CA2347079A1 - Aminoacylase et son utilisation pour la preparation de d-acides amines - Google Patents
Aminoacylase et son utilisation pour la preparation de d-acides amines Download PDFInfo
- Publication number
- CA2347079A1 CA2347079A1 CA002347079A CA2347079A CA2347079A1 CA 2347079 A1 CA2347079 A1 CA 2347079A1 CA 002347079 A CA002347079 A CA 002347079A CA 2347079 A CA2347079 A CA 2347079A CA 2347079 A1 CA2347079 A1 CA 2347079A1
- Authority
- CA
- Canada
- Prior art keywords
- ala
- gly
- leu
- arg
- val
- 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.)
- Abandoned
Links
- 238000004519 manufacturing process Methods 0.000 title claims description 9
- 150000008574 D-amino acids Chemical class 0.000 title abstract description 7
- ULGJWNIHLSLQPZ-UHFFFAOYSA-N 7-[(6,8-dichloro-1,2,3,4-tetrahydroacridin-9-yl)amino]-n-[2-(1h-indol-3-yl)ethyl]heptanamide Chemical compound C1CCCC2=NC3=CC(Cl)=CC(Cl)=C3C(NCCCCCCC(=O)NCCC=3C4=CC=CC=C4NC=3)=C21 ULGJWNIHLSLQPZ-UHFFFAOYSA-N 0.000 title description 3
- 108010003977 aminoacylase I Proteins 0.000 title description 3
- 108090000790 Enzymes Proteins 0.000 claims abstract description 42
- 102000004190 Enzymes Human genes 0.000 claims abstract description 42
- 238000006243 chemical reaction Methods 0.000 claims abstract description 30
- DZTHIGRZJZPRDV-GFCCVEGCSA-N N-acetyl-D-tryptophan Chemical compound C1=CC=C2C(C[C@@H](NC(=O)C)C(O)=O)=CNC2=C1 DZTHIGRZJZPRDV-GFCCVEGCSA-N 0.000 claims abstract description 7
- 230000003301 hydrolyzing effect Effects 0.000 claims abstract description 4
- KDIADSRGMZXPPV-ZCFIWIBFSA-N (2r)-2-[acetyl(thiophen-2-yl)amino]propanoic acid Chemical compound OC(=O)[C@@H](C)N(C(C)=O)C1=CC=CS1 KDIADSRGMZXPPV-ZCFIWIBFSA-N 0.000 claims abstract description 3
- HLORMWAKCPDIPU-SNVBAGLBSA-N (2r)-2-acetamido-3-(4-chlorophenyl)propanoic acid Chemical compound CC(=O)N[C@@H](C(O)=O)CC1=CC=C(Cl)C=C1 HLORMWAKCPDIPU-SNVBAGLBSA-N 0.000 claims abstract 2
- 239000000758 substrate Substances 0.000 claims description 27
- 238000000034 method Methods 0.000 claims description 17
- 235000001014 amino acid Nutrition 0.000 claims description 13
- 150000001413 amino acids Chemical class 0.000 claims description 12
- 239000012634 fragment Substances 0.000 claims description 12
- 244000005700 microbiome Species 0.000 claims description 6
- 239000000203 mixture Substances 0.000 claims description 5
- 230000005764 inhibitory process Effects 0.000 claims description 3
- 238000002360 preparation method Methods 0.000 claims description 3
- 230000002209 hydrophobic effect Effects 0.000 claims description 2
- 102000040430 polynucleotide Human genes 0.000 claims 2
- 108091033319 polynucleotide Proteins 0.000 claims 2
- 239000002157 polynucleotide Substances 0.000 claims 2
- 125000003275 alpha amino acid group Chemical group 0.000 claims 1
- 238000012258 culturing Methods 0.000 claims 1
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 42
- 210000004027 cell Anatomy 0.000 description 20
- 101710097070 D-aminoacylase Proteins 0.000 description 19
- 230000000694 effects Effects 0.000 description 19
- 229940024606 amino acid Drugs 0.000 description 14
- 239000000243 solution Substances 0.000 description 13
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 12
- 238000007792 addition Methods 0.000 description 11
