Use of sequence microdivergence in mycobacterial ortholog to analyze contributions of the water-activating loop histidine of Escherichia coli uracil-DNA glycosylase in reactant binding and catalysis

Biochemical and Biophysical Research Communications

Volumn 320, Issue 3, 2004, Pages 893-899

  Acharya, Narottam ^a   Talawar, Ramappa K ^a   Purnapatre, Kedar ^a,b   Varshney, Umesh ^a  

^a INDIAN INSTITUTE OF SCIENCE   (India)

^b RANBAXY RESEARCH LABORATORIES   (India)

Author keywords

[No Author keywords available]

Indexed keywords

HISTIDINE; URACIL; URACIL DNA GLYCOSYLTRANSFERASE; WATER;

ARTICLE; ASSAY; BINDING AFFINITY; CATALYSIS; ENZYME ACTIVE SITE; ENZYME SUBSTRATE; ESCHERICHIA COLI; INHIBITION KINETICS; MUTANT; MUTATION; MYCOBACTERIUM; ORTHOLOGY; PRIORITY JOURNAL; PROTEIN BINDING; SEQUENCE ANALYSIS; WILD TYPE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BINDING SITES; CATALYSIS; DNA GLYCOSYLASES; ENZYME ACTIVATION; ENZYME STABILITY; ESCHERICHIA COLI; HISTIDINE; KINETICS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURE-ACTIVITY RELATIONSHIP; URACIL-DNA GLYCOSIDASE; WATER;

ESCHERICHIA COLI;

EID: 3042801437     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.06.032     Document Type: Article

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