Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Oxidoreductase
Reexamination Certificate
2006-05-23
2008-11-18
Prouty, Rebecca E. (Department: 1652)
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Oxidoreductase
C435S106000, C435S232000, C435S252330, C435S488000, C435S252300, C435S108000
Reexamination Certificate
active
07452704
ABSTRACT:
The object of the present invention is to provide a novel dehydrogenase having a property which is different from that of known dehydrogenases. The present invention provides a dehydrogenase having the following physicochemical properties:(1) effect: to produce N-alkyl-L-alanine from pyruvic acid and alkylamine or dialkylamine using NADPH and/or NADH as coenzyme;(2) substrate specificity: to show activity to alkylamine or dialkylamine but not to ammonium;(3) optimal pH when using phenylpyruvic acid and methylamine as substrates is around 10; and(4) when treated at 30° C. for 30 minutes, the enzyme is stable at around pH 5 to 10.5.
REFERENCES:
patent: 5942630 (1999-08-01), Barth et al.
patent: 254354 (1988-01-01), None
patent: 57-183799 (1982-11-01), None
patent: 60-218400 (1985-11-01), None
patent: 2001-190298 (2001-07-01), None
patent: 02/077183 (2002-10-01), None
patent: WO 02/101003 (2002-12-01), None
Hester et al., “Purification ofPseudomonas putidabranched-chain keto acid dehydrogenase E1 component”, Methods Enzymology, vol. 324, pp. 129-138 (2000).
Hester et al., “Purification of active E1 a2β2 ofPseudomonas putidabranched-chain-oxoacid dehydrogenase”, Eur. J. Biochem., vol. 233, pp. 828-836 (1995).
Rae et al., “Sequences and expression of pyruvate dehydrogenase fromPseudomonas aeruginosa”, J. Bacteriology, vol. 179, pp. 3561-3571 (1997).
Inoue et al., “Molecular characterization of trhe mde operon involved in L-methionine catabolism ofPseudomonas pulida”, J. Bacteriology, vol. 179, pp. 3956-3962 (1997).
Rinehart et al., “Structures of the Didemnins, Antiviral and Cytotoxic Depsipeptides from a Caribbean Tunicate”, Journal of American Chemical Society, vol. 103, pp. 1857-1859 (1981).
Pettit et al., “Isolation of dolastatins 10-15 from the marine molluscPolabella auricularia”, Tetrahedron, Vo. 49, No. 41, pp. 9151-9170 (1993).
Dorow et al., “A Novel Preparation of Scalemic N-Methyl-α-amino Acids”, Journal of Organic Chemistry, vol. 60, pp. 4986-4987 (1995).
Reddy et al., “A Practical Approach for the Optically PureN-Methyl-α-amino Acids”, Tetrahedron Letters,. vol. 39, pp. 1985-1986 (1998).
Lin et al., “Purification and Characterization ofN-Methylalanine Dehydrogenase”, The Journal of Biological Chemistry, vol. 250, No. 10, pp. 3746-3751 (1975).
Hanessian et al., “Asymmetric Synthesis of L-Azetidine -2-Carboxylic acid and 3-substituted congeners—Conformationally constrained analogs of Phenylalanine, Naphthylalanine, and Leucine”, Bioorganic & Medicinal Chemistry Letters, vol. 9, pp. 1437-1442 (1999).
Fernandez-Garcia et al., “A Short Enantioselective Synthesis of Pipecolic Acid”, Tetrahedron: Asymmetry, vol. 6, No. 12, pp. 2905-2906 (1995).
Callens et al., “Preparation of Trans-5-Hydroxy-L-Pipecolic acid and Cis-4-Hydroxy-L-Pipecolic acid from L-Baikiain (1,2,5,6-L-Tetrahydropyridine-2-carboxylic acid”, Bulletin Society Chim. Belg. Vo. 91, No. 8 (1982).
Shiraiwa et al., “Synthesis of Optically Active 1,4-Thiazane-3-carboxylic AcidviaOptical Resolution by preferential Crystallization of (RS)-2-Amino-3[(2-chloroethyl)sulfanyl]propanoic acid Hydrochloride”, Bioscience Biotechnology, Biochemistry, vol. 62, No. 12, pp. 2382-2387 (1998).
Larsson et al., “Synthesis of Amino Acids with Modified Principal Properties 3: Sulfur-containing Amino Acids”, Acta Chemica Scandinavica, vol. 48, pp. 517-525 (1994).
Kogami et al., “Synthesis of Optically Active 3-Morpholinecaboxylic Acid and Tetrahydro-2H-1,4-thiazine-3-carboxylic Acid”, Bulletin of Chemical Society of Japan, vol. 60, pp. 2963-2965 (1987).
