Angiotensin-converting enzyme

Angiotensin I converting enzyme (peptidyl-dipeptidase A) 1
Rendering of ACE from PDB 1O86
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1O86, 1O8A, 1UZE, 1UZF, 2C6F, 2C6N, 2IUL, 2IUX, 2OC2, 2XY9, 2XYD, 2YDM, 3BKK, 3BKL, 3L3N, 3NXQ
Identifiers
Symbols	ACE; ACE1; CD143; DCP; DCP1; MVCD3
External IDs	OMIM: 106180 MGI: 87874 HomoloGene: 37351 ChEMBL: 1808 GeneCards: ACE Gene
EC number	3.4.15.1
Gene Ontology Molecular function • actin binding • endopeptidase activity • carboxypeptidase activity • protein binding • drug binding • peptidase activity • metallopeptidase activity • metallopeptidase activity • peptidyl-dipeptidase activity • peptidyl-dipeptidase activity • zinc ion binding • chloride ion binding • bradykinin receptor binding • peptide binding • metal ion binding Cellular component • extracellular region • extracellular space • membrane fraction • endosome • plasma membrane • external side of plasma membrane • integral to membrane Biological process • response to hypoxia • kidney development • blood vessel remodeling • angiotensin catabolic process in blood • regulation of renal output by angiotensin • neutrophil mediated immunity • regulation of systemic arterial blood pressure by renin-angiotensin • proteolysis • regulation of blood pressure • regulation of smooth muscle cell migration • regulation of vasoconstriction • sensory perception of pain • response to nutrient levels • response to lipopolysaccharide • mononuclear cell proliferation • regulation of vasodilation • hormone catabolic process • hormone catabolic process • eating behavior • positive regulation of apoptotic process • peptide catabolic process • arachidonic acid secretion • positive regulation of inflammatory response • positive regulation of neurogenesis • heart contraction • hemopoietic stem cell differentiation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	1636	11421
Ensembl	ENSG00000159640	ENSMUSG00000020681
UniProt	P12821	P09470
RefSeq (mRNA)	NM_000789.3	NM_009598.2
RefSeq (protein)	NP_000780.1	NP_033728.1
Location (UCSC)	Chr 17: 61.55 – 61.6 Mb	Chr 11: 105.83 – 105.85 Mb
PubMed search	[1]	[2]
This box: view talk edit

Angiotensin-converting enzyme (ACE, EC 3.4.15.1), an exopeptidase, is a circulating enzyme that participates in the body's renin-angiotensin system (RAS), which mediates extracellular volume (i.e. that of the blood plasma, lymph and interstitial fluid), and arterial vasoconstriction. It is secreted by pulmonary and renal endothelial cells and catalyzes the conversion of decapeptide angiotensin I to octapeptide angiotensin II.^[1]

Functions

Schematic diagram of the renin-angiotensin-aldosterone system

Anatomical diagram of the renin-angiotensin system, showing the role of ACE at the lungs.^[2]

It has two primary functions:

• ACE catalyses the conversion of angiotensin I to angiotensin II, a potent vasoconstrictor in a substrate concentration-dependent manner.^[3]
• ACE degrades bradykinin, a potent vasodilator, and other vasoactive peptides,^[4]

These two actions make ACE inhibition a goal in the treatment of conditions such as high blood pressure, heart failure, diabetic nephropathy, and type 2 diabetes mellitus. Inhibition of ACE (by ACE inhibitors) results in the decreased formation of angiotensin II and decreased metabolism of bradykinin, leading to systematic dilation of the arteries and veins and a decrease in arterial blood pressure. In addition, inhibiting angiotensin II formation diminishes angiotensin II-mediated aldosterone secretion from the adrenal cortex, leading to a decrease in water and sodium reabsorption and a reduction in extracellular volume.^[5]

Genetics and C and N domains function

The ACE gene, ACE, encodes two isozymes. The somatic isozyme is expressed in many tissues, mainly in the lung, including vascular endothelial cells, epithelial kidney cells, and testicular Leydig cells, whereas the germinal is expressed only in sperm. Brain tissue has ACE enzyme, which takes part in local RAAS and converts Aβ42 (which aggregates into plaques) to Aβ40 (which is thought to be less toxic) forms of beta amyloid. The latter is predominantly a function of N domain portion on the ACE enzyme. ACE inhibitors that cross the blood–brain barrier and have preferentially select N terminal activity may, therefore, cause accumulation of Aβ42 and progression of dementia.^{[citation needed]}

See also

• Renin-angiotensin system
• ACE inhibitors
• Hypotensive transfusion reaction
• Angiotensin-converting enzyme 2

References

Further reading

External links

• Proteopedia Angiotensin-converting_enzyme - the Angiotensin-Converting Enzyme Structure in Interactive 3D
• MeSH Angiotensin+Converting+Enzyme

v t e PDB gallery 1o86: CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN CONVERTING ENZYME IN COMPLEX WITH LISINOPRIL.   1o8a: CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN CONVERTING ENZYME (NATIVE).   1uze: COMPLEX OF THE ANTI-HYPERTENSIVE DRUG ENALAPRILAT AND THE HUMAN TESTICULAR ANGIOTENSIN I-CONVERTING ENZYME   1uzf: COMPLEX OF THE ANTI-HYPERTENSIVE DRUG CAPTOPRIL AN THE HUMAN TESTICULAR ANGIOTENSIN I-CONVERTING ENZYME   2c6f: STRUCTURE OF HUMAN SOMATIC ANGIONTENSIN-I CONVERTING ENZYME N DOMAIN   2c6n: STRUCTURE OF HUMAN SOMATIC ANGIONTENSIN-I CONVERTING ENZYME N DOMAIN WITH LISINOPRIL   2iul: HUMAN TACE G13 MUTANT   2iux: HUMAN TACE MUTANT G1234   2oc2: Structure of testis ACE with RXPA380