Identification and clarification of the role of key active site residues in bacterial glutathione S-transferase zeta/maleylpyruvate isomerase

Biochemical and Biophysical Research Communications

Volumn 410, Issue 3, 2011, Pages 452-456

  Fang, Ti ^a   Li, De Feng ^b   Zhou, Ning Yi ^a  

^a WUHAN INSTITUTE OF VIROLOGY   (China)

^b INSTITUTE OF BIOPHYSICS   (China)

Author keywords

Active site mapping; Enzyme kinetics; Glutathione S transferase; Maleylpyruvate isomerase; Site directed mutagenesis

Indexed keywords

ASPARTIC ACID; BACTERIAL ENZYME; CARBOXYL GROUP; GLUTATHIONE; GLUTATHIONE TRANSFERASE; GLUTATHIONE TRANSFERASE ZETA; GLYCINE; ISOMERASE; MALEYLPYRUVATE ISOMERASE; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CATALYSIS; ELECTRON; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME KINETICS; ENZYME SUBSTRATE COMPLEX; IONIZATION; ISOMERIZATION; MOLECULAR EVOLUTION; PHYLOGENY; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; SITE DIRECTED MUTAGENESIS; STEADY STATE;

ARGININE; BACTERIAL PROTEINS; CATALYTIC DOMAIN; CIS-TRANS-ISOMERASES; GLUTATHIONE TRANSFERASE; GLYCINE; MUTATION; RALSTONIA;

BACTERIA (MICROORGANISMS); EUKARYOTA; PROKARYOTA; RALSTONIA SP.;

EID: 79960034249     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.05.155     Document Type: Article

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