- 108090000623 proteins and genes Proteins 0.000 description 11
- 239000000047 product Substances 0.000 description 9
- 238000010511 deprotection reaction Methods 0.000 description 8
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 8
- 108020004414 DNA Proteins 0.000 description 7
- 238000006460 hydrolysis reaction Methods 0.000 description 7
- 241000588986 Alcaligenes Species 0.000 description 6
- XEKOWRVHYACXOJ-UHFFFAOYSA-N Ethyl acetate Chemical compound CCOC(C)=O XEKOWRVHYACXOJ-UHFFFAOYSA-N 0.000 description 6
- 108091028043 Nucleic acid sequence Proteins 0.000 description 6
- 230000007062 hydrolysis Effects 0.000 description 6
- 241000282326 Felis catus Species 0.000 description 5
- 239000013612 plasmid Substances 0.000 description 5
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- 239000007787 solid Substances 0.000 description 5
- UJGRZQYSNYTCAX-SRVKXCTJSA-N Asp-Leu-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CC(O)=O UJGRZQYSNYTCAX-SRVKXCTJSA-N 0.000 description 4
- QOJJMJKTMKNFEF-ZKWXMUAHSA-N Asp-Val-Ser Chemical compound OC[C@@H](C(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@@H](N)CC(O)=O QOJJMJKTMKNFEF-ZKWXMUAHSA-N 0.000 description 4
- 239000007983 Tris buffer Substances 0.000 description 4
- KOSRFJWDECSPRO-UHFFFAOYSA-N alpha-L-glutamyl-L-glutamic acid Natural products OC(=O)CCC(N)C(=O)NC(CCC(O)=O)C(O)=O KOSRFJWDECSPRO-UHFFFAOYSA-N 0.000 description 4
- 108010038633 aspartylglutamate Proteins 0.000 description 4
- 238000005516 engineering process Methods 0.000 description 4
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- 230000000977 initiatory effect Effects 0.000 description 4
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- 239000000725 suspension Substances 0.000 description 4
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 4
- ADSGHMXEAZJJNF-DCAQKATOSA-N Ala-Pro-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@@H]1CCCN1C(=O)[C@H](C)N ADSGHMXEAZJJNF-DCAQKATOSA-N 0.000 description 3
- 241000588724 Escherichia coli Species 0.000 description 3
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 3
- WNGVUZWBXZKQES-YUMQZZPRSA-N Leu-Ala-Gly Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](C)C(=O)NCC(O)=O WNGVUZWBXZKQES-YUMQZZPRSA-N 0.000 description 3
- CWFYZYQMUDWGTI-GUBZILKMSA-N Met-Arg-Asp Chemical compound [H]N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(O)=O CWFYZYQMUDWGTI-GUBZILKMSA-N 0.000 description 3
- YBAFDPFAUTYYRW-UHFFFAOYSA-N N-L-alpha-glutamyl-L-leucine Natural products CC(C)CC(C(O)=O)NC(=O)C(N)CCC(O)=O YBAFDPFAUTYYRW-UHFFFAOYSA-N 0.000 description 3
- IGROJMCBGRFRGI-YTLHQDLWSA-N Thr-Ala-Ala Chemical compound C[C@@H](O)[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(O)=O IGROJMCBGRFRGI-YTLHQDLWSA-N 0.000 description 3
- 108010047495 alanylglycine Proteins 0.000 description 3
- 108010068380 arginylarginine Proteins 0.000 description 3
- 230000036983 biotransformation Effects 0.000 description 3
- 238000005356 chiral GC Methods 0.000 description 3
- 235000019439 ethyl acetate Nutrition 0.000 description 3
- 230000014509 gene expression Effects 0.000 description 3
- 108010055341 glutamyl-glutamic acid Proteins 0.000 description 3
- 108010050848 glycylleucine Proteins 0.000 description 3
