US20060228787A1 - Mutants for the preparation of d-amino acids - Google Patents
Mutants for the preparation of d-amino acids Download PDFInfo
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- US20060228787A1 US20060228787A1 US10/527,061 US52706105A US2006228787A1 US 20060228787 A1 US20060228787 A1 US 20060228787A1 US 52706105 A US52706105 A US 52706105A US 2006228787 A1 US2006228787 A1 US 2006228787A1
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- amino acids
- recombinant microorganism
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- 0 *[C@@H](N)C(=O)O.*[C@@H](N)C(=O)O.*[C@@H](NC(N)=O)C(=O)O.*[C@@H](NC(N)=O)C(=O)O.*[C@@H]1NC(=O)NC1=O.*[C@@H]1NC(=O)NC1=O.*[C@H](NC(N)=O)C(=O)O.*[C@H](NC(N)=O)C(=O)O.*[C@H]1NC(=O)NC1=O.*[C@H]1NC(=O)NC1=O Chemical compound *[C@@H](N)C(=O)O.*[C@@H](N)C(=O)O.*[C@@H](NC(N)=O)C(=O)O.*[C@@H](NC(N)=O)C(=O)O.*[C@@H]1NC(=O)NC1=O.*[C@@H]1NC(=O)NC1=O.*[C@H](NC(N)=O)C(=O)O.*[C@H](NC(N)=O)C(=O)O.*[C@H]1NC(=O)NC1=O.*[C@H]1NC(=O)NC1=O 0.000 description 1
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- 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
- C12N1/00—Microorganisms, e.g. protozoa; Compositions thereof; Processes of propagating, maintaining or preserving microorganisms or compositions thereof; Processes of preparing or isolating a composition containing a microorganism; Culture media therefor
- C12N1/20—Bacteria; Culture media therefor
- C12N1/205—Bacterial isolates
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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
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- 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.)
- C12N9/0012—Oxidoreductases (1.) acting on nitrogen containing compounds as donors (1.4, 1.5, 1.6, 1.7)
- C12N9/0014—Oxidoreductases (1.) acting on nitrogen containing compounds as donors (1.4, 1.5, 1.6, 1.7) acting on the CH-NH2 group of donors (1.4)
- C12N9/0022—Oxidoreductases (1.) acting on nitrogen containing compounds as donors (1.4, 1.5, 1.6, 1.7) acting on the CH-NH2 group of donors (1.4) with oxygen as acceptor (1.4.3)
- C12N9/0024—D-Amino acid oxidase (1.4.3.3)
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- 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)
- C12N9/86—Hydrolases (3) acting on carbon to nitrogen bonds other than peptide bonds (3.5) acting on amide bonds in cyclic amides, e.g. penicillinase (3.5.2)
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- 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
- C12N9/90—Isomerases (5.)
-
- 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
- C12P41/009—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 hydantoins or carbamoylamino compounds
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12R—INDEXING SCHEME ASSOCIATED WITH SUBCLASSES C12C - C12Q, RELATING TO MICROORGANISMS
- C12R2001/00—Microorganisms ; Processes using microorganisms
- C12R2001/01—Bacteria or Actinomycetales ; using bacteria or Actinomycetales
- C12R2001/185—Escherichia
- C12R2001/19—Escherichia coli
Definitions
- the present invention relates to a process for the preparation of D-amino acids.
- these are obtained enzymatically via the so-called hydantoinase route using recombinant microorganisms.
- the present invention likewise relates to microorganisms modified in this way.
- D-Amino acids are compounds which are often employed in organic synthesis as intermediates for the preparation of pharmaceutical active compounds.
- Enzymatic hydrolysis of 5-substituted hydantoins to give N-carbamoyl-amino acids and further reaction thereof to give the corresponding enantiomerically enriched amino acids is a standard method in organic chemistry (“Enzyme Catalysis in Organic Synthesis”, eds.: Drauz, Waldmann, VCH, 1st and 2nd ed.).
- the enantiodifferentiation can take place here either at the stage of hydantoin hydrolysis by hydantoinases, or optionally during cleavage of N-carbamoylamino acids by means of enantioselective carbamoylases.
