[Conformation characteristics of gamma-glutamyl-containing peptides].
Conformational analysis, by the method of atom-atomic potentials, has been carried out for five tripeptides containing gamma-glutamyl bonds and having general formula Glu(gamma)-X-Gly. The spatial structures have been determined and the changes arising on varying the second residue have been analyzed. A comparison of possible conformations and biological activity in respect to a number of enzymes allows to conceive what structural features of these compounds are important for the substrate specificity of the enzymes. In particular, the active site topography has been surmised for glutathione synthetase (EC 6.3.2.3) and gamma-glutamyltranspeptidase (EC 2.3.2.2). The glutathione thiol group has been found to be exposed in all possible conformations that explains its accessibility for various reagents.
D001665:Binding Sites; D004151:Dipeptides; D005978:Glutathione / Q000378:metabolism*; D005981:Glutathione Synthase; D009842:Oligopeptides; D011487:Protein Conformation; D013237:Stereoisomerism; D013379:Substrate Specificity; D005723:gamma-Glutamyltransferase
D004151:Dipeptides; D009842:Oligopeptides; D005723:gamma-Glutamyltransferase; D005981:Glutathione Synthase; D005978:Glutathione; C017341:gamma-glutamylcysteine
Konformatsionnye osobennosti gamma-glutamilsoderzhashchikh peptidov.