X‐ray crystal structures of cytosolic glutathione S‐transferases
Open Access
- 3 March 1994
- journal article
- review article
- Published by Wiley in European Journal of Biochemistry
- Vol. 220 (3) , 645-661
- https://doi.org/10.1111/j.1432-1033.1994.tb18666.x
Abstract
Crystal structures of cytosolic glutathione S‐transferases (EC 2.5.1.18), complexed with glutathione or its analogues, are reviewed. The atomic models define protein architectural relationships between the different gene classes in the superfamily, and reveal the molecular basis for substrate binding at the two adjacent subsites of the active site. Considerable progress has been made in understanding the mechanism whereby the thiol group of glutathione is destabilized (lowering its pKa) at the active site, a rate‐enhancement strategy shared by the soluble glutathione S‐transferases.Keywords
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