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Angiotensin-converting enzyme-2: a molecular and cellular perspective.
F J Warner1, A I Smith, N M Hooper
1School of Biochemistry and Microbiology, University of Leeds, Leeds LS2 9JT, United Kingdom. fiona.warner@med.monash.edu.au.
Cellular and Molecular Life Sciences : CMLS
|November 19, 2004
Summary
Angiotensin-converting enzyme-2 (ACE2) is a carboxypeptidase enzyme. This review covers ACE2
Area of Science:
- Biochemistry
- Enzymology
- Molecular Biology
Background:
- Angiotensin-converting enzyme-2 (ACE2) is a homologue of ACE.
- ACE2 functions as a carboxypeptidase, hydrolyzing angiotensin II to angiotensin (1-7).
- ACE2 also processes other peptides like dynorphin A, apelin-13, and des-Arg(9) bradykinin.
Purpose of the Study:
- To review the biochemistry of ACE2.
- To discuss key findings in ACE2 research.
- To highlight the implications of ACE2 structure and inhibitors for future studies.
Main Methods:
- Literature review of ACE2 biochemistry and function.
- Discussion of structural biology findings (crystal structures).
- Overview of ACE2 inhibitor development.
Main Results:
- ACE2's role in the renin-angiotensin system by hydrolyzing angiotensin II.
- Identification of ACE2's involvement in other peptide systems.
- Elucidation of crystal structures for ACE2 and testicular ACE.
Conclusions:
- ACE2 plays a significant role in cardiovascular and metabolic diseases.
- ACE2 serves as a receptor for SARS-CoV.
- Structural and inhibitor studies provide a foundation for future ACE2 research.