Seebach et al., “Synthesis of Nonproteinogenic (R)- or (S)-Amino acids Analogues of Phenylalanine, Isotopically Labeled and Cyclic Amino Acids fromtert-Butyl 2-(tert-Butyl)-3-methyl-4-oxo-I-imidazolidinecarboxylate (Boc-BMI)”, Liebigs Ann. Chemistry, pp. 1215-1232 (1989).
Fujii et al., “Increase in the Rate of L-Pipecolic Acid Production Usinglat-ExpressingEscherichia colibylysPandyeiEAmplification”, Bioscience Biotechnology Biochemistry, vol. 66, No. 9, pp. 1981-1984 (2002).
Kenklies et al., “Proline biosynthesis from L-ornithine inClostridium sticklandii: purification of Δ1-pyrroline-5-carboxylate reductase, and sequence and expression of the encoding gene,proC”, Microbiology, vol. 145. pp. 819-826 (1999).
Costilow et al., “Reactions Involved in the Conversion of Ornithine to Proline in Clostridia”, Journal of Bacteriology, pp. 662-667 (1969).
Costilow et al., “Ornithine Cyclase (Deaminating)”, The Journal of Biological Chemistry, vol. 246, No. 21, pp. 6655-6660 (1971).
Meister et al., “Enzymatic Synthesis of L-Pipecolic acid and L-Proline”, Journal of Biological Chemistry, vol. 229, pp. 789-800 (1957).
Payton et al., “Δ1-Piperideine-2-Carboxylate Reductase ofPseudomonas putida” Journal of Bacteriology, vol. 149, No. 3, pp. 864-871 (1982).
Nardini et al., “Purification and characterization of ketimine-reducing enzyme”, European Journal of Biochemistry, vol. 173, pp. 689-694 (1988).
Zoller et al., “Oligonucleotide-directed mutagenesis using M13-derived vectors: an efficient and general procedure for the production of point mutations in any fragment of DNA”, Nucleic Acids Research, vol. 10, No. 20, pp. 6487-6500 (1982).
Shortle et al., “Directed Mutagenesis with Sodium Bisulfite”, Methods Enzymology, vol. 100, pp. 457-468 (1983).
Reiser et al., “Transfer and Expression of Heterologous Genes in Yeasts Other ThanSaccharomyces cerevisiae”, Advances in Biochemical Engineering, vol. 43, pp. 75-102 (1990).
Miwa et al., “Construction of novel shuttle vectors and a cosmid vector for the glutamic acid-producing bacteriaBrevibacterium lactofermentumandCorynebacterium glutamicum”, Gene, vol. 39, pp. 281-286 (1985).
Ozaki et al., “Fuctional expression of the genes ofEscherichia coliin gram-positiveCorynebacterium glutamicum”, Moleculat & General Genetics, vol. 196, pp. 175-178 (1984).
Heyer et al., “Replicating Plasmids inSchizosaccharomyces pombe: Improvement of Symmetric Segregartion by a New Genetic Element”, Molecular and Cellular Biology, vol. 6, No. 1, pp. 80-89 (1986).
Saunders et al., “Heterologous gene expression in filamentous fungi”, Trends in Biotechnology, vol. 7, pp. 283-287 (1989).
Maeda et al., “Production of human α-interferon in silkworm using a baculovirus vector”, Nature, vol. 315, pp. 592-597 (1985).
Moore et al., “Culture of Normal Human Leukocytes”, The Journal of the American Medical Association, vol. 199, No. 8, pp. 519-524 (1967).
Eagle, “Nutrition Needs of Mammalian Cells in Tissue Culture”, Science vol. 122, No. 3168, pp. 501-504 (1955).
Lundholm et al., “Plaque Production by the Polyoma Virus”, Virology, vol. 8, p. 396-397 (1959).
Morgan et al., “Nutrition of Animal Cells in Tissue Culture. I. Initial Studies on a Synthetic Medium”, Proceeding of the Society for Experimental Biology and Medicine, vol. 73, No. 1, pp. 1-8 (1950).
Geuke et al., “A new bacterial L-Amino acid oxidase with a broad substrate specificity: purification and characterization”, Enzyme and Microbial Technology, vol. 31, pp. 77-87 (2002).
Lampel et al., “Characterization of the Developmentally RegulatedBacillus subtilisGlucose Dehydrogenase Gene”, Journal of Bacteriology, vol. 166, No. 1, pp. 238-243 (1986).
Keenan et al., “Synthesis of chiral nonracemic 4-trans-substituted pipecolic acid derivatives”, Tetrahedron: Asymmetry, vol. 10, pp. 4331-4341 (1999).
Letavic et al., “Synthesis and Biological Activity of Selective Pipecolic Acid-Based TNF-α Converting Enzyme (TACE) Inhibitors”, Bioorganic & Med
Esaki Nobuyoshi
Hara Mari
Mihara Hisaaki
Ueda Makoto
Greenblum & Bernstein P.L.C.
Meah Younus
Mitsubishi Chemical Corporation
Prouty Rebecca E.
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