THE NATURE OF INTERACTION BETWEEN THE CARBOXYLATE OF SUBSTRATES AND THE GUANIDINIUM MOIETY OF ARG-145 IN CARBOXYPEPTIDASE-A PROBED BY INHIBITORS OF THE ENZYME

Authors
KIM DH PARK JI
Citation
Dh. Kim et Ji. Park, THE NATURE OF INTERACTION BETWEEN THE CARBOXYLATE OF SUBSTRATES AND THE GUANIDINIUM MOIETY OF ARG-145 IN CARBOXYPEPTIDASE-A PROBED BY INHIBITORS OF THE ENZYME, Bioorganic & medicinal chemistry letters, 6(24), 1996, pp. 2967-2970
Citations number
21
Categorie Soggetti
Chemistry Inorganic & Nuclear","Chemistry Medicinal
Journal title
Bioorganic & medicinal chemistry letters → ACNP
ISSN journal
0960894X
Volume
6
Issue
24
Year of publication
1996
Pages
2967 - 2970
Database
ISI
SICI code
0960-894X(1996)6:24<2967:TNOIBT>2.0.ZU;2-2
Abstract
Replacement of the alpha-proton of 2-benzyl-3-hydoroxypropanoic acid a competitive inhibitor of carboxypeptidase A with a fluoro group broug ht about a 2-fold increase in K-i value (0.61 mM --> 1.19 mM), while p K(a) value decreased by 1.4 units (4.36 --> 2.95), suggesting that the carboxylate of the inhibitor and that of substrates as well are hydro gen bonded to the guanidinium moiety of Arg-145 of the enzyme. Copyrig ht (C) 1996 Elsevier Science Ltd