Angiotensin-Converting Enzyme: Difference between revisions
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[[Image: 1o8a2.png|320px|left|thumb| Crystal Structure of Human tACE, [[1o8a]]]] | [[Image: 1o8a2.png|320px|left|thumb| Crystal Structure of Human tACE, [[1o8a]]]] | ||
{{STRUCTURE_1o8a| right| PDB=1o8a | SCENE=Angiotensin-Converting_Enzyme/Ace_opening/1 |CAPTION= Crystal Structure of Human tACE, [[1o8a]] }} | {{STRUCTURE_1o8a| right| PDB=1o8a | SCENE=Angiotensin-Converting_Enzyme/Ace_opening/1 |CAPTION= Crystal Structure of Human tACE complex with zinc and chloride ions, [[1o8a]] }} | ||
[[Angiotensin-Converting Enzyme]] (ACE) is both an exopeptidase and endopeptindase first discovered by Skeggs et al. in 1956. <ref>Skeggs, L. T., Dorer, F. E., Kahn, J. R., Lentz, K. E., Levin, M. (1981) Experimental renal hypertension: the discovery of the Renin-Angiotensin system. Soffer, R. eds. Biochemical Regulation of Blood Pressure ,3-38 John Wiley & Sons, Inc. Hoboken.</ref> ACE is a zinc- and chloride-dependent metallopeptidase that is responsible for the metabolism of key biologically active peptides, namely Angiotensin I and Bradykinin. These two peptides play a critical role in maintaining appropriate blood pressure in the human body along with a host of other homeostatic circulatory functions. ACE catalyzes the conversion of the decapeptide Angiostensin I to the octapeptide Angiostensin II. Due to its critical role in the Renin-Angiotensin-Aldosterone System (RAAS), ACE has been targeted by a number of pharmaceutical compounds to treat hypertension, diabetic nephropathy, and renal failure. <ref>PMID:10780101</ref> | [[Angiotensin-Converting Enzyme]] (ACE) is both an exopeptidase and endopeptindase first discovered by Skeggs et al. in 1956. <ref>Skeggs, L. T., Dorer, F. E., Kahn, J. R., Lentz, K. E., Levin, M. (1981) Experimental renal hypertension: the discovery of the Renin-Angiotensin system. Soffer, R. eds. Biochemical Regulation of Blood Pressure ,3-38 John Wiley & Sons, Inc. Hoboken.</ref> ACE is a zinc- and chloride-dependent metallopeptidase that is responsible for the metabolism of key biologically active peptides, namely Angiotensin I and Bradykinin. These two peptides play a critical role in maintaining appropriate blood pressure in the human body along with a host of other homeostatic circulatory functions. ACE catalyzes the conversion of the decapeptide Angiostensin I to the octapeptide Angiostensin II. Due to its critical role in the Renin-Angiotensin-Aldosterone System (RAAS), ACE has been targeted by a number of pharmaceutical compounds to treat hypertension, diabetic nephropathy, and renal failure. <ref>PMID:10780101</ref> | ||
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