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Department of Molecular and Cell Biology

The structure of testis angiotensin-converting enzyme (tACE-g13) in complex with the inhibitor RXPA380

Abstract

dc:description.abstract

Angiotensin-converting enzyme (ACE), a zinc metalloprotease, is a key regulator of the mammalian renin-angiotensin system (RAS) Primarily, ACF is a dipeptidl peptidase which cleaves angiotensin I to produce angiotensin II, a potent vasoconstrictor. By the same enzymatic mechanism, ACE also inactivates the vasodilator bradykinin. The main overall effect of these actions is an increase in blood pressure. Several ACF inhibitors have been developed as drugs for the treatment of myocardial infarction, hypertension, kidney failure and heart failure.

Degree

thesis:*
Grantor dc:publisher.institution
Department of Molecular and Cell Biology
Year dc:date.issued
2006

Author and committee

dc:creator, dc:contributor.*
Author dc:creator
  • Chitapi, Itai
Advisors dc:contributor.advisor
  • Sewell, Bryan Trevor
  • Sturrock, E D

Rights

Language dc:language.iso
eng

Identifiers

dc:identifier.*
Handle dc:identifier.uri
http://hdl.handle.net/11427/4248
OAI identifier oai:identifier
oai:open.uct.ac.za:11427/4248

Chain of custody

source
Harvested from
University of Cape Town
Base URL
open.uct.ac.za/oai/request
Last updated
2026-07-22
Source record
OAI-PMH GetRecord
related terms
citation

Chitapi, Itai. The structure of testis angiotensin-converting enzyme (tACE-g13) in complex with the inhibitor RXPA380. Department of Molecular and Cell Biology, 2006. http://hdl.handle.net/11427/4248