Enzymatic mechanochemistry: A new approach to studying the mechanism of enzyme action

26Citations
Citations of this article
13Readers
Mendeley users who have this article in their library.
Get full text

Abstract

1. 1. Covalent binding of model enzymes, chymotrypsin and trypsin, to elastic polymer supports, nylon and viscose (cellulose) fibers, human hair, methacrylate rubber, has been effectuated. On mechanical stretching of the fibers, the catalytic activity of the enzymes bound to them decreases, and when they relax, it increases to the initial level. The data obtained by us fit the concept that the effect is due to reversible deformation of the bound enzyme molecules induced by fiber stretching. 2. 2. Analysis of the dependence of the catalytic activity of the enzymes chemically bound to the fiber on the degree of fiber deformation shows that the reversible inactivation of the enzymes induced by support stretching occurs even if the deformation of the enzymes' molecules is as small as 0.5 Å. 3. 3. The deformation of the enzyme molecules induced by fiber stretching entails a change in the substrate specificity of the biocatalysts, i.e. the activity towards "good" substrates decreases, and towards "poor" substrates increases. 4. 4. The deformation of the enzyme molecules induced by fiber stretching resuits in a decrease of the specific catalytic activity of the biocatalyst, whereas its thermal stability increases. 5. 5. The results obtained allowed a new, mechanochemical, approach to be suggested for studying major problems of enzymatic catalysis. © 1976.

Cite

CITATION STYLE

APA

Klibanov, A. M., Samokhin, G. P., Martinek, K., & Berezin, I. V. (1976). Enzymatic mechanochemistry: A new approach to studying the mechanism of enzyme action. BBA - Enzymology, 438(1), 1–12. https://doi.org/10.1016/0005-2744(76)90218-7

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free