Open AccessSubsite Mapping of Enzymes
Author(s) -
THOMA John A,
CROOK Carolyn
Publication year - 1982
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1982.tb06483.x
Subject(s) - monomer , enzyme , hydrolysis , substrate (aquarium) , chemistry , non competitive inhibition , stereochemistry , distortion (music) , hydrolase , ring (chemistry) , biochemistry , biology , computer science , organic chemistry , ecology , polymer , amplifier , computer network , bandwidth (computing)
Our earlier subsite mapping studies led us to believe that ground state distortion occurred when a gluco‐ pyranoside 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 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.