17 | Verfahren zur herstellung von l-aminosäuren aus ihren racemischen n-acetyl-d,l-derivaten durch enzymatische racemat-spaltung mittels isolierter, rekombinanter enzyme |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| SK402002A3 true SK402002A3 (en) | 2002-04-04 |
Family
ID=7915003
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| SK40-2002A SK402002A3 (en) | 1999-07-20 | 2000-06-17 | Method for the production of l-amino acids from their racemic n-acetyl-d,l-derivatives by enzymatic racemate cleavage by means of isolated recombinant enzymes |
Country Status (24)
| Country | Link |
|---|---|
| US (1) | US6686181B1 (pt) |
| EP (1) | EP1200601B1 (pt) |
| JP (1) | JP4723778B2 (pt) |
| KR (1) | KR100672146B1 (pt) |
| CN (1) | CN1175108C (pt) |
| AT (1) | ATE319836T1 (pt) |
| AU (1) | AU778206B2 (pt) |
| BR (1) | BR0012572A (pt) |
| CA (1) | CA2379849A1 (pt) |
| CO (1) | CO5310578A1 (pt) |
| CZ (1) | CZ2002224A3 (pt) |
| DE (2) | DE19933362A1 (pt) |
| DK (1) | DK1200601T3 (pt) |
| ES (1) | ES2258011T3 (pt) |
| HU (1) | HU229651B1 (pt) |
| IL (1) | IL147398A (pt) |
| MX (1) | MXPA02000623A (pt) |
| NZ (1) | NZ516710A (pt) |
| PL (1) | PL203870B1 (pt) |
| RU (1) | RU2270869C2 (pt) |
| SK (1) | SK402002A3 (pt) |
| TW (1) | TWI238193B (pt) |
| UA (1) | UA73743C2 (pt) |
| WO (1) | WO2001005982A1 (pt) |
Families Citing this family (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| PT1481068E (pt) * | 2002-02-26 | 2011-05-09 | Syngenta Ltd | M?todo para produzir selectivamente plantas andro- ou gino-est?reis |
| ES2391468T3 (es) | 2005-03-29 | 2012-11-27 | Meiji Seika Pharma Co., Ltd. | Procedimiento para la producción de ácido L-2-amino-4-(hidroximetilfosfinil)butanoico |
| PL2060578T3 (pl) | 2006-09-04 | 2014-08-29 | Meiji Seika Pharma Co Ltd | Sposób wytwarzania optycznie czynnego kwasu aminofosfinylobutanowego |
| TWI397380B (zh) | 2006-09-20 | 2013-06-01 | Meiji Seika Kaisha | 含磷之α胺基酸之製造方法及其製造中間體 |
| WO2012154483A1 (en) * | 2011-05-06 | 2012-11-15 | Gilead Sciences, Inc. | Dry powder fosfomycin/tobramycin formulation for inhalation |
| CN109988806B (zh) * | 2017-12-29 | 2023-02-28 | 弈柯莱生物科技(上海)股份有限公司 | 一种n-乙酰-草铵膦盐的消旋方法 |
| CN108690854B (zh) * | 2018-04-16 | 2022-03-18 | 浙江工业大学 | 一种利用化学-酶法生产l-草铵膦的方法 |
| CN117597026A (zh) * | 2021-06-11 | 2024-02-23 | Upl有限公司 | 一种用于获得l-草铵膦的方法 |
Family Cites Families (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS5547630A (en) * | 1978-10-02 | 1980-04-04 | Meiji Seika Kaisha Ltd | Optical resolution of phosphorus-containing amino acid |
| US5081024A (en) * | 1988-09-05 | 1992-01-14 | Nissan Chemical Industries, Ltd. | Process for producing optically active amino acids |
| DE4308061A1 (de) * | 1993-03-13 | 1994-09-15 | Hoechst Ag | Neue Aminosäure-Deacetylase mit Spezifität für L-N-Acetyl-Phosphinothricin, ihre Herstellung und Verwendung |
| DE4422045A1 (de) * | 1994-06-26 | 1996-01-04 | Hoechst Schering Agrevo Gmbh | Verfahren zur enzymatischen Spaltung von 2-Amino-4-methylphosphinobutansäureamid-Derivaten |
