protein_function: Converts angiotensin I to angiotensin II by release ofthe terminal His-Leu, this results in an increase of thevasoconstrictor activity of angiotensin. Also able to inactivatebradykinin, a potent vasodilator. Has also a glycosidase activitywhich releases GPI-anchored proteins from the membrane by cleavingthe mannose linkage in the GPI moiety. This GPIase activity seemsto be crucial for the egg-binding ability of the sperm..
Angiotensin-converting enzyme(ACE), an exopeptidase, is a circulating enzyme that participates in the body"s renin-angiotensin system(RAS), which mediates extracellular volume(i.e. that of the blood plasma, lymph and interstitial fluid), and arterial vasoconstriction. It is secreted by pulmonary and renal endothelial cells and catalyzes the conversion of decapeptide angiotensin I to octapeptide angiotensin II. Using a DNA marker at the growth hormone gene locus, which they characterized as "extremely polymorphic" and which showed no recombination with ACE, ACE was mapped to 17q22-q24, consistent with the in situ hybridization mapping to 17q23. ACE, or kininase II, is a dipeptidyl carboxypeptidase that plays an important role in blood pressure regulation and electrolyte balance by hydrolyzing angiotensin I into angiotensin II, a potent vasopressor, and aldosterone-stimulating peptide. The enzyme is also able to inactivate bradykinin, a potent vasodilator.