Aspartate 458 of human glutathione synthetase is important for cooperativity and active site structure

Biochemical and Biophysical Research Communications

Volumn 411, Issue 3, 2011, Pages 536-542

  Brown, Teresa R ^a   Drummond, Michael L ^b   Barelier, Sarah ^a,b   Crutchfield, Amanda S ^a   Dinescu, Adriana ^a   Slavens, Kerri D ^a   Cundari, Thomas R ^b   Anderson, Mary E ^a  

^a TEXAS WOMAN'S UNIVERSITY   (United States)

^b UNIVERSITY OF NORTH TEXAS   (United States)

Author keywords

Glutathione; Glutathione synthetase; Negative cooperativity

Indexed keywords

2 AMINOBUTYRIC ACID; ASPARTIC ACID; GAMMA GLUTAMYL ALPHA AMINOBUTYRATE; GAMMA GLUTAMYL HYDROLASE; GLUTATHIONE; GLUTATHIONE SYNTHASE; UNCLASSIFIED DRUG;

ALLOSTERISM; ARTICLE; CATALYSIS; CIRCULAR DICHROISM; CONTROLLED STUDY; DIFFERENTIAL SCANNING CALORIMETRY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SUBSTRATE; HYDROGEN BOND; HYDROPHOBICITY; MICHAELIS CONSTANT; MUTATIONAL ANALYSIS; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; WILD TYPE;

ALLOSTERIC REGULATION; AMINO ACID SEQUENCE; ASPARTIC ACID; CATALYSIS; CATALYTIC DOMAIN; GLUTATHIONE SYNTHASE; HUMANS; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY;

EID: 79961125960     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.06.166     Document Type: Article

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