Effect of configuration of the inhibitors on the mode of binding to the enzyme, thermolysin.
Preferred conformations of the competitive inhibitors glycyl-L-phenylalanine and glycyl-D-phenylalanine and their mode of binding to thermolysin have been studied. The difference in configuration is shown to affect significantly the mode of binding to thermolysin. Gly-D-Phe prefers to enter the active site in the global minimum conformation whereas Gly-L-Phe may enter in a higher energy conformation. Moreover, D-enantiomer is shown to have a better fit than the L-counterpart in the active site.
D001665:Binding Sites; D004151:Dipeptides / Q000494:pharmacology; D066298:In Vitro Techniques; D008968:Molecular Conformation; D015394:Molecular Structure; D013237:Stereoisomerism; D013816:Thermodynamics; D013820:Thermolysin / Q000037:antagonists & inhibitors*
D004151:Dipeptides; C029660:glycylphenylalanine; D013820:Thermolysin