Open AccessOn the Interaction of β‐Amylase with Substrate and Inhibitors, with Comments on Koshland's Induced‐Fit Hypothesis
Author(s) -
Marshall J. John
Publication year - 1973
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1973.tb02708.x
Subject(s) - amylase , chemistry , hydrolysis , substrate (aquarium) , circular dichroism , lysozyme , cyclodextrin , stereochemistry , enzyme , crystallography , biophysics , biochemistry , biology , ecology
1 The inhibition of β‐amylase by cyclodextrins has been studied; cyclomaltohexaose is a considerably more powerful inhibitor than cyclomaltoheptaose. 2 The inhibition of β‐amylase by these dextrins is substantially reduced in the presence of dimethylsulfoxide; this has been related to the change in conformation which takes place in the cyclodextrins in dimethylsulfoxide solution. 3 Circular dichroism measurements indicate the lack of a conformational change in β‐amylase on interaction with cyclomaltohexaose. 4 It has been concluded that an induced‐fit mechanism is not involved in β‐amylase action. 5 Evidence in support of the involvement of sugar ring distortion during β‐amylase catalysis, such as takes place in lysozyme‐catalyzed hydrolysis, is presented.