| EP1889903A1 (en) | 1996-04-25 | 2008-02-20 | Novartis AG | Biocatalysts with amine acylase activity |
| DE19652284A1 (de) | 1996-12-16 | 1998-06-18 | Hoechst Schering Agrevo Gmbh | Neue Gene codierend für Aminosäure-Deacetylasen mit Spezifität für N-Acetyl-L-Phosphinothricin, ihre Isolierung und Verwendung |
-
1999
- 1999-07-20 DE DE19933362A patent/DE19933362A1/de not_active Ceased
-
2000
- 2000-06-17 RU RU2002104355/13A patent/RU2270869C2/ru not_active IP Right Cessation
- 2000-06-17 AT AT00943826T patent/ATE319836T1/de not_active IP Right Cessation
- 2000-06-17 JP JP2001511194A patent/JP4723778B2/ja not_active Expired - Lifetime
- 2000-06-17 HU HU0201850A patent/HU229651B1/hu not_active IP Right Cessation
- 2000-06-17 EP EP00943826A patent/EP1200601B1/de not_active Expired - Lifetime
- 2000-06-17 DE DE50012368T patent/DE50012368D1/de not_active Expired - Lifetime
- 2000-06-17 PL PL357347A patent/PL203870B1/pl not_active IP Right Cessation
- 2000-06-17 SK SK40-2002A patent/SK402002A3/sk not_active Application Discontinuation
- 2000-06-17 KR KR1020027000746A patent/KR100672146B1/ko not_active IP Right Cessation
- 2000-06-17 IL IL14739800A patent/IL147398A/xx active IP Right Grant
- 2000-06-17 DK DK00943826T patent/DK1200601T3/da active
- 2000-06-17 MX MXPA02000623A patent/MXPA02000623A/es active IP Right Grant
- 2000-06-17 CA CA002379849A patent/CA2379849A1/en not_active Abandoned
- 2000-06-17 ES ES00943826T patent/ES2258011T3/es not_active Expired - Lifetime
- 2000-06-17 BR BR0012572-5A patent/BR0012572A/pt not_active Application Discontinuation
- 2000-06-17 NZ NZ516710A patent/NZ516710A/xx unknown
- 2000-06-17 AU AU58156/00A patent/AU778206B2/en not_active Ceased
- 2000-06-17 CN CNB008105103A patent/CN1175108C/zh not_active Expired - Fee Related
- 2000-06-17 WO PCT/EP2000/005586 patent/WO2001005982A1/de active IP Right Grant
- 2000-06-17 CZ CZ2002224A patent/CZ2002224A3/cs unknown
- 2000-06-17 UA UA2002021417A patent/UA73743C2/uk unknown
- 2000-06-17 US US10/031,356 patent/US6686181B1/en not_active Expired - Lifetime
- 2000-07-12 CO CO00052026A patent/CO5310578A1/es not_active Application Discontinuation
- 2000-07-18 TW TW089114376A patent/TWI238193B/zh not_active IP Right Cessation
Also Published As
| Publication number | Publication date |
|---|---|
| RU2270869C2 (ru) | 2006-02-27 |
| PL357347A1 (en) | 2004-07-26 |
| BR0012572A (pt) | 2002-04-16 |
| KR100672146B1 (ko) | 2007-01-19 |
| HUP0201850A2 (en) | 2002-09-28 |
| IL147398A (en) | 2005-12-18 |
| ATE319836T1 (de) | 2006-03-15 |
| DE50012368D1 (de) | 2006-05-04 |
| MXPA02000623A (es) | 2002-07-02 |
| EP1200601A1 (de) | 2002-05-02 |
| AU778206B2 (en) | 2004-11-25 |
| DK1200601T3 (da) | 2006-07-17 |
| EP1200601B1 (de) | 2006-03-08 |
| CA2379849A1 (en) | 2001-01-25 |
| DE19933362A1 (de) | 2001-02-08 |
| KR20020020943A (ko) | 2002-03-16 |
