ACYP1
{{Short description|Protein-coding gene in the species Homo sapiens}}
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Acylphosphatase-1 is an enzyme that in humans is encoded by the ACYP1 gene.{{cite journal | vauthors = Fiaschi T, Raugei G, Marzocchini R, Chiarugi P, Cirri P, Ramponi G | title = Cloning and expression of the cDNA coding for the erythrocyte isoenzyme of human acylphosphatase | journal = FEBS Letters | volume = 367 | issue = 2 | pages = 145–8 | date = Jun 1995 | pmid = 7796909 | doi = 10.1016/0014-5793(95)00553-L | doi-access = | bibcode = 1995FEBSL.367..145F | s2cid = 43318853 }}{{cite journal | vauthors = Fiaschi T, Marzella R, Veggi D, Marzocchini R, Raugei G, Rocchi M, Ramponi G | title = Assignment of the human erythrocyte acylphosphatase gene (ACYP1) to chromosome band 14q24.3 | journal = Cytogenetics and Cell Genetics | volume = 81 | issue = 3–4 | pages = 235–6 | date = Oct 1998 | pmid = 9730610 | doi = 10.1159/000015037 | s2cid = 46797997 }}{{cite web | title = Entrez Gene: ACYP1 acylphosphatase 1, erythrocyte (common) type| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=97}}
Function
Acylphosphatase is a small cytosolic enzyme that catalyzes the hydrolysis of the carboxyl-phosphate bond of acylphosphates. Two isoenzymes have been isolated, called muscle acylphosphatase and erythrocyte acylphosphatase, on the basis of their tissue localization. This gene encodes the erythrocyte acylphosphatase isoenzyme. Alternatively spliced transcript variants that encode different proteins were identified through data analysis.
References
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External links
- {{UCSC gene info|ACYP1}}
Further reading
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- {{cite journal | vauthors = Nassi P, Nediani C, Liguri G, Taddei N, Ramponi G | title = Effects of acylphosphatase on the activity of erythrocyte membrane Ca2+ pump | journal = The Journal of Biological Chemistry | volume = 266 | issue = 17 | pages = 10867–71 | date = Jun 1991 | doi = 10.1016/S0021-9258(18)99099-X | pmid = 1645713 | doi-access = free }}
- {{cite journal | vauthors = Degl'Innocenti D, Berti A, Stefani M, Liguri G, Ramponi G | title = Immunoaffinity purification and immunoassay determination of human erythrocyte acylphosphatase | journal = Biotechnology and Applied Biochemistry | volume = 12 | issue = 4 | pages = 450–9 | date = Aug 1990 | doi = 10.1111/j.1470-8744.1990.tb00112.x | pmid = 2169259 | s2cid = 26999394 }}
- {{cite journal | vauthors = Liguri G, Camici G, Manao G, Cappugi G, Nassi P, Modesti A, Ramponi G | title = A new acylphosphatase isoenzyme from human erythrocytes: purification, characterization, and primary structure | journal = Biochemistry | volume = 25 | issue = 24 | pages = 8089–94 | date = Dec 1986 | pmid = 3026468 | doi = 10.1021/bi00372a044 }}
- {{cite journal | vauthors = Paoli P, Pazzagli L, Giannoni E, Caselli A, Manao G, Camici G, Ramponi G | title = A nucleophilic catalysis step is involved in the hydrolysis of aryl phosphate monoesters by human CT acylphosphatase | journal = The Journal of Biological Chemistry | volume = 278 | issue = 1 | pages = 194–9 | date = Jan 2003 | pmid = 12409302 | doi = 10.1074/jbc.M206918200 | url = https://flore.unifi.it/bitstream/2158/312459/1/paoli%202003.pdf | doi-access = free }}
- {{cite journal | vauthors = Degl'Innocenti D, Marzocchini R, Malentacchi F, Ramazzotti M, Raugei G, Ramponi G | title = ACYP1 gene possesses two alternative splicing forms that induce apoptosis | journal = IUBMB Life | volume = 56 | issue = 1 | pages = 29–33 | date = Jan 2004 | pmid = 14992377 | doi = 10.1080/15216540310001654349 | doi-access = free }}
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