A carboxylate triad is essential for the polymerase activity of Escherichia coli DNA polymerase I (Klenow Fragment). Presence of two functional triads at the catalytic center

Journal of Biological Chemistry

Volumn 275, Issue 26, 2000, Pages 19685-19692

  Gangurde, Rajiv ^a   Kaushik, Neerja ^a   Singh, Kamalendra ^a   Modak, Mukund J ^a  

^a RUTGERS NEW JERSEY MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DNA DIRECTED DNA POLYMERASE BETA; DNA POLYMERASE;

AMINO ACID SUBSTITUTION; ARTICLE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; ESCHERICHIA COLI; NONHUMAN; PHOSPHORYLATION; PRIORITY JOURNAL;

ALANINE; ASPARTIC ACID; BINDING SITES; CATALYSIS; DNA; DNA POLYMERASE I; DOSE-RESPONSE RELATIONSHIP, DRUG; ESCHERICHIA COLI; GLUTAMIC ACID; KINETICS; MAGNESIUM; MUTAGENESIS, SITE-DIRECTED; PHOSPHORIC ACIDS; PLASMIDS; SODIUM CHLORIDE; TRANSFECTION; TRICHLOROACETIC ACID;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0034733652     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M002307200     Document Type: Article

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