Denslow N D, Ryan J W, Nguyen H P
Department of Biochemistry and Molecular Biology, University of Florida, Gainesville 32610.
Biochem Biophys Res Commun. 1994 Dec 30;205(3):1790-5. doi: 10.1006/bbrc.1994.2877.
Members of the newly recognized proline peptidase family share the ability to hydrolyze imide bonds and share six blocks of highly homologous 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 conserved 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.