- FIG. 1 shows the conversion of hydroxymethylhydantoin and ethylhydantoin with E. coli JM109 transformed with a D-carbamoylase and D-hydantoinase from Arthrobacter crystallopoietes DSM 20117 (in accordance with the patent application DE10114999.9 and DE10130169.3).
- the reaction conditions are chosen according to example 1.
- FIG. 1 shows by way of example, in the conversion of various 5-monosubstituted hydantoins, marked breakdown of the D-amino acids formed takes place. This reduces the yield which can be achieved and makes working up of the product difficult.
- D-amino acid oxidases [EC 1.4.3.3], D-amino acid dehydrogenases [EC 1.4.99.1], D-amino acid aminotransferases [EC 2.6.1.21], D-amino acid N-acetyltransferases [EC 2.3.1.36], D-hydroxyamino acid dehydratases [EC 4.2.1.14] and D-amino acid racemases [EC 5.1.1.10] can participate in the breakdown of D-amino acids.
- D-amino acid oxidases [EC 1.4.3.3]
- D-amino acid dehydrogenases [EC 1.4.99.1]
- D-amino acid aminotransferases [EC 2.6.1.21]
- D-amino acid N-acetyltransferases [EC 2.3.1.36]
- D-hydroxyamino acid dehydratases [EC 4.2.1.14]
- D-amino acid racemases [EC 5.1.1.10]
- the object of the present invention was therefore to provide a microorganism which is capable of production of D-amino acids via the carbamoylase/hydantoinase route and helps to render possible a higher yield of D-amino acid produced. It should be possible to employ this advantageously on an industrial scale under economic and ecological aspects. In particular, it should have very good growth properties under the usual economically appropriate conditions, and a sufficient genetic and physical stability and a sufficiently fast rate of conversion for hydantoins.
- Claims 1 to 5 relate to particular microorganisms modified in this way, while claims 6 and 7 protect a process for the preparation of D-amino acids.
- Microorganisms for recombinant embodiments which can be used are in principle all the organisms possible to the expert for this purpose, such as fungi, e.g. Aspergillus sp., Streptomyces sp., Hansenula polymorpha, Pichia pastoris and Saccharomyces cerevisiae, or also prokaryotes, such as E. coli and Bacillus sp.
- fungi e.g. Aspergillus sp., Streptomyces sp., Hansenula polymorpha, Pichia pastoris and Saccharomyces cerevisiae
- prokaryotes such as E. coli and Bacillus sp.
- Microorganisms of the genus Escherichia coli can be regarded as preferred microorganisms according to the invention. The following are very particularly preferred: E.
- Organisms modified in this way can be produced by methods familiar to the expert. This serves to multiply and produce a sufficient amount of the recombinant enzymes. The processes for this are well-known to the expert (Sambrook, J.; Fritsch, E. F. and Maniatis, T. (1989), Molecular cloning: a laboratory manual, 2nd ed., Cold Spring Harbor Laboratory Press, New York).
- the said nucleic acid sequences are thus cloned into a host organism with plasmids or vectors by known methods and the polypeptides expressed in this way can be detected with suitable screening methods. All the possible detection reactions for the molecules formed are in principle suitable for the detection.
- detection reactions which are suitable in principle are all the possible detection reactions for ammonia and ammonium ions, such as Nessler reagent (Vogel, A., I., (1989) Vogel's textbook of quantitative chemical analysis, John Wiley & Sons, Inc., 5 th ed., 679-698, New York), the indophenol reaction, also called Berthelot's reaction (Wagner, R., (1969) Neuesynthesis zur Stickstoffanalytik in der Wasserchemie, Vom Wasser, VCH-Verlag, vol. 36, 263-318, Weinheim), in particular enzymatic determination by means of glutamate dehydrogenase (Bergmeyer, H., U., and Beutler, H.-O.
- Possible plasmids or vectors are in principle all the embodiments available to the expert for this purpose.
- Such plasmids and vectors can be found e.g. in Studier and colleagues (Studier, W. F.; Rosenberg A. H.; Dunn J. J.; Dubendroff J. W.; (1990), Use of the T7 RNA polymerase to direct expression of cloned genes, Methods Enzymol. 185, 61-89) or the brochures of Novagen, Promega, New England Biolabs, Clontech or Gibco BRL. Further preferred plasmids and vectors can be found in: Glover, D. M. (1985), DNA cloning: A Practical Approach, vol.
