Is .gamma.-chymotrypsin a tetrapeptide acyl-enzyme adduct of .alpha.-chymotrypsin?
| Autor: | Melinda M. Dixon, Brian W. Matthews |
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| Rok vydání: | 1989 |
| Předmět: |
Models
Molecular chemistry.chemical_classification Chymotrypsin biology Tetrapeptide Macromolecular Substances Protein Conformation Chemistry Stereochemistry Hydrogen Bonding Alpha-chymotrypsin Biochemistry Adduct Crystallography Gamma-chymotrypsin Enzyme X-Ray Diffraction X-ray crystallography biology.protein Molecule |
| Zdroj: | Biochemistry. 28:7033-7038 |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/bi00443a038 |
| Popis: | Refinement of the structure of gamma-chymotrypsin based on X-ray crystallographic data to 1.6-A resolution has confirmed the overall conformation of the molecule as reported previously [Cohen, G. H., Silverton, E. W., & 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. |
| Databáze: | OpenAIRE |
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