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Function of Conserved Residues of Human Glutathione Synthetase: Implications for the ATP-Grasp Enzymes

Description: 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.
Item Type: Refine your search to only Article
Partner: UNT College of Science
open access

Formal oxo- and aza-[3 + 2] reactions of α-enaminones and quinones: a double divergent process and the roles of chiral phosphoric acid and molecular sieves

Description: Article develops a double divergent process for the reaction of α-enaminones with quinones through facile manipulation of catalyst and additive, leading to structurally completely different products.
Date: September 21, 2020
Creator: Luo, Weiwei; Sun, Zhicheng; Fernando, E. H. Nisala; Nesterov, Vladimir N.; Cundari, Thomas R., 1964- & Wang, Hong
Item Type: Refine your search to only Article
Partner: UNT College of Science
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