- Particularly preferred cloning vectors of D-carbamoylases in E. coli are, for example, derivatives of pBR322, pACYC184, pUC18 or pSC101, which can carry constitutive and also inducible promoters for expression control.
- Particularly preferred promoters are lac, tac, trp, trc, T3, T5, T7, rhaBAD, araBAD, ⁇ pL and phoA promoters, which are sufficiently known to the expert [Strategies for achieving high-level expression of genes in Escherichia coli, Makrides S. C. Microbiol.Rev. 60(3), 512-538].
- D-amino acid oxidase (dadA) or D-serine dehydratase (dsdA) of these organisms is carried out here by methods described above, which are known to the expert.
- D-serine dehydratase- or D-amino acid oxidase-deficient strains with D-carbamoylase activity the fundamental molecular biology methods are thus known to the expert (Sambrook, J.; Fritsch, E. F. and Maniatis, T. (1989), Molecular cloning: a laboratory manual, 2nd ed., Cold Spring Harbor Laboratory Press, New York).
- hydantoinases which are to be employed here are those from Thermus sp., Bacillus sp., Mycobacterium sp., Corynebacterium sp., Agrobacterium sp., E. coli, Burkholderia sp., Pseudomonas sp., or Arthrobacter sp.
- Hydantoin racemase can preferably be used from Pseudomonas sp., Arthrobacter sp., or Agrobacterium sp., optionally with the addition of auxiliary substances, such as metal ions, for example Mn 2+ ions.
- a hydantoin is converted with the said cells or cell constituents in a suitable solvent, such as, for example, water, to which further water-soluble or water-insoluble organic solvents can be added, at pH values of between 6.0 and 11, preferably between 7 and 10, and a temperature of between 10° C. and 100° C., preferably between 30° C. and 70° C., particularly preferably between 37° C. and 60° C.
- a suitable solvent such as, for example, water, to which further water-soluble or water-insoluble organic solvents can be added, at pH values of between 6.0 and 11, preferably between 7 and 10, and a temperature of between 10° C. and 100° C., preferably between 30° C. and 70° C., particularly preferably between 37° C. and 60° C.
- the enzymes in question can also be used in the free form for the use.
- the enzymes can furthermore also be employed as a constituent of an intact guest organism or in combination with the broken-down cell mass of the host organism, which has been pur
- the recombinant cells in flocculated, cross-linked or immobilized form, for example using agar, agarose, carrageenan, alginates, pectins, chitosan, polyacrylamides and other synthetic carriers (Chemical aspects of immobilized systems in biotechnologies. Navratil, Marian; Sturdik, Ernest. Chemicke Listy (2000), 94(6), 380-388; Industrial applications of immobilized biocatalysts and biomaterials. Chibata, Ichiro. Advances in Molecular and Cell Biology (1996), 15A(Biochemical Technology), 151-160; Immobilization of genetically engineered cells: a new strategy for higher stability. Kumar, P. K. R.; Schuegerl, K. Journal of Biotechnology (1990), 14(3-4), 255-72.).
- D-Aminobutyric acid, D-serine, D-methionine, D-tryptophan and D-phenylalanine are preferably prepared.
- Organisms with D-carbamoylase-active and hydantoinase-active and dadA-inactivated and/or dsdA-inactivated cells are preferably used in this process for the preparation of D-amino acids. It should be mentioned here that both L-, D- or DL-carbamoylamino acids and 5-monosubstituted hydantoins, which can be converted into the corresponding carbamoylamino acids via sufficiently known hydantoinases, are possible as the educt (“Enzyme Catalysis in Organic Synthesis”, eds.: Drauz, Waldmann, VCH, 1 st and 2 nd ed.).
- dadA- and/or dsdA-deficient strains used can co-express here the carbamoylase and hydantoinase, optionally also a hydantoin racemase or carbamoylamino acid racemase, and can be employed either in the free or in the immobilized form (see above).
- DSM15181 (ET3) and DSM15182 (ET4) were deposited by Degussa AG on Apr. 09, 2002 at the Deutsche Sammlung fur Mikroorganismen und Zellkulturen [German Collection of Microorganisms and Cell Cultures], Mascheroder Weg 1b, D-38124 Braunschweig.
- the E. coli cells transformed with pJAVIER16 were placed individually on LBamp plates (ampicillin concentration: 100 ⁇ g/ml).
