Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase
Patent
1992-01-27
1994-05-03
Wax, Robert A.
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Hydrolase
4351723, 935 10, 935 14, C12N 922
Patent
active
053087623
ABSTRACT:
A T4 endonuclease V DNA repair enzyme contains an amino acid sequence within its carboxyl terminal region which is involved in dimer specific binding. The region includes polar nonaromatic basic amino acids and aromatic amino acids between amino acid 128 to 137 positions. The specific activity of the enzyme is greatly increased at low salt concentrations when substitutions are made in aromatic amino acids in the carboxy terminal region.
REFERENCES:
Recinos et al. (1986) J. Bacteriol. 168:1014-1018.
Recinos et al (1988) Biochem. 27:1832-1838.
Lloyd et al (1989) Proteins Struc. Funct. Genet. 6:128-138.
Recinos, A., et al. "Expression of the bacteriophage T4 denV structural gene in Escherichia coli" 1986. J. Bacteriol. 168:1014-1018.
Recinos, A. & Lloyd, R. S. "Site directed mutagenesis of the T4 Endonuclease V Gene: Role of Lysine-130" 1988 Biochemistry 27:1832-1838.
Lloyd, R. S. & Augustine, M. L. "Site directed mutagenesis of the T4 Endonuclease V Gene: Mutations which Enhance Enzyme Specific Activity at Low Salt Concentrations" 1989 Proteins Struct. Funct. Genet. 6:128-138.
Bugalsky Gabriele E.
Vanderbilt University
Wax Robert A.
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