Open Accessα‐Chymotrypsin‐Catalyzed Hydrolysis of N ‐Furylacryloyl‐Tyrosine Derivatives
Author(s) -
Yu S. H.,
Viswanatha T.
Publication year - 1969
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1969.tb00778.x
Subject(s) - chemistry , chymotrypsin , tyrosine , acylation , hydrolysis , substrate (aquarium) , non competitive inhibition , catalysis , enzyme , kinetics , stereochemistry , medicinal chemistry , organic chemistry , biochemistry , trypsin , biology , ecology , physics , quantum mechanics
The hydrolysis of furylacryloyl‐tyrosine derivatives by chymotrypsin has been investigated. The reaction of N ‐furylacryloyl‐ l ‐tyrosine methyl ester with the enzyme can be followed spectrophotometrically at 340 nm. The product of the reaction, N ‐furylacryloyl‐ l ‐tyrosine, does not function as an inhibitor. The d ‐isomer of the substrate functions as a competitive inhibitor. The reaction of furylacryloyl‐ l ‐tyrosine methyl ester with chymotrypsin at low pH is accompanied by absorption changes separable into three distinct stages. These studies offer evidence for the occurrence of the reaction via the acylenzyme route in the case of typical substrates. Analysis of the kinetics of the reaction suggest the formation of an additional intermediate prior to the acylation of the enzyme.