The angiotensin I converting enzyme.
The angiotensin I converting enzyme (kininase II; peptidyl dipeptidase; EC3.4.15.1) has a dual function: it converts angiotensin I to angiotensin II and it inactivates bradykinin. Lung, kidney, guinea pig plasma and testicles are among the richest sources of the enzyme. Vascular endothelial cells and bursh borders of renal proximal tubular cells contain high concentrations of the enzyme. The availability of synthetic peptide inhibitors was a great help in establishing the function of converting enzyme in normal and pathological conditions.
D000804:Angiotensin II / Q000378:metabolism; D000806:Angiotensin-Converting Enzyme Inhibitors; D000818:Animals; D000937:Antigen-Antibody Reactions; D001808:Blood Vessels / Q000201:enzymology; D001920:Bradykinin / Q000378:metabolism; D006023:Glycoproteins / Q000032:analysis; D006801:Humans; D006973:Hypertension / Q000188:drug therapy; D007668:Kidney / Q000201:enzymology; D008168:Lung / Q000098:blood supply / Q000378:metabolism; D008970:Molecular Weight; D007703:Peptidyl-Dipeptidase A / Q000032:analysis / Q000378:metabolism*; D012771:Shock, Hemorrhagic / Q000188:drug therapy; D013045:Species Specificity; D013439:Sulfhydryl Reagents / Q000494:pharmacology; D013722:Teprotide / Q000494:pharmacology / Q000627:therapeutic use
D000806:Angiotensin-Converting Enzyme Inhibitors; D006023:Glycoproteins; D013439:Sulfhydryl Reagents; D000804:Angiotensin II; D013722:Teprotide; D007703:Peptidyl-Dipeptidase A; D001920:Bradykinin