Conversion of angiotensin-1 to angiotensin-2 by a latent endothelial cell peptidyl dipeptidase that is not angiotensin-converting enzyme.
Cultured bovine pulmonary artery endothelial cells contain a second peptidyl dipeptidase, distinct from angiotensin-converting enzyme, present in an inactive form associated with a non-dialyzable inhibitor. Partial purification by glycine affinity chromatography separates enzyme from inhibitor to yield a preparation which hydrolyzes angiotensin-1, bradykinin, substance P, atriopeptin-2, enkephalin and Hip-His-Leu. This enzyme is resistant to inhibition by lisinopril, captopril, thiorphan, phosphoramidon, soybean trypsin inhibitor, PMSF and aminopeptidase and carboxypeptidase inhibitors, but is inhibited by EDTA.
D000803:Angiotensin I / Q000378:metabolism*; D000804:Angiotensin II / Q000096:biosynthesis*; D000809:Angiotensins / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D010450:Endopeptidases / Q000378:metabolism*; D004727:Endothelium / Q000201:enzymology*; D007700:Kinetics; D013379:Substrate Specificity
D000809:Angiotensins; D000804:Angiotensin II; D000803:Angiotensin I; D010450:Endopeptidases; C047929:peptidyl dipeptidase 4