Structure of angiotensin I-converting enzyme.

@article{Sturrock2004StructureOA,
  title={Structure of angiotensin I-converting enzyme.},
  author={Edward D. Sturrock and Ramanathan Natesh and Jason M van Rooyen and Kamala Rani Acharya},
  journal={Cellular and molecular life sciences : CMLS},
  year={2004},
  volume={61 21},
  pages={
          2677-86
        }
}
Angiotensin-converting enzyme (ACE) is a zinc- and chloride-dependent metallopeptidase that plays a vital role in the metabolism of biologically active peptides. Until recently, much of the inhibitor design and mechanism of action of this ubiquitous enzyme was based on the structures of carboxypeptidase A and thermolysin. When compared to the recently solved structures of the testis isoform of ACE (tACE) and its Drosophila homologue (AnCE), carboxypeptidase A showed little structural homology… CONTINUE READING

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