Pre-Steady-State Kinetics of RB69 DNA Polymerase and Its Exo Domain Mutants: Effect of pH and Thiophosphoryl Linkages on 3′-5′ Exonuclease Activity

Biochemistry

Volumn 43, Issue 13, 2004, Pages 3853-3861

  Wang, C X ^a   Zakharova, E ^a   Li, J ^a   Joyce, C M ^a   Wang, J ^a   Konigsberg, W ^a  

^a YALE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; ENZYME KINETICS; MUTAGENESIS; PH EFFECTS; REACTION KINETICS;

DNA POLYMERASE; KLENOW FRAGMENT (KF); PRE-STEADY-STATE KINETICS;

DNA;

DNA POLYMERASE; DOUBLE STRANDED DNA; EXONUCLEASE; METAL ION; MUTANT PROTEIN; PHOSPHORUS DERIVATIVE; THIOL DERIVATIVE;

ARTICLE; DNA REPAIR; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE; PH; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; STEADY STATE; WILD TYPE;

ALANINE; AMINO ACID SUBSTITUTION; BACTERIOPHAGE T4; BASE PAIR MISMATCH; DNA POLYMERASE I; DNA-DIRECTED DNA POLYMERASE; ENZYME ACTIVATION; EXODEOXYRIBONUCLEASES; GLUTAMINE; HYDROGEN-ION CONCENTRATION; KINETICS; MUTAGENESIS, SITE-DIRECTED; PHOSPHATES; PHOSPHORYLATION; PROTEIN STRUCTURE, TERTIARY; RNA EDITING; SUBSTRATE SPECIFICITY; T-PHAGES; THIONUCLEOTIDES; VIRAL PROTEINS;

EID: 1842539357     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0302292     Document Type: Article

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