Angiotensin-converting enzyme: Difference between revisions
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|caption=Angiotensin I converting enzyme {{PDB|}} |
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| update_protein_box = yes |
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|Symbol=ACE |
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| update_summary = no |
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|AltSymbols=CD143, CD143 |
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| update_citations = yes |
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|HGNCid=2707 |
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|Chromosome=17 |
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|Arm=q |
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|Band=23 |
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|LocusSupplementaryData= |
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|EntrezGene=1636 |
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| PDB = {{PDB2|1o86}}, {{PDB2|1o8a}}, {{PDB2|1uze}}, {{PDB2|1uzf}}, {{PDB2|2c6f}}, {{PDB2|2c6n}}, {{PDB2|2iul}}, {{PDB2|2iux}}, {{PDB2|2oc2}} |
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| HGNCid = 2707 |
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| Symbol = ACE |
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| AltSymbols =; ACE1; CD143; DCP; DCP1; MGC26566 |
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| Homologene = 37351 |
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| MGIid = 87874 |
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| GeneAtlas_image1 = PBB_GE_ACE_209749_s_at_tn.png |
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| DateOfBotUpdate = 20:38, 4 October 2007 (UTC) |
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| Function = {{GNF_GO|id=GO:0004180 |text = carboxypeptidase activity}} {{GNF_GO|id=GO:0004246 |text = peptidyl-dipeptidase A activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016798 |text = hydrolase activity, acting on glycosyl bonds}} {{GNF_GO|id=GO:0031404 |text = chloride ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} |
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| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} |
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| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0008217 |text = blood pressure regulation}} |
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| Orthologs = {{GNF_Ortholog_box |
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| Hs_EntrezGene = 1636 |
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| Hs_Ensembl = ENSG00000159640 |
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| Hs_RefseqProtein = NP_000780 |
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| Hs_GenLoc_db = |
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| Hs_GenLoc_chr = 17 |
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| Hs_GenLoc_start = 58908166 |
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| Hs_GenLoc_end = 58938721 |
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| Mm_EntrezGene = 11421 |
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| Mm_Ensembl = ENSMUSG00000020681 |
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| Mm_RefseqmRNA = NM_009598 |
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| Mm_RefseqProtein = NP_033728 |
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| Mm_GenLoc_db = |
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| Mm_GenLoc_chr = 11 |
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| Mm_GenLoc_start = 105784052 |
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| Mm_GenLoc_end = 105805352 |
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| Mm_Uniprot = Q3TU20 |
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}} |
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'''Angiotensin I converting enzyme''' ('''ACE''', {{EC number|3.4.15.1}}) is an [[exopeptidase]]. |
'''Angiotensin I converting enzyme''' ('''ACE''', {{EC number|3.4.15.1}}) is an [[exopeptidase]]. |
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==References== |
==References== |
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{{reflist}} |
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<references/> |
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==Further reading== |
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{{refbegin | 2}} |
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{{PBB_Further_reading |
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| citations = |
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*{{cite journal | author=Niu T, Chen X, Xu X |title=Angiotensin converting enzyme gene insertion/deletion polymorphism and cardiovascular disease: therapeutic implications. |journal=Drugs |volume=62 |issue= 7 |pages= 977-93 |year= 2002 |pmid= 11985486 |doi= }} |
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*{{cite journal | author=Roĭtberg GE, Tikhonravov AV, Dorosh ZhV |title=[Role of angiotensin-converting enzyme gene polymorphism in the development of metabolic syndrome] |journal=Ter. Arkh. |volume=75 |issue= 12 |pages= 72-7 |year= 2004 |pmid= 14959477 |doi= }} |
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*{{cite journal | author=Vynohradova SV |title=[The role of angiotensin-converting enzyme gene I/D polymorphism in development of metabolic disorders in patients with cardiovascular pathology] |journal=Tsitol. Genet. |volume=39 |issue= 1 |pages= 63-70 |year= 2005 |pmid= 16018179 |doi= }} |
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*{{cite journal | author=König S, Luger TA, Scholzen TE |title=Monitoring neuropeptide-specific proteases: processing of the proopiomelanocortin peptides adrenocorticotropin and alpha-melanocyte-stimulating hormone in the skin. |journal=Exp. Dermatol. |volume=15 |issue= 10 |pages= 751-61 |year= 2006 |pmid= 16984256 |doi= 10.1111/j.1600-0625.2006.00472.x }} |
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*{{cite journal | author=Sabbagh AS, Otrock ZK, Mahfoud ZR, ''et al.'' |title=Angiotensin-converting enzyme gene polymorphism and allele frequencies in the Lebanese population: prevalence and review of the literature. |journal=Mol. Biol. Rep. |volume=34 |issue= 1 |pages= 47-52 |year= 2007 |pmid= 17103020 |doi= 10.1007/s11033-006-9013-y }} |
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*{{cite journal | author=Castellon R, Hamdi HK |title=Demystifying the ACE polymorphism: from genetics to biology. |journal=Curr. Pharm. Des. |volume=13 |issue= 12 |pages= 1191-8 |year= 2007 |pmid= 17504229 |doi= }} |
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*{{cite journal | author=Lazartigues E, Feng Y, Lavoie JL |title=The two fACEs of the tissue renin-angiotensin systems: implication in cardiovascular diseases. |journal=Curr. Pharm. Des. |volume=13 |issue= 12 |pages= 1231-45 |year= 2007 |pmid= 17504232 |doi= }} |
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}} |
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{{refend}} |
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==External links== |
==External links== |
Revision as of 20:38, 4 October 2007
Angiotensin I converting enzyme (ACE, EC 3.4.15.1) is an exopeptidase.
Functions
It has two primary functions:
- it catalyses the conversion of angiotensin I to angiotensin II, a potent vasoconstrictor. [5]
- it is involved in the inactivation of bradykinin, a potent vasodilator.
These two actions of ACE make it an ideal target 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 decreased formation of Angiotensin II (a far more potent vasoconstrictor than Angiotensin I) and decreased inactivation of bradykinin.
Synonyms
ACE is also known as:
- peptidyl dipeptidase A
- carboxycathepsin
- kininase II (kinin-kallikrein system)
- CD 143
- ACE1
Genetics
The ACE gene, ACE, encodes 2 isozymes. The somatic isozyme is expressed in many tissues, including vascular endothelial cells, epithelial kidney cells, and testicular Leydig cells, whereas the germinal is expressed only in sperm.
See also
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000159640 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020681 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Template:GeorgiaPhysiology
Further reading
External links
- Angiotensin+Converting+Enzyme at the U.S. National Library of Medicine Medical Subject Headings (MeSH)