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Deacylation kinetics of γ‐chymotrypsin in solution and in the crystal
Author(s) -
Merli A.,
Rossi G.L.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80475-6
Subject(s) - chymotrypsin , chemistry , hydrolysis , kinetics , catalysis , crystal structure , crystallography , alpha chymotrypsin , crystal (programming language) , enzyme , stereochemistry , organic chemistry , trypsin , physics , programming language , quantum mechanics , computer science
The rate of catalyzed hydrolysis of the acyl enzyme analogs indolacryloyl‐γ‐chymotrypsin and furylacryloyl‐γ‐chymotrypsin in the crystal has been measured by single crystal microspectrophotometry and compared with the rate of catalyzed hydrolysis of acyl‐γ‐chymotrypsin in solution and acyl‐α‐chymotrypsin both in solution and in the crystal. The maximal deacylation rate is the same for both species and independent of the physical state. However, the pH dependence of the deacylation rate of crystalline acyl‐γ‐chymotrypsin shows a 0.9 unit shift in the p K of the catalytic system which is unique and probably consequent to specific lattice interactions.