Biology:ACYP2
From HandWiki
Short description: Protein-coding gene in the species Homo sapiens
Generic protein structure example |
Acylphosphatase-2 is an enzyme that in humans is encoded by the ACYP2 gene.[1][2]
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.[2]
References
- ↑ "Chemical synthesis and expression of a gene coding for human muscle acylphosphatase". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1216 (3): 369–74. Dec 1993. doi:10.1016/0167-4781(93)90003-v. PMID 8268218.
- ↑ 2.0 2.1 "Entrez Gene: ACYP2 acylphosphatase 2, muscle type". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=98.
External links
- Human ACYP2 genome location and ACYP2 gene details page in the UCSC Genome Browser.
Further reading
- "Glycine residues appear to be evolutionarily conserved for their ability to inhibit aggregation". Structure 13 (8): 1143–1151. Aug 2005. doi:10.1016/j.str.2005.04.022. PMID 16084386.
- "Reversal of protein aggregation provides evidence for multiple aggregated States". Journal of Molecular Biology 346 (2): 603–616. Feb 2005. doi:10.1016/j.jmb.2004.11.067. PMID 15670608.
- "A nucleophilic catalysis step is involved in the hydrolysis of aryl phosphate monoesters by human CT acylphosphatase". The Journal of Biological Chemistry 278 (1): 194–199. Jan 2003. doi:10.1074/jbc.M206918200. PMID 12409302. https://flore.unifi.it/bitstream/2158/312459/1/paoli%202003.pdf.
- "Kinetic partitioning of protein folding and aggregation". Nature Structural Biology 9 (2): 137–143. Feb 2002. doi:10.1038/nsb752. PMID 11799398.
- "Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding". Nature Structural Biology 6 (11): 1005–1009. Nov 1999. doi:10.1038/14890. PMID 10542090.
- "The 5'-untranslated region of the human muscle acylphosphatase mRNA has an inhibitory effect on protein expression". FEBS Letters 417 (1): 130–134. Nov 1997. doi:10.1016/S0014-5793(97)01270-2. PMID 9395090.
- "Differential migration of acylphosphatase isoenzymes from cytoplasm to nucleus during apoptotic cell death". Biochemical and Biophysical Research Communications 231 (3): 717–721. Feb 1997. doi:10.1006/bbrc.1997.6176. PMID 9070879.
- "Cloning and expression of the cDNA coding for the erythrocyte isoenzyme of human acylphosphatase". FEBS Letters 367 (2): 145–148. Jun 1995. doi:10.1016/0014-5793(95)00553-L. PMID 7796909.
- "Differential modulation of expression of the two acylphosphatase isoenzymes by thyroid hormone". The Biochemical Journal 311 (2): 567–73. Oct 1995. doi:10.1042/bj3110567. PMID 7487897.
- "Human skeletal muscle acylphosphatase: the primary structure". Molecular Biology & Medicine 2 (6): 369–78. Dec 1984. PMID 6100723.
- "A new acylphosphatase isoenzyme from human erythrocytes: purification, characterization, and primary structure". Biochemistry 25 (24): 8089–8094. Dec 1986. doi:10.1021/bi00372a044. PMID 3026468.
Original source: https://en.wikipedia.org/wiki/ACYP2.
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