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Function of Conserved Residues of Human Glutathione Synthetase: Implications for the ATP-Grasp Enzymes
Article examining the mechanism of Glutathione synthetase, an enzyme that belongs to the glutathione synthetase ATP-binding domain-like superfamily. A variety of structural alignment methods were applied and four highly conserved residues of human glutathione synthetase (Glu-144, Asn-146, Lys-305, and Lys-364) were identified in the binding site. The function of these was studied by experimental and computational site-directed mutagenesis.
Date:
May 21, 2004
Creator:
Dinescu, Adriana; Cundari, Thomas R., 1964-; Bhansali, Vikas S.; Luo, Jia-Li & Anderson, Mary E.
System:
The UNT Digital Library