Is .gamma.-chymotrypsin a tetrapeptide acyl-enzyme adduct of .alpha.-chymotrypsin?
- 22 August 1989
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 28 (17), 7033-7038
- https://doi.org/10.1021/bi00443a038
Abstract
Refinement of the structure of .gamma.-chymotrypsin based on X-ray crystallographic data to 1.6-.ANG. resolution has confirmed the overall conformation of the molecule as reported previously [Cohen, G. H., Silverton, E. W., and Davies, D. R. (1981) J. Mol. Biol. 148, 449-479]. In addition, the new refinement suggests that .gamma.-chymotrypsin, which is operationally defined by its crystalline habit, may not be the free enzyme but rather a complex, possibly an acyl-enzyme adduct, with the tetrapeptide Pro-Gly-Ala-Tyr (or a close homologue). The crystallographic refinement provides a detailed geometrical description of the enzyme-substrate-solvent interactions that occur in the presumptive adduct.This publication has 13 references indexed in Scilit:
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