The active site specificity of angiotensin II converting Enzyme 2 investigated through single and multiple residue changes and {beta}-amino acid substrate analogs

Daniel J Clayton, Iresha Hanchapola, Patrick Perlmutter, Alexander Ian Smith, Marie Isabel Aguilar

Research output: Chapter in Book/Report/Conference proceedingChapter (Book)Researchpeer-review

2 Citations (Scopus)

Abstract

Angiotensin converting enzyme 2 (ACE2) is a zinc carboxypeptidase involved in the renin angiotensin system (RAS). This enzyme inactivates the potent vasopressive peptide angiotensin II (AngII) by removing the C-terminal phenylalanine residue. ACE2 is also found to be upregulated in the heart in human and animal models of cardiovascular disease and specifically in the human fibrotic liver [1]. Given the role of ACE2 in the RAS and its suspected involvement in other organ systems, a stable and specific inhibitor of low toxicity would be useful in further elucidating the precise role that ACE2 plays in the pathology of heart and liver disease and as a possible therapeutic for hypotension associated with chronic liver failure.
Original languageEnglish
Title of host publicationPeptides for Youth: The Proceedings of the 20th American Peptide Symposium
EditorsS Del Valle, E Escher, W D Lubell
Place of PublicationUSA
PublisherSpringer
Pages559 - 560
Number of pages2
Edition611
ISBN (Print)9780387736563
Publication statusPublished - 2009

Cite this

Clayton, D. J., Hanchapola, I., Perlmutter, P., Smith, A. I., & Aguilar, M. I. (2009). The active site specificity of angiotensin II converting Enzyme 2 investigated through single and multiple residue changes and {beta}-amino acid substrate analogs. In S. Del Valle, E. Escher, & W. D. Lubell (Eds.), Peptides for Youth: The Proceedings of the 20th American Peptide Symposium (611 ed., pp. 559 - 560). Springer.