Valine 44 and valine 45 of human glutathione synthetase are key for subunit stability and negative cooperativity

Biochemical and Biophysical Research Communications

Volumn 410, Issue 3, 2011, Pages 597-601

  Slavens, Kerri D ^a   Brown, Teresa R ^a   Barakat, Khaldoon A ^b   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

ALANINE; GLUTATHIONE SYNTHASE; TRYPTOPHAN; UNCLASSIFIED DRUG; VALINE; VALINE 44; VALINE 45;

ARTICLE; BINDING AFFINITY; BINDING SITE; CONTROLLED STUDY; DIFFERENTIAL SCANNING CALORIMETRY; DNA SEQUENCE; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME BINDING; ENZYME PURIFICATION; ENZYME STABILITY; GENE MUTATION; HUMAN; MUTATION; PRIORITY JOURNAL;

ALLOSTERIC REGULATION; CATALYTIC DOMAIN; ENZYME STABILITY; GLUTATHIONE SYNTHASE; HUMANS; ISOENZYMES; MUTATION; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; VALINE;

EID: 79960042725     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.06.034     Document Type: Article

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