- 2.5 ml LBamp medium with 1 mM ZnCl 2 were inoculated with an individual colony and incubated for 30 hours at 37° C. and 250 rpm.
- This culture was diluted 1:50 in 100 ml LBamp medium with 1 mM ZnCl 2 and 2 g/l rhamnose and incubated for 18 h at 30° C.
- the culture was centrifuged for 10 min at 10,000 g, the supernatant was discarded and the biomass was weighed.
- Various hydantoin derivatives e.g.
- DadA was deleted in E. coli BW25113 (deposited at CGSC under number CGSC7636) by the method described by Datsenko & Wanner (One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products, Datsenko, Kirill A. and Wanner, Barry L. PNAS (2000), 97(12), 6640-6645)
- the following primers were used for this for amplification of the chloramphenicol resistance from pKD13 (deposited at CGSC under number CGSC7633): 5′_AACCAGTGCCGCGAATGCCGGGCAAATCTCCCCCGGATATGCTGCAC CGTATTCCGGGGATCCGTCGACC_3′: Seq. 5 5′_AGGGGTACCGGTAGGCGCGTGGCGCGGATAACCGTCGGCGATTCCGG GGATCCGTCGACC-3′ Seq. 6
- E. coli BW25113 (pKD46) (deposited at CGSC under number CGSC7630) and selection of kanamycin-resistant clones rendered possible the isolation of E. coli ET2.
- the chloramphenicol resistance from pKD13 was in turn amplified with the following primers: 5′_GCGGGCACATTCCTGCTGTCATTTATCATCTAAGCGCAAAGAGACGT ACTGTGTAGGCTGGAGCTGCTTC_3′ Seq. 7 5′_GCAGCATCGCTCACCCAGGGAAAGGATTGCGATGCTGCGTTGAAACG TTAATGGGAATTAGCCATGGTCC_3′ : Seq. 8
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Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US12/357,218 US9194009B2 (en) | 2002-11-04 | 2009-01-21 | Mutants for the preparation of D-amino acids |
Applications Claiming Priority (3)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
DE10251184A DE10251184A1 (de) | 2002-11-04 | 2002-11-04 | Mutanten zur Herstellung von D-Aminosäuren |
DE102-51-184.5 | 2002-11-04 | ||
PCT/EP2003/011432 WO2004042047A1 (en) | 2002-11-04 | 2003-10-15 | Mutants for the preparation of d-amino acids |
Related Child Applications (1)
Application Number | Title | Priority Date | Filing Date |
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US12/357,218 Continuation US9194009B2 (en) | 2002-11-04 | 2009-01-21 | Mutants for the preparation of D-amino acids |
Publications (1)
Publication Number | Publication Date |
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US20060228787A1 true US20060228787A1 (en) | 2006-10-12 |
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ID=32103290
Family Applications (2)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
US10/527,061 Abandoned US20060228787A1 (en) | 2002-11-04 | 2003-10-15 | Mutants for the preparation of d-amino acids |
US12/357,218 Active 2026-03-29 US9194009B2 (en) | 2002-11-04 | 2009-01-21 | Mutants for the preparation of D-amino acids |
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US12/357,218 Active 2026-03-29 US9194009B2 (en) | 2002-11-04 | 2009-01-21 | Mutants for the preparation of D-amino acids |
Country Status (9)
Country | Link |
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US (2) | US20060228787A1 (de) |
EP (1) | EP1558727B1 (de) |
JP (1) | JP2006504428A (de) |
CN (1) | CN100510052C (de) |
AT (1) | ATE439430T1 (de) |
AU (1) | AU2003283269A1 (de) |
CA (1) | CA2511751A1 (de) |
DE (2) | DE10251184A1 (de) |
WO (1) | WO2004042047A1 (de) |
Families Citing this family (10)
Publication number | Priority date | Publication date | Assignee | Title |
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EP2521448A1 (de) | 2010-01-08 | 2012-11-14 | President and Fellows of Harvard College | Verfahren und beschichtungen zur bearbeitung von biofilmen |
