articleJournal of Biological ChemistryApr 1, 2002HYBRID OA

Hydrolysis of Biological Peptides by Human Angiotensin-converting Enzyme-related Carboxypeptidase

Millennium Engineering and Integration (United States) · Cardiovascular Research Center · +2 more institutions

PubMed
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Abstract

Human angiotensin-converting enzyme-related carboxypeptidase (ACE2) is a zinc metalloprotease whose closest homolog is angiotensin I-converting enzyme. To begin to elucidate the physiological role of ACE2, ACE2 was purified, and its catalytic activity was characterized. ACE2 proteolytic activity has a pH optimum of 6.5 and is enhanced by monovalent anions, which is consistent with the activity of ACE. ACE2 activity is increased approximately 10-fold by Cl(-) and F(-) but is unaffected by Br(-). ACE2 was screened for hydrolytic activity against a panel of 126 biological peptides, using liquid chromatography-mass spectrometry detection. Eleven of the peptides were hydrolyzed by ACE2, and in each case, the…

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Authors

14

Topics & keywords

Keywords
  • Hydrolysis
  • Carboxypeptidase
  • Enzyme
  • Chemistry
  • Angiotensin II
  • Angiotensin III
  • Biochemistry
  • Metalloproteinase
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