title: Subsite mapping of enzymes. Double inhibition studies.
abstract: Our earlier subsite mapping studies led us to believe that ground state distortion occurred when a glucopyranoside ring filled the site which held the substrate monomer unit transferred to water during hydrolysis. We tested this hypothesis by performing double inhibitor studies on two amylases (EC 3.2.1.1) of bacterial origin. A general theory for multiple inhibition of this type is developed and applied to these two enzymes. Our data are consistent with the hypothesis that ground state strain occurs when substrates are bound to carbohydrates. An explanation is offered to account for the fact that monomers give strictly competitive inhibition patterns. The subsite model predicts that noncompetitive or mixed inhibition patterns can occur.
mesh_terms: D000681:Amylases / Q000037:antagonists & inhibitors / Q000378:metabolism; D001407:Bacillus / Q000201:enzymology; D001665:Binding Sites / Q000187:drug effects; D004798:Enzymes / Q000378:metabolism*; D005942:Gluconates / Q000494:pharmacology; D007783:Lactones; D008757:Methylglucosides / Q000494:pharmacology; D008956:Models, Chemical
chemical_list: D004798:Enzymes; D005942:Gluconates; D007783:Lactones; D008757:Methylglucosides; C027020:methylglucoside; D000681:Amylases; C010730:beta-glucono-1,5-lactone