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Human testis angiotensin-converting enzyme: Crystal structure of a glycosylation mutant and investigation of a putative hinge-mechanism by normal mode analysis.Watermeyer, Jean Margaret January 2004 (has links)
Human angiotensin-converting enzyme (ACE) is a key enzyme in the regulation of blood pressure via the renin-angiotensin and kallikrein-kinin systems. A number of orally active drugs have been developed over the years that target somatic ACE, for the treatment of hypertension, myocardial infarction and congestive heart failure. Protein structural information about ACE is an important key for the understanding of the mechanism and substrate-specificity of the enzyme. However, this information has only begun to be elucidated in the past year, with the solution of crystal structures of human testis ACE (tACE), and homologues Drosophila AnCE and human ACE2. tACE is identical to the C-terminal domain of somatic ACE, which consists of two homologous domains, each having a slightly different substrate-specificity. This thesis describes the purification, crystallisation and X-ray crystal structure-determination of a glycosylation-deficient mutant of tACE, tACEG1,3, to 2.9 Å / .
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Human testis angiotensin-converting enzyme: Crystal structure of a glycosylation mutant and investigation of a putative hinge-mechanism by normal mode analysis.Watermeyer, Jean Margaret January 2004 (has links)
Human angiotensin-converting enzyme (ACE) is a key enzyme in the regulation of blood pressure via the renin-angiotensin and kallikrein-kinin systems. A number of orally active drugs have been developed over the years that target somatic ACE, for the treatment of hypertension, myocardial infarction and congestive heart failure. Protein structural information about ACE is an important key for the understanding of the mechanism and substrate-specificity of the enzyme. However, this information has only begun to be elucidated in the past year, with the solution of crystal structures of human testis ACE (tACE), and homologues Drosophila AnCE and human ACE2. tACE is identical to the C-terminal domain of somatic ACE, which consists of two homologous domains, each having a slightly different substrate-specificity. This thesis describes the purification, crystallisation and X-ray crystal structure-determination of a glycosylation-deficient mutant of tACE, tACEG1,3, to 2.9 Å / .
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The mechanism of action of captopril in human renal cell carcinoma /Reid, Janet Louise. January 2003 (has links) (PDF)
Thesis (Ph.D.) - University of Queensland, 2003. / Includes bibliography.
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Human testis angiotensin-converting enzyme: crystal structure of a glycosylation mutant and investigation of a putative hinge-mechanism by normal mode analysisWatermeyer, Jean Margaret January 2004 (has links)
Magister Scientiae - MSc / Human angiotensin-converting enzyme (ACE) is a key enzyme in the
regulation of blood pressure via the renin-angiotensin and kallikrein-kinin
systems. A number of orally active drugs have been developed over the
years that target somatic ACE, for the treatment of hypertension, myocardial
infarction and congestive heart failure. Protein structural information about
ACE is an important key for the understanding of the mechanism and
substrate-specificity of the enzyme. However, this information has only
begun to be elucidated in the past year, with the solution of crystal structures
of human testis ACE (tACE), and homologues Drosophila AnCE and
human ACE2. tACE is identical to the C-terminal domain of somatic ACE,
which consists of two homologous domains, each having a slightly different
substrate-specificity.
This thesis describes the purification, crystallisation and X-ray crystal
structure-determination of a glycosylation-deficient mutant of tACE, tACEG1,3,
to 2.9 Å. The structure of tACE-G1,3 aligns closely with that of
native tACE, indicating that the mutations did not alter the conformation.
The ability to achieve minimal glycosylation of tACE for crystallisation
purposes via mutation, rather than using expensive glycosidase inhibitors,
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should prove advantageous for further structural studies, such as the study of
the binding of novel inhibitors.
In all of the tACE structures thus far observed, the active site is closed off
from the external medium in a deep cleft, so that it is unclear how a large
substrate molecule could gain access. However, a hinge motion that opens
this cleft has been observed in the structures of ACE2. Temperature factor
and sequence comparison between tACE, tACE-G1,3, AnCE and ACE2
suggests the functional conservation of three flexible loop regions, as well as
the sequence conservation of three constrained regions, involved in the
hinge. Normal mode analysis reveals the intrinsic flexibility of tACE, and
further suggests that a putative open form of tACE would behave similarly
to the open form of ACE2. Based on these indications, a conservation of the
ACE2 hinge-bending mechanism is proposed.
Temperature factor analysis also reveals that subdomain II, containing
bound chloride ions, is more structurally rigid than subdomain I, in all
structures considered.
Based on these results, lines of investigation are suggested that should yield
insight into the mechanisms of action of ACE and its association with
various substrates and inhibitors, ideally aiding in the development of novel
drugs for the treatment of cardiac disease. / South Africa
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The estimation of renin in biological fluidsLee, Michael R. January 1965 (has links)
No description available.
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Formation of drug-protein conjugates from captoprilYeung, J. H. K. January 1984 (has links)
No description available.
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Ligand binding studies of Drosophila angiotensin converting enzymes and mouse major urinary proteinBingham, Richard Jonathan January 2003 (has links)
No description available.
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The interaction of thiopeptides with angiotensin converting enzyme : synthesis, conformation, and enzymologyMaziak, Louise Ann. January 1984 (has links)
No description available.
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A comparison of hemodynamic responses in losartan- and enalapril- treated normotensive rats /Wang, De, January 1999 (has links)
Thesis (M. Med. Sc.)--University of Hong Kong, 1999. / Includes bibliographical references (leaves 48-62).
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A comparison of hemodynamic responses in losartan- and enalapril- treated normotensive ratsWang, De, January 1999 (has links)
Thesis (M.Med.Sc.)--University of Hong Kong, 1999. / Includes bibliographical references (leaves 48-62). Also available in print.
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