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(12) United States Patent (10) Patent No.: US 7,217,544 B2 Hummel Et Al

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(12) United States Patent (10) Patent No.: US 7,217,544 B2 Hummel Et Al US007217544B2 (12) United States Patent (10) Patent No.: US 7,217,544 B2 Hummel et al. (45) Date of Patent: May 15, 2007 (54) METHOD FOR THE PREPARATION OF (56) References Cited L-AMNO ACDS FROM D-AMNO ACDS U.S. PATENT DOCUMENTS (75) Inventors: Werner Hummel, Titz (DE); Birgit Geueke, Zürich (CH); Steffen Osswald 5,854,035 A 12/1998 Stoyan et al. ............... 435,116 s ?i. s 6,187.574 B1 2/2001 Garcia Lopez et al. ..... 435,189 Rodenbach (DE); Christoph 2003/0092033 A1* 5/2003 Weiner et al. ................. 435/6 Weckbecker, Grindau-Lieblos (DE); Klaus Huthmacher, Gelnhausen (DE) FOREIGN PATENT DOCUMENTS (73) Assignee: Degussa AG, Düsseldorf (DE) DE 10240 603 3, 2004 (*) Notice: Subject to any disclaimer, the term of this EP O 792 933 9, 1997 patent is extended or adjusted under 35 EP 1375 649 1, 2004 U.S.C. 154(b) by 0 days. OTHER PUBLICATIONS (21) Appl. No.: 11/056,165 de Graaf, et al., “Metabolic Engineering for L-Lysine Production by (22) Filed: Feb. 14, 2005 Coryneformbacterium glutamicum,’ Adv. Biochem. Eng. (Under 37 CFR 1.47) Biotechnol. 73:9-29 (20001). (65) Prior Publication Data (Continued) US 2006/OO63238 A1 Mar. 23, 2006 Primary Examiner Tekchand Saidha (30) Foreign Application Priority Data Assistant Examiner Iqbal Chowdhury Feb. 19, 2004 (DE) ...................... 10 2004 OO8 445 (74) Attorney, Agent, or Firm—Michael A. Sanzo; Law Office of Michael A. Sanzo, LLC (51) Int. Cl. CI2P I3/04 (2006.01) (57) ABSTRACT CI2P 2L/06 (2006.01) CI2N 9/06 (2006.01) The invention relates to recombinant microorganisms CI2N L/20 (2006.01) which, in comparison to the starting organism, have a higher CI2N 9/02 (2006.01) concentration or activity of a D-amino acid oxidase, of an C7H 2L/04 (2006.01) L-amino acid dehydrogenase, of an NADH cosubstrate (52) U.S. Cl. ................... 435/106; 435/191: 435/252.3: regenerating enzyme and, if necessary, of a catalase. The 435/189: 435/69. 1536/23.2 invention also includes methods for preparing L-amino acids (58) Field of Classification Search ................ 435/106, from D-amino acids using of these microorganisms. 435/191, 252.3, 189: 536/23.2 See application file for complete search history. 15 Claims, 3 Drawing Sheets T7Nde 6639 bps e pE2D 6478 bps US 7,217,544 B2 Page 2 OTHER PUBLICATIONS Nakajima, et al., “Enzymatic Conversion of Racemic Methionine to the L-Enantiomer,” J. Chem. Soc. Chem. Commun. 13:947-948 Enright, et al., “Stereoinversion of B- and Y-Substituted O-Amino Acids Using a Chemo-enzymatic Oxidation-Reduction Procedure.” (1990). Chem. Commun. 20:2636-2637 (2003). Patel, “Enzymatic Synthesis of Chiral Intermediates for Gabler, et al., “Detection and Substrate Selectivity of New Micro Omapatrilat, and Antihypertensive Drug.” Biomol. Eng. 17:167-182 bial D-Amino Acid Oxidases,” Enzyme and Microbial Tech. 27:605 (2001). 611 (2000). Sahm, et al., "Construction of L-Lysine, L-Threonine-, or Galkin, et al., “Synthesis of Optically Active Amino Acids from L-Isoleucine-Overproducing Strains of Corynebacterium O-Keto Acids with Escherichia coli Cells Expressing Heterologous Genes.” Appl. Environ. Microbiol. 63(12):4651-4656 (1997). glutamicum,’ Ann. N.Y. Acad. Sci. 782:25-39 (1996). Hanson, et al., “Enzymatic Synthesis of L-6-Hydroxynorleucine.” Schmid, et al., “The Use of Enzymes in the Chemical Industry in Biorg. Medicinal Chem. 7:2247-2252 (1999). Europe.” Curr: Opin. Biotechnol. 13(4):359-366 (2002). Lin, et al., “Expression of Trigonopsis variabilis D-Amino Acid Trost, et al., “Minimization of By-Product Formation During Oxidase Gene in Escherichia coli and Characterization of its D-Amino Acid Oxidase Catalyzed Racemate Resolution of D/L- Inactive Mutants.” Enzyme Microbiol. Technol. 27:482-491 (2000). Na Amnieh, “Entwicklung eines rekombinanten GanzZellsystems Amino Acids.” J. Mol. Cat. B. Enzymatic 19-20: 189-195 (2002). Klonierung, Coexpression und Mutagenese der phenylalanin English Language Abstract for Reference B1 (EP 0 792 933). Dehydrogenase aus Rhodococcus sp. M4 und des malic enzymes English Language Abstract for Reference B3 (DE 10240 603). aus E. coli K12, Dissertation, 2002, Universitat Dusseldorf. English Language Abstract. * cited by examiner U.S. Patent May 15, 2007 Sheet 2 of 3 US 7,217,544 B2 2 3 4. 5 6 7 8 Strain No. Figure 2 120 180 240 Time 1 min Figure 3 U.S. Patent May 15, 2007 Sheet 3 of 3 US 7,217,544 B2 e E G () - 60 120 180 240 Time f min Figure 4 US 7,217,544 B2 1. 2 METHOD FOR THE PREPARATION OF 7(10):2247–2252 (1999): Nakajima, et al., J. Chem. Soc. L-AMNO ACIDS FROM D-AMNO ACDS Chem. Commun. 13:947-8 (1990)). CROSS REFERENCE TO RELATED APPLICATIONS 5 D-AAO -- D. L-AA -- L-AA + Ketonic Acid + NH4 The present application claims priority to German appli 1N cation 10 2004 008 445.9, filed on Feb. 19, 2004, the FADox FADred contents of which is hereby incorporated by reference. 