- 230000010354 integration Effects 0.000 description 3
- 238000012423 maintenance Methods 0.000 description 3
- 230000000813 microbial effect Effects 0.000 description 3
- 239000013615 primer Substances 0.000 description 3
- 108010061238 threonyl-glycine Proteins 0.000 description 3
- 230000002103 transcriptional effect Effects 0.000 description 3
- QKWRJUOQPQWTEH-SNVBAGLBSA-N (2r)-2-[acetyl(naphthalen-2-yl)amino]propanoic acid Chemical compound C1=CC=CC2=CC(N(C(C)=O)[C@H](C)C(O)=O)=CC=C21 QKWRJUOQPQWTEH-SNVBAGLBSA-N 0.000 description 2
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 2
- WQVFQXXBNHHPLX-ZKWXMUAHSA-N Ala-Ala-His Chemical compound C[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@@H](Cc1cnc[nH]1)C(O)=O WQVFQXXBNHHPLX-ZKWXMUAHSA-N 0.000 description 2
- JBVSSSZFNTXJDX-YTLHQDLWSA-N Ala-Ala-Thr Chemical compound C[C@@H](O)[C@@H](C(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](C)N JBVSSSZFNTXJDX-YTLHQDLWSA-N 0.000 description 2
- QDRGPQWIVZNJQD-CIUDSAMLSA-N Ala-Arg-Gln Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(N)=O)C(O)=O QDRGPQWIVZNJQD-CIUDSAMLSA-N 0.000 description 2
- OKEWAFFWMHBGPT-XPUUQOCRSA-N Ala-His-Gly Chemical compound OC(=O)CNC(=O)[C@@H](NC(=O)[C@@H](N)C)CC1=CN=CN1 OKEWAFFWMHBGPT-XPUUQOCRSA-N 0.000 description 2
- DVJSJDDYCYSMFR-ZKWXMUAHSA-N Ala-Ile-Gly Chemical compound [H]N[C@@H](C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(O)=O DVJSJDDYCYSMFR-ZKWXMUAHSA-N 0.000 description 2
- CCDFBRZVTDDJNM-GUBZILKMSA-N Ala-Leu-Glu Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(O)=O CCDFBRZVTDDJNM-GUBZILKMSA-N 0.000 description 2
- DHBKYZYFEXXUAK-ONGXEEELSA-N Ala-Phe-Gly Chemical compound OC(=O)CNC(=O)[C@@H](NC(=O)[C@@H](N)C)CC1=CC=CC=C1 DHBKYZYFEXXUAK-ONGXEEELSA-N 0.000 description 2
- AAWLEICNDUHIJM-MBLNEYKQSA-N Ala-Thr-His Chemical compound C[C@H]([C@@H](C(=O)N[C@@H](CC1=CN=CN1)C(=O)O)NC(=O)[C@H](C)N)O AAWLEICNDUHIJM-MBLNEYKQSA-N 0.000 description 2
- OTOXOKCIIQLMFH-KZVJFYERSA-N Arg-Ala-Thr Chemical compound C[C@@H](O)[C@@H](C(O)=O)NC(=O)[C@H](C)NC(=O)[C@@H](N)CCCN=C(N)N OTOXOKCIIQLMFH-KZVJFYERSA-N 0.000 description 2
- OTCJMMRQBVDQRK-DCAQKATOSA-N Arg-Asp-Leu Chemical compound [H]N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(O)=O OTCJMMRQBVDQRK-DCAQKATOSA-N 0.000 description 2
- DPLFNLDACGGBAK-KKUMJFAQSA-N Arg-Phe-Glu Chemical compound C1=CC=C(C=C1)C[C@@H](C(=O)N[C@@H](CCC(=O)O)C(=O)O)NC(=O)[C@H](CCCN=C(N)N)N DPLFNLDACGGBAK-KKUMJFAQSA-N 0.000 description 2
- YNSUUAOAFCVINY-OSUNSFLBSA-N Arg-Thr-Ile Chemical compound [H]N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H]([C@@H](C)CC)C(O)=O YNSUUAOAFCVINY-OSUNSFLBSA-N 0.000 description 2
- GHODABZPVZMWCE-FXQIFTODSA-N Asp-Glu-Glu Chemical compound OC(=O)C[C@H](N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(O)=O GHODABZPVZMWCE-FXQIFTODSA-N 0.000 description 2
- VFUXXFVCYZPOQG-WDSKDSINSA-N Asp-Glu-Gly Chemical compound [H]N[C@@H](CC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)NCC(O)=O VFUXXFVCYZPOQG-WDSKDSINSA-N 0.000 description 2
- QCVXMEHGFUMKCO-YUMQZZPRSA-N Asp-Gly-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)CNC(=O)[C@@H](N)CC(O)=O QCVXMEHGFUMKCO-YUMQZZPRSA-N 0.000 description 2
- XLILXFRAKOYEJX-GUBZILKMSA-N Asp-Leu-Gln Chemical compound [H]N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(O)=O XLILXFRAKOYEJX-GUBZILKMSA-N 0.000 description 2
