Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Oxidoreductase
Patent
1994-05-24
1996-12-10
Low, Christopher S. F.
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Oxidoreductase
435189, 435 691, 4351723, 4353201, 4352523, 43525233, 536 232, 930240, 935 10, 935 14, C12N 904
Patent
active
055830250
ABSTRACT:
Mutants of 2,5-diketo-D-gluconic acid reductase A, an enzyme used to produce 2-keto-L-gulonic acid, a precursor of ascorbic acid (vitamin C) are prepared by site-directed mutagenesis. These mutants have increased catalytic activity, increased expression levels, and/or enhanced temperature stability.
REFERENCES:
patent: Re30872 (1982-02-01), Sonoyamas et al.
patent: 3959076 (1976-05-01), Sonoyama et al.
patent: 3998697 (1976-12-01), Sonoyama et al.
patent: 4543331 (1985-09-01), Sonoyama et al.
patent: 4757012 (1988-07-01), Estell et al.
patent: 4758514 (1988-07-01), Light et al.
patent: 4945052 (1990-07-01), Hardy et al.
patent: 5004690 (1991-04-01), Light et al.
patent: 5008193 (1991-04-01), Anderson et al.
patent: 5017691 (1991-05-01), Lee et al.
patent: 5032514 (1991-07-01), Anderson et al.
patent: 5376544 (1994-12-01), Lazarus et al.
Miller, J. V. et al., "Purification and Characterization of 2,5-Diketo-D-Gulonate Reductase from Corynebacterium Sp.," J. Biol. Chem. 262:9016-9020 (1987).
Nicholson, H. et al., "Enhanced Protein Thermostability from Designed Mutations that Interact with .alpha.-Helix Dipoles," Nature 336:651-656 (1988).
Rastetter, W. H., "Enzyme Egineering: Applications and Promise," Trends Biotechnol. 1:80-84 (1983).
Richardson, J. S. et al., "Amino Acid Preferences for Specific Locations at the Ends of .alpha.-Helices," Science 240:1648-1652 (1988).
Sonoyama, T. et al., "Purification and Properties of Two 2,5 Diketo-D-Gluconate Reductases from a Mutant Strain Derived from Corynebacterium sp.," J. Ferment. Technol. 65:311-317 (1987).
Sonoyama, T. et al., "Distribution of Microorganisms Capable of Reducing 2,5 Diketo-D-Gluconate to 2-Keto-L-Gulonate," Agric. Biol. Chem. 51:2003-2004 (1987).
Sonoyama, T. et al., "Production of 2-Keto-L-Gulonic Acid from D-Glucose by Two Stage Fermentation," Appl. Environ. Microbiol. 43:1064-1069 (1982).
Wells, J. A. et al., "Recruitment of Substrate-Specificity Properties from One Enzyme into a Related One by Protein Engineering," Proc. Natl. Acad. Sci. (U.S.A.) 84:5167-5171 (1987).
Wilkinson, A. J. et al., "A Large Increase in Enzyme-Substrate Affinity by Protein Engineering," Nature 307:187-188 (1984).
Anderson, S. et al., "Production of 2-Keto-L-Gulonate, and Intermediate in L-Ascorbate Synthesis, by a Genetically Modified Erwinia herbicola," Science 230:144-149 (1985).
Grindley, J. F. et al., "Conversion of Glucose to 2-Keto-L-Gulonate, and Intermediate in L-Ascorbate Synthesis by a Recombinant Strain of Erwinia citreus," Appl. Environ. Microbiol. 54:1770-1775 (1988).
Kellis, J. T. et al., "Contribution of Hydrophobic Interactions to Protein Stability," Nature 333:784-786 (1988).
Imanaka, T. et al., "A New Way of Enhancing the Thermostability of Proteases," Nature 324:695-697 (1986).
Matthews, B. W. et al., "Enhanced Protein Thermostability from Site-Directed Mutations that Decreases the Entropy of Unfolding," Proc. Natl. Acad. Sci. (U.S.A.) 84:6663-6667 (1987).
Matsumura, M. et al., "Substantial Increase of Protein Stability by Multiple Disulphide Bonds," Nature 342:291-293 (1989).
Schulz et al. 1979 (9th Printing) in Principles of Protein Structures Springer Verlag, New York, pp. 171-175.
Anderson Stephen
Hurle Mark
Lazarus Robert A.
Powers David B.
Auerbach Jeffrey I.
Low Christopher S. F.
Rutgers The State University of New Jersey
LandOfFree
Enzymes for the production of 2-keto-L-gulonic acid does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Enzymes for the production of 2-keto-L-gulonic acid, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Enzymes for the production of 2-keto-L-gulonic acid will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-423551