Open AccessENZYMATIC INACTIVATION OF PEPTIDE HORMONES POSSESSING A C-TERMINAL AMIDE GROUP
Author(s) -
John D. Glass,
Irving L. Schwartz,
Roderich Walter
Publication year - 1969
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.63.4.1426
Subject(s) - tetrapeptide , chemistry , biochemistry , vasopressin , enzyme , carboxamide , peptide , arginine , phenylalanine , peptide hormone , moiety , stereochemistry , amino acid , hormone , biology , endocrinology
A partially purified enzyme extracted from the bladder of the toad,Bufo marinus L., was found to cleave the glycine amide moiety from oxytocin, 8-lysine-vasopressin, 8-arginine-vasopressin, and other hormone analogs terminating in a primary carboxamide group; however, this enzyme does not attack hormone analogs terminating with a methylamide, dimethylamide, or carboxyl group. Preliminary experiments indicate that a functionally similar enzyme is also present in the mammalian kidney, the major target organ of neurohypophyseal antidiuretic hormones. This enzyme, besides inactivating oxytocin and 8-lysine-vasopressin, also cleaves the phenylalanine amide moiety from a tetrapeptide analog of gastrin, another hormone terminating in a primary carboxamide group. Attention is drawn to the possible general significance of “carboxamidopeptidases” for the termination of the action of peptide hormones in which the C-terminal amino acid residue bears a carboxamide group.