- KPSHWSWFPUDEGF-FXQIFTODSA-N Asp-Pro-Ala Chemical compound OC(=O)[C@H](C)NC(=O)[C@@H]1CCCN1C(=O)[C@@H](N)CC(O)=O KPSHWSWFPUDEGF-FXQIFTODSA-N 0.000 description 2
- MNQMTYSEKZHIDF-GCJQMDKQSA-N Asp-Thr-Ala Chemical compound [H]N[C@@H](CC(O)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](C)C(O)=O MNQMTYSEKZHIDF-GCJQMDKQSA-N 0.000 description 2
- 241000894006 Bacteria Species 0.000 description 2
- XMVZMBGFIOQONW-GARJFASQSA-N Cys-Lys-Pro Chemical compound C1C[C@@H](N(C1)C(=O)[C@H](CCCCN)NC(=O)[C@H](CS)N)C(=O)O XMVZMBGFIOQONW-GARJFASQSA-N 0.000 description 2
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- GBRUQFBAJOKCTF-DCAQKATOSA-N Pro-His-Asp Chemical compound [H]N1CCC[C@H]1C(=O)N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CC(O)=O)C(O)=O GBRUQFBAJOKCTF-DCAQKATOSA-N 0.000 description 2
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- YMAWOPBAYDPSLA-UHFFFAOYSA-N glycylglycine Chemical compound [NH3+]CC(=O)NCC([O-])=O YMAWOPBAYDPSLA-UHFFFAOYSA-N 0.000 description 1
- 108010040030 histidinoalanine Proteins 0.000 description 1
- 108010018006 histidylserine Proteins 0.000 description 1
- 150000001469 hydantoins Chemical class 0.000 description 1
- 238000005984 hydrogenation reaction Methods 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 238000011081 inoculation Methods 0.000 description 1
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- 239000000543 intermediate Substances 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
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- 108010044374 isoleucyl-tyrosine Proteins 0.000 description 1
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 1
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- 229960004452 methionine Drugs 0.000 description 1
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- 239000002547 new drug Substances 0.000 description 1
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- 229960005190 phenylalanine Drugs 0.000 description 1
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- 229920001451 polypropylene glycol Polymers 0.000 description 1
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- ONDSBJMLAHVLMI-UHFFFAOYSA-N trimethylsilyldiazomethane Chemical compound C[Si](C)(C)[CH-][N+]#N ONDSBJMLAHVLMI-UHFFFAOYSA-N 0.000 description 1
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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
- 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
- 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
- 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
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- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Microbiology (AREA)
- General Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Biomedical Technology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Analytical Chemistry (AREA)
- Enzymes And Modification Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Abstract
Enzyme isolé capable d'hydrolyser N-acétyl-D-tryptophane à une concentration de substrat de 10 g/l et exerçant une conversion plus rapide de (R)-N-acétyl-2-thiènylalanine que de (R)-N-acétyl-4-chlorophénylalanine. Cet enzyme est utile pour préparer des D-acides aminés.
