Lisinopril-Angiotensin Converting Enzyme
From Proteopedia
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| - | + | ==ACE Structure== | |
<StructureSection load='2c6n' Caption for this structure'Structure of human somatic angiontensin-I converting enzyme N domain with lisinopril | <StructureSection load='2c6n' Caption for this structure'Structure of human somatic angiontensin-I converting enzyme N domain with lisinopril | ||
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| - | This is a default text for your page '''Lisinopril-Angiotensin Converting Enzyme'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
| - | == | + | == Function of Enzyme== |
The angiotensin converting enzyme (ACE) is an enzyme that is found renin angiotensin system which is often known as RAS. RAS is a hormone system that regulates blood pressure and fluid as well as electrolyte balance. It is a zinc and chloride dependent metallopeptidase that is membrane bound. The job of the enzyme is to catalyze the conversion of angiotensin I to the physiologically active peptide angiotensin II. It does this cleaving C-terminal dipeptide on the angiotensin I. It also inactivates the hormone bradykinin (vasodepressor) by removing two C-terminal dipeptides. This enzyme is a type 1 membrane bound protein that has 28 residue C- terminal cytosolic domains as well as 22- residue hydrophobic transmembrane domains and it has 1227 residue extracellular domain. The extracellular domain has two more domains that branch off of it. Which are N- domains and C-domains. In each of these domains are two histidine residues which are used to binding zinc ligands with glutamine to make the geometry tetrahedral. Through mutational analyses and detailed kinetics it is clear that both zinc sites have activity which is considered to be catalytic. | The angiotensin converting enzyme (ACE) is an enzyme that is found renin angiotensin system which is often known as RAS. RAS is a hormone system that regulates blood pressure and fluid as well as electrolyte balance. It is a zinc and chloride dependent metallopeptidase that is membrane bound. The job of the enzyme is to catalyze the conversion of angiotensin I to the physiologically active peptide angiotensin II. It does this cleaving C-terminal dipeptide on the angiotensin I. It also inactivates the hormone bradykinin (vasodepressor) by removing two C-terminal dipeptides. This enzyme is a type 1 membrane bound protein that has 28 residue C- terminal cytosolic domains as well as 22- residue hydrophobic transmembrane domains and it has 1227 residue extracellular domain. The extracellular domain has two more domains that branch off of it. Which are N- domains and C-domains. In each of these domains are two histidine residues which are used to binding zinc ligands with glutamine to make the geometry tetrahedral. Through mutational analyses and detailed kinetics it is clear that both zinc sites have activity which is considered to be catalytic. | ||
Revision as of 16:51, 3 May 2019
ACE Structure
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The drug Lisinopril was patent in
Mechanism of Action ==
Side Effects
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</StructureSection>
References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
