Acot8 (基因名), Acyl-coenzyme A thioesterase 8 (蛋白名), ACOT8_RAT.
Rat Acot8/ Acyl-coenzyme A thioesterase 8 ELISA Kit
Acyl-CoA thioesterase 8, Choloyl-coenzyme A thioesterase, Pte1, Peroxisomal acyl-coenzyme A thioester hydrolase 1, PTE-1, Peroxisomal long-chain acyl-CoA thioesterase 1
Natural and recombinant rat Acyl-coenzyme A thioesterase 8
Serum, plasma, tissue homogenates, cell culture supernates and other biological fluids
Acyl-coenzyme A (acyl-CoA) thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH (PubMed:11785945). Acyl-coenzyme A thioesterase 8/ACOT8 display no strong substrate specificity with respect to the carboxylic acid moiety of Acyl-CoAs. Hydrolyzes medium length (C2 to C20) straight-chain, saturated and unsaturated acyl-CoAS but is inactive towards substrates with longer aliphatic chains (PubMed:11785945). Moreover, it catalyzes the hydrolysis of CoA esters of bile acids, such as choloyl-CoA and chenodeoxycholoyl-CoA and competes with bile acid CoA:amino acid N-acyltransferase (BAAT). ACOT8 is also able to hydrolyze CoA esters of dicarboxylic acids (By similarity). It is involved in the metabolic regulation of peroxisome proliferation (By similarity).
Peroxisome matrix Predominantly localized in the peroxisome but a localization to the cytosol cannot be excluded.
MSKPEDLGDA | NGDADRGDLS | GDLRSVLVTS | VLNLEPLDED | LYRGRHYWVP |
TSQRLFGGQI | VGQALVAAA | KSVSEDVHVH | SLHCYFVRAG | DPKVPVLYHV |
ERTRTGASFS | VRAVKAVQHG | K AIFICQAS | FQQMQPSPLQ | HQFSMPTVPP |
PEELLDHEAL | IDQYLRDPNL | HEKYRVGLNR | IA AREVPIE | IKLVNPPALN |
QLQTLEPKQM | FWVRARGYIG | EGDIKMHCCV | AAYISDYAFL | GTA LLPHQS |
KYKVNFMVSL | DHSMWFHAPF | RADHWMLYEC | ESPWAGGSRG | LVHGRLWRRD |
GVLA VTCAQ | EGVIRSKPRV | SESKL
"Identification of peroxisomal acyl-CoA thioesterases in yeast and humans."
"Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-mediated CD4 down-regulation."
"A novel acyl-CoA thioesterase enhances its enzymatic activity by direct binding with HIV Nef."
"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."
"A revised nomenclature for mammalian acyl-CoA thioesterases/hydrolases."
"The identification of a succinyl-CoA thioesterase suggests a novel pathway for succinate production in peroxisomes."
"Overexpression of human acyl-CoA thioesterase upregulates peroxisome biogenesis."
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
"The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism."
"The DNA sequence and comparative analysis of human chromosome 20."
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