Cobalt activation of Escherichia coli 5′-nucleotidase is due to zinc ion displacement at only one of two metal-ion-binding sites

Biochemical Journal

Volumn 372, Issue 2, 2003, Pages 625-630

  McMillen, Lyle ^a   Beacham, Ifor R ^a   Burns, Dennis M ^a  

^a GRIFFITH UNIVERSITY   (Australia)

Author keywords

Co2+ activation; Consensus sequence; Phosphoesterase; Sequence motif; Zinc metalloenzyme

Indexed keywords

CATALYSIS; CHEMICAL ACTIVATION; CLONING; COBALT; ENZYMES; GENES; MUTAGENESIS; ZINC;

METAL-ION-BINDING SITES;

ESCHERICHIA COLI;

5' NUCLEOTIDASE; ASPARTIC ACID; BACTERIAL ENZYME; BACTERIAL PROTEIN; COBALT; GLUTAMIC ACID; HISTIDINE; MUTANT PROTEIN; PROTEIN USHA; UNCLASSIFIED DRUG; ZINC ION;

ARTICLE; BINDING SITE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; ESCHERICHIA COLI; IN VITRO STUDY; METAL BINDING; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN MOTIF; SITE DIRECTED MUTAGENESIS; WILD TYPE;

5'-NUCLEOTIDASE; AMINO ACID SUBSTITUTION; BINDING SITES; CATALYSIS; COBALT; DNA PRIMERS; ENZYME ACTIVATION; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; KINETICS; METALS; MODELS, BIOLOGICAL; MUTAGENESIS, SITE-DIRECTED; PHOSPHORIC DIESTER HYDROLASES; POLYMERASE CHAIN REACTION; STRUCTURE-ACTIVITY RELATIONSHIP; ZINC;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0037662630     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021800     Document Type: Article

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