Significance of active site residues in the n-domain selectivity of angiotensin-converting enzyme

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dc.contributor.advisorSturrock, Edward Den_ZA
dc.contributor.authorDouglas, Ross Gavinen_ZA
dc.date.accessioned2015-01-08T19:59:58Z
dc.date.available2015-01-08T19:59:58Z
dc.date.issued2011en_ZA
dc.description.abstractAngiotensin-converting enzyme (ACE) is a zinc metallopeptidase that plays an important role in vascular function; with ACE inhibitors being clinically utilised in the treatment of cardiovascular disease and diabetic nephropathy. Somatic ACE consists of two homologous catalytically active domains (designated N- and C-domains) that share high overall sequence identity and structural topology. Despite the high degree of similarity between domains, each domain displays differences in substrate processing and inhibitor binding abilities. This suggests that active site residues differing between the two domains could provide unique interactions within the N-domain that allow for N-selective binding and processing. Literature reports of ACE crystal structures and studies with substrate and inhibitor analogues have implicated unique residues present in the S2 and S2' subsites in providing important interactions for N-selectivity.en_ZA
dc.identifier.apacitationDouglas, R. G. (2011). <i>Significance of active site residues in the n-domain selectivity of angiotensin-converting enzyme</i>. (Thesis). University of Cape Town ,Faculty of Health Sciences ,Division of Medical Biochemistry. Retrieved from http://hdl.handle.net/11427/11786en_ZA
dc.identifier.chicagocitationDouglas, Ross Gavin. <i>"Significance of active site residues in the n-domain selectivity of angiotensin-converting enzyme."</i> Thesis., University of Cape Town ,Faculty of Health Sciences ,Division of Medical Biochemistry, 2011. http://hdl.handle.net/11427/11786en_ZA
dc.identifier.citationDouglas, R. 2011. Significance of active site residues in the n-domain selectivity of angiotensin-converting enzyme. University of Cape Town.en_ZA
dc.identifier.ris TY - Thesis / Dissertation AU - Douglas, Ross Gavin AB - Angiotensin-converting enzyme (ACE) is a zinc metallopeptidase that plays an important role in vascular function; with ACE inhibitors being clinically utilised in the treatment of cardiovascular disease and diabetic nephropathy. Somatic ACE consists of two homologous catalytically active domains (designated N- and C-domains) that share high overall sequence identity and structural topology. Despite the high degree of similarity between domains, each domain displays differences in substrate processing and inhibitor binding abilities. This suggests that active site residues differing between the two domains could provide unique interactions within the N-domain that allow for N-selective binding and processing. Literature reports of ACE crystal structures and studies with substrate and inhibitor analogues have implicated unique residues present in the S2 and S2' subsites in providing important interactions for N-selectivity. DA - 2011 DB - OpenUCT DP - University of Cape Town LK - https://open.uct.ac.za PB - University of Cape Town PY - 2011 T1 - Significance of active site residues in the n-domain selectivity of angiotensin-converting enzyme TI - Significance of active site residues in the n-domain selectivity of angiotensin-converting enzyme UR - http://hdl.handle.net/11427/11786 ER - en_ZA
dc.identifier.urihttp://hdl.handle.net/11427/11786
dc.identifier.vancouvercitationDouglas RG. Significance of active site residues in the n-domain selectivity of angiotensin-converting enzyme. [Thesis]. University of Cape Town ,Faculty of Health Sciences ,Division of Medical Biochemistry, 2011 [cited yyyy month dd]. Available from: http://hdl.handle.net/11427/11786en_ZA
dc.language.isoengen_ZA
dc.publisher.departmentDivision of Medical Biochemistryen_ZA
dc.publisher.facultyFaculty of Health Sciencesen_ZA
dc.publisher.institutionUniversity of Cape Town
dc.subject.otherMedical Biochemistryen_ZA
dc.titleSignificance of active site residues in the n-domain selectivity of angiotensin-converting enzymeen_ZA
dc.typeDoctoral Thesis
dc.type.qualificationlevelDoctoral
dc.type.qualificationnamePhDen_ZA
uct.type.filetypeText
uct.type.filetypeImage
uct.type.publicationResearchen_ZA
uct.type.resourceThesisen_ZA
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