Method for producing purine nucleoside by fermentation

Details Method for producing purine nucleoside by fermentation Method for producing purine nucleoside by fermentation

1998-07-17

2008-10-14

Saidha, Tekchand (Department: 1652)

Chemistry: molecular biology and microbiology

Micro-organism, tissue cell culture or enzyme using process...

Preparing compound containing saccharide radical

C435S088000, C435S183000, C435S193000, C435S194000, C435S243000, C435S252800

Reexamination Certificate

active

07435560

ABSTRACT:
A microorganism which has a gene encoding an enzyme in which feedback inhibition is desensitized by substitution of one or two amino acids in PRPP amidotransferase encoded by purF ofEscherichia coli, a gene encoding a protein which is an inactivated repressor of purine nucleotide biosynthesis encoded by purR, a gene encoding an enzyme which is inactivated purine nucleoside phosphorylase encoded by deoD, a gene encoding an enzyme which is inactivated succinyl-AMP synthase encoded by purA, a gene encoding an enzyme which is inactivated 6-phosphogluconate dehydrase encoded by edd, a gene encoding an enzyme which is inactivated phosphoglucose isomerase encoded by pgi and like is bred and a purine nucleoside is produced by culturing the microorganism.

REFERENCES:
patent: 3152966 (1964-10-01), Kinoshita et al.
patent: 3258408 (1966-06-01), Okumura et al.
patent: 3298923 (1967-01-01), Banno et al.
patent: 5766925 (1998-06-01), Sugimoto et al.
patent: 5804414 (1998-09-01), Moriya et al.
patent: 5876983 (1999-03-01), Sugimoto et al.
patent: 5919694 (1999-07-01), Sugimoto et al.
patent: 2004/0086985 (2004-05-01), Matsui et al.
patent: 0 282 989 (1988-09-01), None
patent: 0 406 436 (1991-01-01), None
patent: 1 004 663 (2000-05-01), None
patent: 1 217 076 (2002-06-01), None
patent: 63-230094 (1988-09-01), None
patent: 63-248394 (1988-10-01), None
patent: 90/05784 (1990-05-01), None
Neuhard et al. “Purines and Pyrimidines.” In:Escherichia coliandSalmonella typhimurium: Cellular and Molecular Biology. Edited by F. C. Neidhardt. Washington, D.C: American Society for Microgiology, 1987, vol. 1, pp. 445-473.
Mascarenhas et al. Appl Environ Microbiol. Oct. 1991;57(10):2995-9.
Gelpi. .J Chromatogr A. May 26, 1995;703(1-2):59-80.
Rolfes et al. J Biol Chem. Dec. 25, 1988;263(36):19653-61.
Accession P09452 Mar. 1, 1989.
Roy A. Levine, et al., Mol Gen Genet, vol. 181, pp. 313-318, “Selection for Purine Regulatory Mutants in anE. coliHypoxanthine Phosphoribosyl Transferase-Guanine Phosphoribosyl Transferase Double Mutant”, 1981.
Stanley G. Bower, et al., The Journal of Biological Chemistry, vol. 264, No. 17, pp. 10287-10291, “Characterization of theEscherichia coliPRS A1-Encoded Mutant Phosphoribosylpyrophosphate Synthetase Identifies a Divalent Cation-Nucleotide Binding Site”, Jun. 15, 1989.
Gaochao Zhou et al., The Journal of Biological Chemistry, vol. 269, No. 9, pp. 6784-6789, “Binding of Purine Nucleotides to Two Regulatory Sites Results in Synergistic Feedback Inhibition of Glutamine 5-Phosphoribosylpyrophosphate Amidotransferase”, Mar. 4, 1994.
F.R. Blattner, et al., “The Complete Genome Sequence ofEscherichia coliK-12”, Science, vol. 277, Sep. 5, 1997, pp. 1453-1462.
Seikagaku Jiten (Dictionary of Biochemistry) 2ndedition, Tokyo Kagaku Doujin (1990), pp. 1147-1151.
Japanese Patent Official Gazette No. 3117707 (Corresponds to JP 2-500062).
Wolfe, S. A., et al., “Nucleotide Sequence and Analysis of the purA Gene Encoding Adenylosuccinate Synthetase ofEscherichia coliK12,” Journal of Biological Chemistry, vol. 263, No. 35, Dec. 15, 1988, pp. 19147-19153.
Choi, K. Y., et al., “Mutagenesis of Amino Acid Residues Required for Binding of Corepressors to the Purine Repressor,” Journal of Biological Chemistry, vol. 269, No. 39, Sep. 30, 1994, pp. 24066-24072.
Mori, H., et al., “Cloning of a Guanosine-Inosine Kinase Gene ofEscherichia coliand Characterization of the Purified Gene Product,” Journal of Bacteriology, vol. 177, No. 17, Sep. 1995, pp. 4921-4926.
Andrews, S. C., et al., “Nucleotide Sequence of the Gene Encoding the GMP Reductase ofEscherichia coliK12,” Biochem. J., vol. 255, No. 1, Oct. 1, 1988, pp. 35-43.
Egan, S. E., et al., “Molecular Characterization of the Entner-Doudoroff Pathway inEscherichia coli: Sequence Analysis and Localization of Promoters for the edd-eda Operon,” Journal of Bacteriology, vol. 174, No. 14, Jul. 1992, pp. 4638-4646.
Seeger, C., et al., “Identification and Characterization of the Genes (xapA, xapB, and xapR) Involved in Xanthosine Catabolism inEscherichia coli,” Journal of Bacteriology, vol. 177, No. 19, Oct. 1995, pp. 5506-5516.
Mushegian, A. R., et al., “Unexpected sequence similarity between nucleosidases and phosphoribosyitransferases of different specificity,” Protein Science, 1994, 3:1081-1088.
Chang, Z., et al., “Deducted Amino Acid Sequence ofEscherichia coliAdenosine Deaminase Reveals Evolutionarily Conserved Amino Acid Residues: Implications for Catalytic Function,” Biochemistry, 30(8), 1991, pp. 2273-2280.
Raushel, F. M., et al., “The Amidotransferase Family of Enzymes: Molecular Machines for the Production and Delivery of Ammonia,” Biochemistry, vol. 38, No. 25, Jun. 22, 1999, pp. 7891-7899.
Anna Modrak-Wojcik, et al., “Molecular Architecture ofE. coliPurine Nucleoside Phosphorylase Studied by Analytical Ultracentrifugation and CD Spectroscopy”, Protein Science, vol. 15, 2006, pp. 1794-1800.
Westh Hansen, S. E., et al., “Studies on the Sequence and Structure of theEscherichia coliK-12 nupG Gene, Encoding a Nucleoside-transport System,” Eur. J. Biochem., 168, 1987, pp. 385-391.

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