The enhanced affinity for thiolate anion and activation of enzyme-bound glutathione is governed by an arginine residue of human Mu class glutathione S-transferases

Journal of Biological Chemistry

Volumn 275, Issue 5, 2000, Pages 3296-3304

  Patskovsky, Yury V ^a   Patskovska, Larysa N ^a   Listowsky, Irving ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; GLUTATHIONE PEROXIDASE; GLUTATHIONE TRANSFERASE;

ARTICLE; BINDING AFFINITY; CATALYSIS; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME REGULATION; ENZYME STRUCTURE; PRIORITY JOURNAL; STEADY STATE;

ARGININE; BINDING SITES; CATALYSIS; CLONING, MOLECULAR; ENZYME ACTIVATION; GLUTATHIONE; GLUTATHIONE TRANSFERASE; HUMANS; MOLECULAR SEQUENCE DATA; MUTATION; RECOMBINANT PROTEINS;

FELIS CATUS;

EID: 0034603086     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.275.5.3296     Document Type: Article

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