Subsite Mapping of Enzymes

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Abstract
Subsite mapping studies led to the belief that ground state distortion occurred when a glucopyranoside ring filled the site which held the substrate monomer unit transferred to water during hydrolysis. This hypothesis was tested by performing double inhibitor studies on 2 amylases (EC 3.2.1.1) of bacterial origin (Taka-amylase A, Bacillus amyloliquefaciens]. A general theory for multiple inhibition of this type is developed and applied to these 2 enzymes. The data are consistent with the hypothesis that ground state strain occurs when substrates are bound to carbohydrases. 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.