Kohen, A. and Klinman, J.P. (1998) Enzyme Catalysis: Beyond Classical Paradigms. Accounts of Chemical Research , 31 (7). pp. 397-404.
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Abstract
Despite many decades of intense study, a full description of enzyme catalysis at the molecular level remains to be achieved. A number of aspects of biocatalysis are widely accepted, including (i) the conversion of a chemical reaction from an inter- to an intramolecular process with the concomitant decrease in the entropy of activation and (ii) the stabilization of the transition state (TS) by the precise orientation of multiple functional groups at the enzyme active site. These functional groups perform the roles of general acid/base, electrophilic/nucleophilic catalysis and charge neutralization via electrostatic and H-bonding interactions. The process of covalent bond breaking and forming in enzyme catalysis is accompanied by substrate binding, product release, and protein rearrangement steps, which are rate determining for many enzymes. The resulting, multibarrier..........
| Item Type: | Article |
|---|---|
| Author Affiliation: | Departments of Chemistry and Molecular and Cell Biology, University of California at Berkeley, Berkeley, California 94720 |
| Subjects: | Plant Physiology and Biochemistry > Biochemistry |
| Divisions: | General |
| Depositing User: | Mr. SanatKumar Behera |
| Date Deposited: | 12 Apr 2012 06:03 |
| Last Modified: | 12 Apr 2012 06:05 |
| Official URL: | http://dx.doi.org/10.1021/ar9701225 |
| URI: | http://eprints.icrisat.ac.in/id/eprint/4663 |
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