ACYP2
{{Short description|Protein-coding gene in the species Homo sapiens}}
{{Infobox_gene}}
Acylphosphatase-2 is an enzyme that in humans is encoded by the ACYP2 gene.{{cite journal | vauthors = Modesti A, Raugei G, Taddei N, Marzocchini R, Vecchi M, Camici G, Manao G, Ramponi G | title = Chemical synthesis and expression of a gene coding for human muscle acylphosphatase | journal = Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression | volume = 1216 | issue = 3 | pages = 369–74 | date = Dec 1993 | pmid = 8268218 | doi = 10.1016/0167-4781(93)90003-v }}{{cite web | title = Entrez Gene: ACYP2 acylphosphatase 2, muscle type| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=98}}
Function
Acylphosphatase can hydrolyze the phosphoenzyme intermediate of different membrane pumps, particularly the Ca2+/Mg2+-ATPase from sarcoplasmic reticulum of skeletal muscle. Two isoenzymes have been isolated, called muscle acylphosphatase and erythrocyte acylphosphatase on the basis of their tissue localization. This gene encodes the muscle-type isoform (MT). An increase of the MT isoform is associated with muscle differentiation.
References
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External links
- {{UCSC gene info|ACYP2}}
Further reading
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- {{cite journal | vauthors = Parrini C, Taddei N, Ramazzotti M, Degl'Innocenti D, Ramponi G, Dobson CM, Chiti F | title = Glycine residues appear to be evolutionarily conserved for their ability to inhibit aggregation | journal = Structure | volume = 13 | issue = 8 | pages = 1143–1151 | date = Aug 2005 | pmid = 16084386 | doi = 10.1016/j.str.2005.04.022 | doi-access = free }}
- {{cite journal | vauthors = Calamai M, Canale C, Relini A, Stefani M, Chiti F, Dobson CM | title = Reversal of protein aggregation provides evidence for multiple aggregated States | journal = Journal of Molecular Biology | volume = 346 | issue = 2 | pages = 603–616 | date = Feb 2005 | pmid = 15670608 | doi = 10.1016/j.jmb.2004.11.067 }}
- {{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 = 194–199 | date = Jan 2003 | pmid = 12409302 | doi = 10.1074/jbc.M206918200 | s2cid = 25162379 | url = https://flore.unifi.it/bitstream/2158/312459/1/paoli%202003.pdf | doi-access = free }}
- {{cite journal | vauthors = Chiti F, Taddei N, Baroni F, Capanni C, Stefani M, Ramponi G, Dobson CM | title = Kinetic partitioning of protein folding and aggregation | journal = Nature Structural Biology | volume = 9 | issue = 2 | pages = 137–143 | date = Feb 2002 | pmid = 11799398 | doi = 10.1038/nsb752 | s2cid = 22724295 }}
- {{cite journal | vauthors = Chiti F, Taddei N, White PM, Bucciantini M, Magherini F, Stefani M, Dobson CM | title = Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding | journal = Nature Structural Biology | volume = 6 | issue = 11 | pages = 1005–1009 | date = Nov 1999 | pmid = 10542090 | doi = 10.1038/14890 | s2cid = 3124119 }}
- {{cite journal | vauthors = Fiaschi T, Marzocchini R, Raugei G, Veggi D, Chiarugi P, Ramponi G | title = The 5'-untranslated region of the human muscle acylphosphatase mRNA has an inhibitory effect on protein expression | journal = FEBS Letters | volume = 417 | issue = 1 | pages = 130–134 | date = Nov 1997 | pmid = 9395090 | doi = 10.1016/S0014-5793(97)01270-2 | bibcode = 1997FEBSL.417..130F | s2cid = 23901221 }}
- {{cite journal | vauthors = Chiarugi P, Degl'Innocenti D, Raugei G, Fiaschi T, Ramponi G | title = Differential migration of acylphosphatase isoenzymes from cytoplasm to nucleus during apoptotic cell death | journal = Biochemical and Biophysical Research Communications | volume = 231 | issue = 3 | pages = 717–721 | date = Feb 1997 | pmid = 9070879 | doi = 10.1006/bbrc.1997.6176 }}
- {{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 = 145–148 | date = Jun 1995 | pmid = 7796909 | doi = 10.1016/0014-5793(95)00553-L | s2cid = 43318853 | doi-access = | bibcode = 1995FEBSL.367..145F }}
- {{cite journal | vauthors = Chiarugi P, Raugei G, Marzocchini R, Fiaschi T, Ciccarelli C, Berti A, Ramponi G | title = Differential modulation of expression of the two acylphosphatase isoenzymes by thyroid hormone | journal = The Biochemical Journal | volume = 311 | issue = 2 | pages = 567–73 | date = Oct 1995 | pmid = 7487897 | pmc = 1136037 | doi = 10.1042/bj3110567}}
- {{cite journal | vauthors = Manao G, Camici G, Modesti A, Liguri G, Berti A, Stefani M, Cappugi G, Ramponi G | title = Human skeletal muscle acylphosphatase: the primary structure | journal = Molecular Biology & Medicine | volume = 2 | issue = 6 | pages = 369–78 | date = Dec 1984 | pmid = 6100723 }}
- {{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 = 8089–8094 | date = Dec 1986 | pmid = 3026468 | doi = 10.1021/bi00372a044 }}
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{{PDB Gallery|geneid=98}}
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