| JP2003505031A (ja) | 2003-02-12 |
| CN1371422A (zh) | 2002-09-25 |
| PL203870B1 (pl) | 2009-11-30 |
| NZ516710A (en) | 2002-11-26 |
| UA73743C2 (en) | 2005-09-15 |
| JP4723778B2 (ja) | 2011-07-13 |
| HUP0201850A3 (en) | 2005-01-28 |
| CN1175108C (zh) | 2004-11-10 |
| US6686181B1 (en) | 2004-02-03 |
| CZ2002224A3 (cs) | 2002-06-12 |
| AU5815600A (en) | 2001-02-05 |
| TWI238193B (en) | 2005-08-21 |
| ES2258011T3 (es) | 2006-08-16 |
| CO5310578A1 (es) | 2003-08-29 |
| IL147398A0 (en) | 2002-08-14 |
| WO2001005982A1 (de) | 2001-01-25 |
| HU229651B1 (hu) | 2014-03-28 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| KR0170365B1 (ko) | 아미노기 전달 효소, 이의 제조방법 및 용도 | |
| Runser et al. | d-p-Hydroxyphenylglycine production from dl-5-p-hydroxyphenylhydantoin by Agrobacterium sp. | |
| CN106916857B (zh) | 一种生产l-草铵膦的方法 | |
| WO2009009117A2 (en) | Chemoenzymatic processes for preparation of levetiracetam | |
| Meiwes et al. | Asymmetric synthesis of l-thienylalanines | |
| SK402002A3 (en) | Method for the production of l-amino acids from their racemic n-acetyl-d,l-derivatives by enzymatic racemate cleavage by means of isolated recombinant enzymes | |
| US7858348B2 (en) | N-acetyl-(R,S)-beta-amino acid acylase gene | |
| WO2023088077A1 (en) | Biocatalysts and methods for the synthesis of pregabalin intermediates | |
| Syldatk et al. | Biotechnological production of D‐or L‐amino acids from 5‐monosubstituted hydantoins | |
| Lo et al. | Enantioselective synthesis of (S)‐2‐amino‐4‐phenylbutanoic acid by the hydantoinase method | |
| EP1174499A1 (en) | Novel amidase gene | |
| US7629154B2 (en) | Deinococcus N-acylamino acid racemase and use of preparing L-amino acid | |
| AU2002254519B2 (en) | D-hydantoinase from ochrobactrum anthropi | |
| WO2018029097A1 (en) | Method for synthesising amides | |
| CA2480301A1 (en) | Process for preparing optically active beta-aminocarboxylic acids from racemic n-acylated beta-aminocarboxylic acids | |
| JP2557614B2 (ja) | １―アリールアルキルエステルのエナンチオ選択的切断のための微生物エステラーゼ | |
| KR100244054B1 (ko) | 디-엔-카르바모일-알파-아미노산의 제조법 | |
| Żądło‐Dobrowolska et al. | Other Carbon–Nitrogen Bond‐Forming Biotransformations | |
| CN112143718A (zh) | 一种双功能酶生物催化剂及其制备方法和应用 | |
| EP1446492A2 (en) | Process for the preparation of an enantiomerically enriched a-amino acid | |
| JPH03210183A (ja) | エステルヒドロラーゼ遺伝子の大腸菌内でのクローニング、発現、および配列決定 | |
| Kittelmann et al. | Isolation and characterization of N-acetyldehydroleucine acylase, a new enzyme from Zoogloea ramigera | |
| Soriano Maldonado et al. | Amidohydrolase Process: Expanding the use ofl-N-carbamoylase/N-succinyl-amino acid racemase tandem for theproduction of different optically pure l-amino acids | |
| CS228431B1 (cs) | Způsob dělení optických isomerů derivátů fenylalaninu substituovaných v p-poloze | |
| MXPA99003870A (en) | Mutant penicillin g acylases |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| FC9A | Refused patent application |