The three-dimensional structure of Cys-47-modified mouse liver glutathione S-transferase P1-1: Carboxymethylation dramatically decreases the affinity for glutathione and is associated with a loss of electron density in the αB-310B region

Journal of Biological Chemistry

Volumn 273, Issue 5, 1998, Pages 2844-2850

  Vega, M Cristina ^a   Walsh, Sinead B ^b   Mantle, Timothy J ^b   Coll, Miquel ^a  

^a Ctr d'Investigacio i D   (Spain)

^b TRINITY COLLEGE DUBLIN   (Ireland)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; GLUTATHIONE TRANSFERASE; LIVER ENZYME; SULFUR; TYROSINE;

ARTICLE; CARBOXYLATION; ENZYME ACTIVE SITE; ENZYME KINETICS; ENZYME MODIFICATION; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; METHYLATION; MICHAELIS CONSTANT; MOUSE; NONHUMAN; PRIORITY JOURNAL; STEREOCHEMISTRY; X RAY DIFFRACTION;

ANIMALS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; CYSTEINE; GLUTATHIONE; GLUTATHIONE S-TRANSFERASE PI; GLUTATHIONE TRANSFERASE; IODOACETATES; IODOACETIC ACID; ISOENZYMES; LIVER; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION;

EID: 0032579563     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.273.5.2844     Document Type: Article

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