Arg304 of human DNA primase is a key contributor to catalysis and NTP binding: Primase and the family X polymerases share significant sequence homology

Biochemistry

Volumn 38, Issue 24, 1999, Pages 7727-7736

  Kirk, Brian W ^a   Kuchta, Robert D ^a  

^a UNIVERSITY OF COLORADO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; DNA DIRECTED DNA POLYMERASE BETA; DNA PRIMASE; MUTANT PROTEIN; NUCLEOSIDE TRIPHOSPHATE;

AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ANALYSIS; ENZYME SUBUNIT; HUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; ARGININE; BASE SEQUENCE; BINDING SITES; DNA POLYMERASE BETA; DNA PRIMASE; DNA-DIRECTED DNA POLYMERASE; ENZYME ACTIVATION; GENE EXPRESSION; HUMANS; MOLECULAR SEQUENCE DATA; MULTIGENE FAMILY; MUTAGENESIS, SITE-DIRECTED; NUCLEOTIDES; PHOSPHATES; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; TEMPLATES, GENETIC;

EUKARYOTA;

EID: 0033564245     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi990247c     Document Type: Article

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