WO2012151554A1 (en) | 2011-05-04 | 2012-11-08 | President And Fellows Of Harvard College | Polyamines for treating biofilms |
PL2780451T3 (pl) * | 2011-11-16 | 2018-03-30 | Evonik Technochemie Gmbh | Mutanty hydantoinazy |
CN107937377A (zh) * | 2017-11-09 | 2018-04-20 | 江南大学 | 一种d‑n‑氨甲酰水解酶及应用 |
WO2019183344A1 (en) | 2018-03-21 | 2019-09-26 | Case Western Reserve University | Thermoresponsive compositions and methods for preventing and disrupting biofilms |
CN110699396B (zh) * | 2019-11-15 | 2022-03-01 | 江南大学 | 一种级联反应制备d-芳香族氨基酸的方法 |
EP4105335A1 (de) | 2021-06-16 | 2022-12-21 | Evonik Operations GmbH | Enzymatisches verfahren zur herstellung von l-glufosinat-p-alkylestern |
WO2023174511A1 (en) | 2022-03-14 | 2023-09-21 | Evonik Operations Gmbh | Enzymatic method for the production of l-glufosinate p-esters |
CN116926139A (zh) * | 2022-04-12 | 2023-10-24 | 元素驱动(杭州)生物科技有限公司 | 一种n-乙酰-d-氨基酸、d-氨基酸、d-氨基酸衍生物的制备方法 |
WO2023232225A1 (en) | 2022-05-31 | 2023-12-07 | Evonik Operations Gmbh | Enzymatic method for the diastereoselective production of l-glufosinate p-esters |
Citations (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US6352848B1 (en) * | 1998-04-02 | 2002-03-05 | Degussa-Huls Aktiengesellschaft | Recombinant L-N-carbamoylase from Arthrobacter aurescens and method of producing L-amino acids therewith |
Family Cites Families (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
IT1277125B1 (it) * | 1995-12-21 | 1997-11-04 | Eniricerche Spa | Mutanti termostabili della d-n-alfa-carbamilasi |
US5728555A (en) * | 1996-09-30 | 1998-03-17 | Monsanto Company | Preparation of d-amino acids by direct fermentative means |
DE10114999A1 (de) * | 2001-03-26 | 2002-10-10 | Degussa | D-Carbamoylase aus Arthrobacter crystallopoietes DSM 20117 |
-
2002
- 2002-11-04 DE DE10251184A patent/DE10251184A1/de not_active Withdrawn
-
2003
- 2003-10-15 CA CA002511751A patent/CA2511751A1/en not_active Abandoned
- 2003-10-15 EP EP03775186A patent/EP1558727B1/de not_active Expired - Lifetime
- 2003-10-15 JP JP2004548747A patent/JP2006504428A/ja active Pending
- 2003-10-15 AT AT03775186T patent/ATE439430T1/de not_active IP Right Cessation
- 2003-10-15 CN CNB2003801024249A patent/CN100510052C/zh not_active Expired - Lifetime
- 2003-10-15 AU AU2003283269A patent/AU2003283269A1/en not_active Abandoned
- 2003-10-15 US US10/527,061 patent/US20060228787A1/en not_active Abandoned
- 2003-10-15 DE DE60328813T patent/DE60328813D1/de not_active Expired - Lifetime
- 2003-10-15 WO PCT/EP2003/011432 patent/WO2004042047A1/en active Application Filing
-
2009
- 2009-01-21 US US12/357,218 patent/US9194009B2/en active Active
Patent Citations (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US6352848B1 (en) * | 1998-04-02 | 2002-03-05 | Degussa-Huls Aktiengesellschaft | Recombinant L-N-carbamoylase from Arthrobacter aurescens and method of producing L-amino acids therewith |
Also Published As
Publication number | Publication date |
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JP2006504428A (ja) | 2006-02-09 |
DE10251184A1 (de) | 2004-05-13 |
ATE439430T1 (de) | 2009-08-15 |
CN100510052C (zh) | 2009-07-08 |
EP1558727A1 (de) | 2005-08-03 |
US20090203091A1 (en) | 2009-08-13 |
EP1558727B1 (de) | 2009-08-12 |
CA2511751A1 (en) | 2004-05-21 |
AU2003283269A1 (en) | 2004-06-07 |
US9194009B2 (en) | 2015-11-24 |
WO2004042047A1 (en) | 2004-05-21 |
DE60328813D1 (de) | 2009-09-24 |
CN1708583A (zh) | 2005-12-14 |
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