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB9822947.9 | 1998-10-20 | ||
| GBGB9822947.9A GB9822947D0 (en) | 1998-10-20 | 1998-10-20 | Aminoacylase and its use in the production of d-aminoacids |
| GBGB9907739.8A GB9907739D0 (en) | 1999-04-01 | 1999-04-01 | Aminoacylase and its use in the production of D-aminoacids |
| GB9907739.8 | 1999-04-01 | ||
| PCT/GB1999/003458 WO2000023598A1 (fr) | 1998-10-20 | 1999-10-20 | Aminoacylase et son utilisation pour la preparation de d-acides amines |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2347079A1 true CA2347079A1 (fr) | 2000-04-27 |
Family
ID=26314541
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA002347079A Abandoned CA2347079A1 (fr) | 1998-10-20 | 1999-10-20 | Aminoacylase et son utilisation pour la preparation de d-acides amines |
Country Status (6)
| Country | Link |
|---|---|
| EP (1) | EP1121446A1 (fr) |
| JP (1) | JP2002527110A (fr) |
| KR (1) | KR20010075649A (fr) |
| AU (1) | AU6222799A (fr) |
| CA (1) | CA2347079A1 (fr) |
| WO (1) | WO2000023598A1 (fr) |
Families Citing this family (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP4526157B2 (ja) | 2000-01-27 | 2010-08-18 | ダイセル化学工業株式会社 | D−アミノアシラーゼ、およびそれをコードする遺伝子 |
| KR20020087948A (ko) * | 2001-02-01 | 2002-11-23 | 미쯔이가가꾸가부시끼가이샤 | 신규 d-아미노아실라제를 코딩하는 dna 및 그것을사용한 d-아미노산의 제조 방법 |
| EP1435388B1 (fr) | 2002-12-24 | 2012-12-12 | Daicel Corporation | Mutants de la D-aminoacylase d'Alcaligenes denitrificans pour une meilleure producion d'aminoacides-D |
| CN108624577B (zh) * | 2017-03-22 | 2021-07-27 | 中国科学院天津工业生物技术研究所 | 用于催化n-乙酰-d-色氨酸水解生成d-色氨酸的新酶 |
| KR20220096237A (ko) | 2020-12-30 | 2022-07-07 | 이종학 | 수산물 유통 서비스 시스템 |
Family Cites Families (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS5037277B2 (fr) * | 1972-08-31 | 1975-12-01 | ||
| JPS5233194B2 (fr) * | 1973-04-24 | 1977-08-26 | ||
| JPS62126976A (ja) * | 1985-11-26 | 1987-06-09 | Agency Of Ind Science & Technol | D−アミノアシラ−ゼの製造法 |
| JPH0783711B2 (ja) * | 1987-06-29 | 1995-09-13 | ダイセル化学工業株式会社 | 新規なd―アミノアシラーゼの製造法 |
| US4981799A (en) * | 1987-08-21 | 1991-01-01 | Takeda Chemical Industries, Ltd. | Acylamino acid racemase, production and use thereof |
| JP2869793B2 (ja) * | 1989-03-07 | 1999-03-10 | 第一化学薬品株式会社 | 酸性d―アミノ酸に作用するd―アミノアシラーゼ及びその製造法 |
| US5206162A (en) * | 1991-10-17 | 1993-04-27 | National Science Council Of Republic Of China | Process for making D-aminoacylase |
| JP4063400B2 (ja) * | 1997-07-31 | 2008-03-19 | ダイセル化学工業株式会社 | D−アミノアシラーゼ |
-
1999
- 1999-10-20 CA CA002347079A patent/CA2347079A1/fr not_active Abandoned
- 1999-10-20 KR KR1020017004943A patent/KR20010075649A/ko not_active Ceased
- 1999-10-20 JP JP2000577305A patent/JP2002527110A/ja active Pending
- 1999-10-20 AU AU62227/99A patent/AU6222799A/en not_active Abandoned
- 1999-10-20 EP EP99949259A patent/EP1121446A1/fr not_active Withdrawn
- 1999-10-20 WO PCT/GB1999/003458 patent/WO2000023598A1/fr not_active Ceased
Also Published As
| Publication number | Publication date |
|---|---|
| JP2002527110A (ja) | 2002-08-27 |
| WO2000023598A1 (fr) | 2000-04-27 |
| KR20010075649A (ko) | 2001-08-09 |
| EP1121446A1 (fr) | 2001-08-08 |
| AU6222799A (en) | 2000-05-08 |
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