Editing Angiotensin-converting enzyme (section)

{{Short description|Mammalian protein found in humans}}{{cs1 config|name-list-style=vanc}}
{{Use dmy dates|date=December 2023}}
{{hatnote|Not to be confused with [[Angiotensin-converting enzyme 2|Angiotensin-converting enzyme 2 (ACE2)]].}}
{{enzyme
| Name = Angiotensin-converting enzyme
| EC_number = 3.4.15.1
| CAS_number = 9015-82-1
| IUBMB_EC_number = 
| GO_code = 
| image = 4asq.jpg
| width = 270
| caption = Angiotensin-converting enzyme monomer, ''Drosophila melanogaster''
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'''Angiotensin-converting enzyme''' ({{EC number|3.4.15.1}}), or '''ACE''', is a central component of the [[renin–angiotensin system]] (RAS), which controls blood pressure by regulating the volume of fluids in the body. It converts the hormone [[angiotensin I]] to the active [[vasoconstriction|vasoconstrictor]] [[angiotensin II]]. Therefore, ACE indirectly increases blood pressure by causing blood vessels to constrict. [[ACE inhibitor]]s are widely used as pharmaceutical drugs for treatment of [[cardiovascular disease]]s.<ref name="Kaplans Essentials of Cardiac Anesthesia 2018 p. ">{{cite book | title=Kaplan's Essentials of Cardiac Anesthesia | publisher=Elsevier | year=2018 | isbn=978-0-323-49798-5 | doi=10.1016/c2012-0-06151-0 | quote=Mechanisms of Action:ACE inhibitors act by inhibiting one of several proteases responsible for cleaving the decapeptide Ang I to form the octapeptide Ang II. Because ACE is also the enzyme that degrades bradykinin, ACE inhibitors increase circulating and tissue levels of bradykinin (Fig. 8.4). }}</ref>

Other lesser known functions of ACE are degradation of [[bradykinin]],<ref>{{cite book | title = ACEi and ARBS in Hypertension and Heart Failure | volume = 5 | vauthors = Fillardi PP | publisher = Springer International Publishing | year = 2015 | isbn = 978-3-319-09787-9 | location = Switzerland | pages = 10–13 }}</ref> [[substance P]]<ref>{{cite journal | vauthors = Dicpinigaitis PV | title = Angiotensin-converting enzyme inhibitor-induced cough: ACCP evidence-based clinical practice guidelines | journal = Chest | volume = 129 | issue = 1 Suppl | pages = 169S–173S | date = January 2006 | pmid = 16428706 | doi = 10.1378/chest.129.1_suppl.169S }}</ref> and [[amyloid beta|amyloid beta-protein]].<ref name = "Hemming_2005">{{cite journal | vauthors = Hemming ML, Selkoe DJ | title = Amyloid beta-protein is degraded by cellular angiotensin-converting enzyme (ACE) and elevated by an ACE inhibitor | journal = The Journal of Biological Chemistry | volume = 280 | issue = 45 | pages = 37644–37650 | date = November 2005 | pmid = 16154999 | pmc = 2409196 | doi = 10.1074/jbc.M508460200 | doi-access = free }}</ref>