Lisinopril-Angiotensin Converting Enzyme

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Structure 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.

Structure of Lisinopril

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