Escherichia coli DNA polymerase I (Klenow fragment) uses a hydrogen-bonding fork from Arg668 to the primer terminus and incoming deoxynucleotide triphosphate to catalyze DNA replication

Journal of Biological Chemistry

Volumn 279, Issue 32, 2004, Pages 33043-33046

  Meyer, Aviva S ^a   Blandino, Maureen ^a   Spratt, Thomas E ^a  

^a AMERICAN HEALTH FOUNDATION   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; HYDROGEN BONDS; MUTAGENESIS; PARAMETER ESTIMATION; PROTEINS;

METHYLENE GROUP; MOIETY;

DNA;

ADENOSINE TRIPHOSPHATE; ALANINE; AMINO ACID; ARGININE; BACTERIAL ENZYME; DNA; DNA DIRECTED DNA POLYMERASE BETA; DNA POLYMERASE; OLIGODEOXYNUCLEOTIDE; PHOSPHORUS 32; URIDINE TRIPHOSPHATE;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; DNA REPLICATION; ENZYME KINETICS; ESCHERICHIA COLI; HYDROGEN BOND; ISOTOPE LABELING; MOLECULAR INTERACTION; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DNA INTERACTION; SITE DIRECTED MUTAGENESIS;

ARGININE; BINDING SITES; CATALYSIS; DNA POLYMERASE I; DNA REPLICATION; ESCHERICHIA COLI; GUANINE; HYDROGEN BONDING; MUTAGENESIS, SITE-DIRECTED; OLIGODEOXYRIBONUCLEOTIDES; URIDINE TRIPHOSPHATE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 4043150758     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.C400232200     Document Type: Article

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