Differences in the properties and enzymatic specificities of the two active sites of angiotensin I-converting enzyme (kininase II). Studies with bradykinin and other …
E Jaspard, L Wei, F Alhenc-Gelas - Journal of Biological Chemistry, 1993 - ASBMB
Angiotensin I-converting enzyme (ACE, EC 3.4. 15.1) has been recently shown to contain
two very similar domains, each of which bears a functional active site hydrolyzing Hip-His-
Leu or angiotensin I (AI). The substrate specificity of the two active sites of ACE was
compared using wild-type recombinant ACE and mutants, where one active site is
suppressed by deletion or inactivated by mutations of 2 histidines coordinating an essential
zinc atom. Both active sites converted bradykinin (BK) to BK1-7 and BK1-5 with similar …
two very similar domains, each of which bears a functional active site hydrolyzing Hip-His-
Leu or angiotensin I (AI). The substrate specificity of the two active sites of ACE was
compared using wild-type recombinant ACE and mutants, where one active site is
suppressed by deletion or inactivated by mutations of 2 histidines coordinating an essential
zinc atom. Both active sites converted bradykinin (BK) to BK1-7 and BK1-5 with similar …