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
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.