Biochemical analysis of point mutations in the 5′-3′ exonuclease of DNA polymerase I of Streptococcus pneumoniae: Functional and structural implications

Journal of Biological Chemistry

Volumn 276, Issue 22, 2001, Pages 19172-19181

  Amblar, Mónica ^a   García De Lacoba, Mario ^b   Corrales, Maria A ^b   López, Paloma ^b  

^a UNIVERSIDADE NOVA DE LISBOA   (Portugal)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

DNA; ENZYMES; MUTAGENESIS; REACTION KINETICS;

METAL BINDING;

BIOCHEMISTRY;

DNA; DNA DIRECTED DNA POLYMERASE BETA; EXONUCLEASE; HYBRID PROTEIN; PHOSPHODIESTERASE I; SPLEEN EXONUCLEASE; UNCLASSIFIED DRUG; ASPARTIC ACID; EXODEOXYRIBONUCLEASE; EXODEOXYRIBONUCLEASE V; GLUTAMIC ACID; HISTIDINE; LIGAND; MAGNESIUM CHLORIDE; SINGLE STRANDED DNA;

AMINO ACID SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; DISSOCIATION CONSTANT; DNA BINDING; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME MECHANISM; ENZYME STRUCTURE; MUTATIONAL ANALYSIS; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN DOMAIN; STREPTOCOCCUS PNEUMONIAE; WILD TYPE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; DOSE RESPONSE; ENZYMOLOGY; GENETICS; KINETICS; METABOLISM; MOLECULAR GENETICS; MUTAGENESIS; MUTATION; NUCLEOTIDE SEQUENCE; PLASMID; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY;

BACTERIA (MICROORGANISMS); EUKARYOTA; PROKARYOTA; STREPTOCOCCUS; STREPTOCOCCUS PNEUMONIAE;

AMINO ACID SEQUENCE; ASPARTIC ACID; BINDING SITES; CATALYSIS; CATALYTIC DOMAIN; CONSERVED SEQUENCE; DNA; DNA POLYMERASE I; DNA, SINGLE-STRANDED; DOSE-RESPONSE RELATIONSHIP, DRUG; EXODEOXYRIBONUCLEASE V; EXODEOXYRIBONUCLEASES; GLUTAMIC ACID; HISTIDINE; KINETICS; LIGANDS; MAGNESIUM CHLORIDE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS; MUTATION; PLASMIDS; POINT MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; STREPTOCOCCUS PNEUMONIAE;

EID: 0035376980     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M008678200     Document Type: Article

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