Angiotensin-converting enzyme 2

From Wikipedia, the free encyclopedia

Angiotensin I converting enzyme (peptidyl-dipeptidase A) 2

PDB rendering based on 1r42.

Available structures: 1r42, 1r4l, 2ajf

Identifiers

Symbol(s)

ACE2; ACEH; DKFZP434A014

External IDs

OMIM: 300335 MGI: 1917258 HomoloGene: 41448

Gene ontology
Molecular Function:	• viral receptor activity • carboxypeptidase activity • peptidyl-dipeptidase A activity • protein binding • zinc ion binding • chloride ion binding • metal ion binding
Cellular Component:	• extracellular region • membrane • integral to membrane
Biological Process:	• proteolysis • entry of virus into host cell

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_021804 (mRNA)
NP_068576 (protein)

NM_027286 (mRNA)
NP_081562 (protein)

Location

Chr X: 15.49 - 15.53 Mb

Chr X: 159.48 - 159.53 Mb

Pubmed search

[1]

[2]

Angiotensin I converting enzyme 2 (ACE2) is an exopeptidase that catalyses the conversion of angiotensin I to the nonapeptide angiotensin[1-9].^[1] ACE 2 has direct effects on cardiac function^[2], and is expressed predominantly in vascular endothelial cells of the heart and the kidneys.^[2]

[edit] See also

[edit] References

^ Donoghue M, Hsieh F, Baronas E, Godbout K, Gosselin M, Stagliano N, Donovan M, Woolf B, Robison K, Jeyaseelan R, Breitbart RE, Acton S (2000). "A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9". Circ. Res. 87 (5): E1–9. PMID 10969042.
^ Boehm M, Nabel EG (2002). "Angiotensin-converting enzyme 2--a new cardiac regulator". N. Engl. J. Med. 347 (22): 1795–7. doi:10.1056/NEJMcibr022472. PMID 12456857.

[edit] Further reading

Turner AJ, Tipnis SR, Guy JL, et al. (2002). "ACEH/ACE2 is a novel mammalian metallocarboxypeptidase and a homologue of angiotensin-converting enzyme insensitive to ACE inhibitors.". Can. J. Physiol. Pharmacol. 80 (4): 346–53. PMID 12025971.
Turner AJ, Hiscox JA, Hooper NM (2004). "ACE2: from vasopeptidase to SARS virus receptor.". Trends Pharmacol. Sci. 25 (6): 291–4. doi:10.1016/j.tips.2004.04.001. PMID 15165741.
Katovich MJ, Grobe JL, Huentelman M, Raizada MK (2005). "Angiotensin-converting enzyme 2 as a novel target for gene therapy for hypertension.". Exp. Physiol. 90 (3): 299–305. doi:10.1113/expphysiol.2004.028522. PMID 15640278.
Ferrario CM, Trask AJ, Jessup JA (2006). "Advances in biochemical and functional roles of angiotensin-converting enzyme 2 and angiotensin-(1-7) in regulation of cardiovascular function.". Am. J. Physiol. Heart Circ. Physiol. 289 (6): H2281–90. doi:10.1152/ajpheart.00618.2005. PMID 16055515.
Jia HP, Look DC, Hickey M, et al. (2006). "Infection of human airway epithelia by SARS coronavirus is associated with ACE2 expression and localization.". Adv. Exp. Med. Biol. 581: 479–84. PMID 17037581.
Lazartigues E, Feng Y, Lavoie JL (2007). "The two fACEs of the tissue renin-angiotensin systems: implication in cardiovascular diseases.". Curr. Pharm. Des. 13 (12): 1231–45. PMID 17504232.
Raizada MK, Ferreira AJ (2007). "ACE2: a new target for cardiovascular disease therapeutics.". J. Cardiovasc. Pharmacol. 50 (2): 112–9. doi:10.1097/FJC.0b013e3180986219. PMID 17703127.
Dean RG, Burrell LM (2007). "ACE2 and diabetic complications.". Curr. Pharm. Des. 13 (26): 2730–5. PMID 17897017.
Tipnis SR, Hooper NM, Hyde R, et al. (2000). "A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase.". J. Biol. Chem. 275 (43): 33238–43. doi:10.1074/jbc.M002615200. PMID 10924499.
Donoghue M, Hsieh F, Baronas E, et al. (2000). "A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9.". Circ. Res. 87 (5): E1–9. PMID 10969042.
Vickers C, Hales P, Kaushik V, et al. (2002). "Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase.". J. Biol. Chem. 277 (17): 14838–43. doi:10.1074/jbc.M200581200. PMID 11815627.
Crackower MA, Sarao R, Oudit GY, et al. (2002). "Angiotensin-converting enzyme 2 is an essential regulator of heart function.". Nature 417 (6891): 822–8. doi:10.1038/nature00786. PMID 12075344.
Harmer D, Gilbert M, Borman R, Clark KL (2003). "Quantitative mRNA expression profiling of ACE 2, a novel homologue of angiotensin converting enzyme.". FEBS Lett. 532 (1-2): 107–10. PMID 12459472.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Donoghue M, Wakimoto H, Maguire CT, et al. (2004). "Heart block, ventricular tachycardia, and sudden death in ACE2 transgenic mice with downregulated connexins.". J. Mol. Cell. Cardiol. 35 (9): 1043–53. PMID 12967627.
Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMID 12975309.
Li W, Moore MJ, Vasilieva N, et al. (2003). "Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus.". Nature 426 (6965): 450–4. doi:10.1038/nature02145. PMID 14647384.
Wong SK, Li W, Moore MJ, et al. (2004). "A 193-amino acid fragment of the SARS coronavirus S protein efficiently binds angiotensin-converting enzyme 2.". J. Biol. Chem. 279 (5): 3197–201. doi:10.1074/jbc.C300520200. PMID 14670965.
Towler P, Staker B, Prasad SG, et al. (2004). "ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis.". J. Biol. Chem. 279 (17): 17996–8007. doi:10.1074/jbc.M311191200. PMID 14754895.