Mechanistic studies on carboxypeptidase A from goat pancreas Part II: Evidence for carboxyl group.
Loading...
Date
1985-09
Authors
Journal Title
Journal ISSN
Volume Title
Publisher
Abstract
Studies with substrate analogues and the pH optimum indicated the involvement of
carboxyl group in the active site of goat carboxypeptidase A. Chemical modification of the
enzyme with 1-cyclohexyl-3-(2-morpholinoethyl) carbodiimide methoI -p-toluene sulphonate, a
carboxyl specific reagent, led to loss of both esterase and peptidase activities. Protection
studies showed that this carboxyl group was in the active site and was protected by ßphenylpropionic
acid and glycyl-L-tyrosine. Kinetic studies also confirmed the involvement of
carboxylic group because the enzyme modification with water soluble carbodiimide was a two
step reaction which excluded the possibility of tyrosine or lysine which are known to give a one
step reaction with this reagent.
Description
Keywords
Active site, carboxyl group, carboxypeptidase A, chemical modification, goat
Citation
Dua R D, Gupta Kamlesh. Mechanistic studies on carboxypeptidase A from goat pancreas Part II: Evidence for carboxyl group. Journal of Biosciences. 1985 Sept; 9(1&2): 91-97.