10 >-( Leu)H NADH CO2(+Pyruvate) FIELD OF THE INVENTION H2O % O2 Q )( FDH (MAE) NAD Formate The present invention relates to recombinant microorgan N-1 HO (Malat) isms which, in comparison to the starting organisms, have a Catalase 2 higher concentration or activity of: a) a D-amino acid 15 L-AA oxidase; b) an L-amino acid dehydrogenase; and c) an NADH cosubstrate-regenerating enzyme. In addition, the For a rapid and complete conversion in the cell-free recombinant microorganism may include a higher concen system, a catalase must also be present. This is needed tration or activity of a catalase. The invention is also directed because hydrogen peroxide is produced in the oxidative step to methods in which these microorganisms are used in the catalyzed by the amino acid oxidase and this leads to the preparation of L-amino acids from D-amino acids. decarboxylation of the ketonic acid and to deactivation of enzymes (Trost, et al., J. Mol. Catalysis B. Enzymatic BACKGROUND OF THE INVENTION 19–20:189-195 (2002)). The conversion of racemate into 25 enantiomerically pure amino acids is possible in this system Many natural amino acids are prepared in enantiomeri with >99% ee and >95% yield. However, this method is cally pure form by fermentation using genetically modified costly, since four different enzymes have to be separately bacteria (de Graaf, et al., Adv. Biochem. Eng. Biotechnol. prepared and isolated. 73:9-29 (2001); Sahm, et al., Ann. NY Acad. Sci. 782:25-39 (1996)). Although not all proteinogenic amino acids (and SUMMARY OF THE INVENTION only very few unnatural or D-amino acids) can be prepared 30 in this way, chemical syntheses for enantiomerically pure In its first aspect, the invention is directed to a recombi amino acids are very costly. As a result, several enzymatic nant microorganism, which has been engineered in Such a processes have been developed, and used on a scale of way that, compared to the starting organism, it has a higher several metric tons per year. The methods range from kinetic 35 concentration or activity of: a) a D-amino acid oxidase; b) an racemate cleavage with the aid of acylases, amidases, L-amino acid dehydrogenase; and c) an enzyme that regen esterases, hydantoinases, amino acid oxidases and proteases, erates NADH. The “starting organism' is the microorganism to enantioselective syntheses by means of lyases, ami prior to the performance of steps to increase activity, e.g., notransferases and dehydrogenases (Schmid, et al., Curr: prior to transformation with a vector encoding an enzyme. Opin. Biotechnol. 13(4):359-366 (2002)). 40 The recombinant microorganism may be made by trans In addition to enantioselective syntheses, enantiomeri forming the starting microorganism with one or more vec cally enriched amino acid preparations may be obtained by tors, that together encode: a D-amino acid oxidase; an dynamic kinetic racemate cleavages, in which the unwanted L-amino acid dehydrogenase; and an enzyme that regener enantiomer is racemized in situ. A 100% yield can be ates NADH. Thus, after transformation has been completed, achieved by combining a D- or L-amino acid oxidase with 45 the recombinant microorganism has at least one additional an unselective chemical reduction of the incipientimino acid copy of a polynucleotide; encoding a D-amino acid oxidase; back to the principal amino acid. The reducing agent, e.g., a polynucleotide encoding an L-amino acid dehydrogenase; NaBH must, however, be employed in an excess of at least and a polynucleotide encoding an enzyme that regenerates 25 equivalents, which makes this option very costly (Enright NADH. et al., Chemical Communications 20:2636–2637 (2003)). 50 Preferred D-amino acid oxidases include: the D-amino The amination of C-ketonic acids by amino acid dehy acid oxidase of arthrobacter protophormiae (accession drogenases is generally known. Although the educt is many number gi2140775); the D-amino acid oxidase of trigonop times more costly than, for example, the corresponding sis variabilis (accession number gi1616634); the D-aspar racemic amino acid, by coupling an amino acid oxidase with tate oxidase of bos taurus (accession number gi27806895); an amino acid dehydrogenase the corresponding ketonic 55 the D-amino acid oxidase of rhodosporidium; and the acid can be obtained in situ from an amino acid. When both D-amino acid oxidase of rhototorula gracillis. Preferred of the enzymes have the opposite enantio-Selectivity, a L-amino acid dehydrogenases include: the L-leucine dehy D-amino acid can be completely converted into an L-amino drogenase of bacillus cereus (accession numbergió741938); acid or an L-amino acid converted into a D-amino acid. the L-phenylalaninedehydrogenase of rhodococcus (acces Thus, starting with a racemate, an enantiomerically pure 60 sion number gió25925); the L-lysine dehydrogenase of compound can be produced.
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