Angiotensin-converting enzyme

Angiotensin-converting enzyme monomer, Drosophila melanogaster
Identifiers
EC no.3.4.15.1
CAS no.9015-82-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins
ACE
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesACE, angiotensin I converting enzyme, ACE1, CD143, DCP, DCP1, ICH, MVCD3, Angiotensin-converting enzyme
External IDsOMIM: 106180; MGI: 87874; HomoloGene: 37351; GeneCards: ACE; OMA:ACE - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_009598
NM_207624
NM_001281819

RefSeq (protein)

NP_001268748
NP_033728
NP_997507

Location (UCSC)Chr 17: 63.48 – 63.5 MbChr 11: 105.86 – 105.88 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Angiotensin-converting enzyme (EC 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 vasoconstrictor angiotensin II. Therefore, ACE indirectly increases blood pressure by causing blood vessels to constrict. ACE inhibitors are widely used as pharmaceutical drugs for treatment of cardiovascular diseases.[5]

Other lesser known functions of ACE are degradation of bradykinin,[6] substance P[7] and amyloid beta-protein.[8]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000159640Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020681Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Kaplan's Essentials of Cardiac Anesthesia. Elsevier. 2018. doi:10.1016/c2012-0-06151-0. ISBN 978-0-323-49798-5. 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).
  6. ^ Fillardi PP (2015). ACEi and ARBS in Hypertension and Heart Failure. Vol. 5. Switzerland: Springer International Publishing. pp. 10–13. ISBN 978-3-319-09787-9.
  7. ^ Dicpinigaitis PV (January 2006). "Angiotensin-converting enzyme inhibitor-induced cough: ACCP evidence-based clinical practice guidelines". Chest. 129 (1 Suppl): 169S–173S. doi:10.1378/chest.129.1_suppl.169S. PMID 16428706.
  8. ^ Hemming ML, Selkoe DJ (November 2005). "Amyloid beta-protein is degraded by cellular angiotensin-converting enzyme (ACE) and elevated by an ACE inhibitor". The Journal of Biological Chemistry. 280 (45): 37644–37650. doi:10.1074/jbc.M508460200. PMC 2409196. PMID 16154999.

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