The protein encoded by this gene is a peroxisomalthioesterase 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 immunodeficiencyvirus-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
↑Jones JM, Nau K, Geraghty MT, Erdmann R, Gould SJ (Apr 1999). "Identification of peroxisomal acyl-CoA thioesterases in yeast and humans". J Biol Chem. 274 (14): 9216–23. doi:10.1074/jbc.274.14.9216. PMID10092594.
↑Liu LX, Margottin F, Le Gall S, Schwartz O, Selig L, Benarous R, Benichou S (Jul 1997). "Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-mediated CD4 down-regulation". J Biol Chem. 272 (21): 13779–85. doi:10.1074/jbc.272.21.13779. PMID9153233.
↑Hunt MC, Yamada J, Maltais LJ, Wright MW, Podesta EJ, Alexson SE (Aug 2005). "A revised nomenclature for mammalian acyl-CoA thioesterases/hydrolases". J Lipid Res. 46 (9): 2029–32. doi:10.1194/jlr.E500003-JLR200. PMID16103133.
↑Hunt MC, Rautanen A, Westin MA, Svensson LT, Alexson SE (Aug 2006). "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. doi:10.1096/fj.06-6042com. PMID16940157.
Hunt MC, Alexson SE (2002). "The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism". Prog. Lipid Res. 41 (2): 99–130. doi:10.1016/S0163-7827(01)00017-0. PMID11755680.
Watanabe H, Shiratori T, Shoji H, et al. (1997). "A novel acyl-CoA thioesterase enhances its enzymatic activity by direct binding with HIV Nef". Biochem. Biophys. Res. Commun. 238 (1): 234–9. doi:10.1006/bbrc.1997.7217. PMID9299485.
Cohen GB, Rangan VS, Chen BK, et al. (2000). "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. doi:10.1074/jbc.M000536200. PMID10807905.
Jones JM, Gould SJ (2000). "Identification of PTE2, a human peroxisomal long-chain acyl-CoA thioesterase". Biochem. Biophys. Res. Commun. 275 (1): 233–40. doi:10.1006/bbrc.2000.3285. PMID10944470.
Fossey SC, Mychaleckyj JC, Pendleton JK, et al. (2001). "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. doi:10.1006/geno.2001.6584. PMID11549316.
Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20". Nature. 414 (6866): 865–71. doi:10.1038/414865a. PMID11780052.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID14702039.
Ishizuka M, Toyama Y, Watanabe H, et al. (2004). "Overexpression of human acyl-CoA thioesterase upregulates peroxisome biogenesis". Exp. Cell Res. 297 (1): 127–41. doi:10.1016/j.yexcr.2004.02.029. PMID15194431.
Westin MA, Hunt MC, Alexson SE (2006). "The identification of a succinyl-CoA thioesterase suggests a novel pathway for succinate production in peroxisomes". J. Biol. Chem. 280 (46): 38125–32. doi:10.1074/jbc.M508479200. PMID16141203.
Takagi M, Suto F, Suga T, Yamada J (2006). "Sterol Regulatory Element-Binding Protein-2 modulates human brain acyl-CoA hydrolase gene transcription". Mol. Cell. Biochem. 275 (1–2): 199–206. doi:10.1007/s11010-005-1990-y. PMID16335799.
Yamaori S, Ukena E, Fujiyama N, et al. (2007). "Nafamostat is hydrolysed by human liver cytosolic long-chain acyl-CoA hydrolase". Xenobiotica. 37 (3): 260–70. doi:10.1080/00498250601167091. PMID17624024.