GUINEA-PIG MEMBRANE-BOUND AMINOPEPTIDASE-P IS A MEMBER OF THE PROLINEPEPTIDASE FAMILY

Citation
Nd. Denslow et al., GUINEA-PIG MEMBRANE-BOUND AMINOPEPTIDASE-P IS A MEMBER OF THE PROLINEPEPTIDASE FAMILY, Biochemical and biophysical research communications, 205(3), 1994, pp. 1790-1795
Citations number
20
Categorie Soggetti
Biology,Biophysics
ISSN journal
0006291X
Volume
205
Issue
3
Year of publication
1994
Pages
1790 - 1795
Database
ISI
SICI code
0006-291X(1994)205:3<1790:GMAIAM>2.0.ZU;2-O
Abstract
Members of the newly recognized proline peptidase family share the abi lity to hydrolyze imide bonds and share six blocks of highly homologou s amino acid sequences. We have found that guinea pig lung and kidney forms of aminopeptidase P, both forms bound to membranes via glycosyl phosphatidylinositol lipid anchors, share at least three of the six co nserved blocks of amino acid sequences. In addition, aminopeptidase P acts as an aminoacylproline hydrolase and thus appears to be a member of the proline peptidase family. (C) 1994 Academic Press, Inc.