Biology:ACOT8
From HandWiki
Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
Acyl-coenzyme A thioesterase 8 is an enzyme that in humans is encoded by the ACOT8 gene.[1][2][3][4][5]
The protein encoded by this gene is a peroxisomal thioesterase that appears to be involved more in the oxidation of fatty acids rather than in their formation. The encoded protein can bind to the human immunodeficiency virus-1 protein Nef, and mediate Nef-induced down-regulation of CD4 in T-cells. Multiple transcript variants encoding several different isoforms have been found for this gene.[5]
References
- ↑ "Identification of peroxisomal acyl-CoA thioesterases in yeast and humans". J Biol Chem 274 (14): 9216–23. Apr 1999. doi:10.1074/jbc.274.14.9216. PMID 10092594.
- ↑ "Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-mediated CD4 down-regulation". J Biol Chem 272 (21): 13779–85. Jul 1997. doi:10.1074/jbc.272.21.13779. PMID 9153233.
- ↑ "A revised nomenclature for mammalian acyl-CoA thioesterases/hydrolases". J Lipid Res 46 (9): 2029–32. Aug 2005. doi:10.1194/jlr.E500003-JLR200. PMID 16103133.
- ↑ "Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs". FASEB J 20 (11): 1855–64. Aug 2006. doi:10.1096/fj.06-6042com. PMID 16940157. https://arrow.dit.ie/scschbioart/11.
- ↑ 5.0 5.1 "Entrez Gene: ACOT8 acyl-CoA thioesterase 8". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10005.
Further reading
- "The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism". Prog. Lipid Res. 41 (2): 99–130. 2002. doi:10.1016/S0163-7827(01)00017-0. PMID 11755680.
- "A novel acyl-CoA thioesterase enhances its enzymatic activity by direct binding with HIV Nef". Biochem. Biophys. Res. Commun. 238 (1): 234–9. 1997. doi:10.1006/bbrc.1997.7217. PMID 9299485.
- "Mutation of a Conserved Residue (D123) Required for Oligomerization of Human Immunodeficiency Virus Type 1 Nef Protein Abolishes Interaction with Human Thioesterase and Results in Impairment of Nef Biological Functions". J. Virol. 74 (11): 5310–9. 2000. doi:10.1128/JVI.74.11.5310-5319.2000. PMID 10799608.
- "The human thioesterase II protein binds to a site on HIV-1 Nef critical for CD4 down-regulation". J. Biol. Chem. 275 (30): 23097–105. 2000. doi:10.1074/jbc.M000536200. PMID 10807905.
- "Identification of PTE2, a human peroxisomal long-chain acyl-CoA thioesterase". Biochem. Biophys. Res. Commun. 275 (1): 233–40. 2000. doi:10.1006/bbrc.2000.3285. PMID 10944470.
- "A high-resolution 6.0-megabase transcript map of the type 2 diabetes susceptibility region on human chromosome 20". Genomics 76 (1–3): 45–57. 2001. doi:10.1006/geno.2001.6584. PMID 11549316. https://cdr.lib.unc.edu/downloads/6w924p34v.
- "The DNA sequence and comparative analysis of human chromosome 20". Nature 414 (6866): 865–71. 2002. doi:10.1038/414865a. PMID 11780052. Bibcode: 2001Natur.414..865D.
- "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. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. 2004. doi:10.1038/ng1285. PMID 14702039.
- "Overexpression of human acyl-CoA thioesterase upregulates peroxisome biogenesis". Exp. Cell Res. 297 (1): 127–41. 2004. doi:10.1016/j.yexcr.2004.02.029. PMID 15194431.
- "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. 2004. doi:10.1101/gr.2596504. PMID 15489334.
- "The identification of a succinyl-CoA thioesterase suggests a novel pathway for succinate production in peroxisomes". J. Biol. Chem. 280 (46): 38125–32. 2006. doi:10.1074/jbc.M508479200. PMID 16141203.
- "Sterol Regulatory Element-Binding Protein-2 modulates human brain acyl-CoA hydrolase gene transcription". Mol. Cell. Biochem. 275 (1–2): 199–206. 2006. doi:10.1007/s11010-005-1990-y. PMID 16335799.
- "Nafamostat is hydrolysed by human liver cytosolic long-chain acyl-CoA hydrolase". Xenobiotica 37 (3): 260–70. 2007. doi:10.1080/00498250601167091. PMID 17624024.
External links
- ACOT8 human gene location in the UCSC Genome Browser.
- ACOT8 human gene details in the UCSC Genome Browser.
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