LIPID MAPS® Gene/Proteome Database (LMPD)

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LMPD Record

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LMP000269

UniProt Annotations

Entry Information
Gene Nameacyl-CoA thioesterase 8
Protein EntryACOT8_MOUSE
UniProt IDP58137
SpeciesMouse
Comments
Comment typeDescription
Biophysicochemical PropertiesKinetic parameters: KM=29.4 uM for acetyl-CoA; KM=8.0 uM for propionyl-CoA; KM=22.6 uM for butyryl-CoA; KM=23.4 uM for hexanoyl-CoA; KM=6.9 uM for octanoyl-CoA; KM=2.9 uM for decanoyl-CoA; KM=2.5 uM for myristoyl-CoA; KM=1.7 uM for palmitoyl-CoA; KM=1.4 uM for palmitoleoyl-CoA; KM=1.6 uM for oleoyl-CoA; KM=4.2 uM for arachidoyl-CoA; KM=6.7 uM for arachidonoyl-CoA; KM=6.3 uM for trihydroxycoprostanoyl-CoA; KM=14.6 uM for choloyl-CoA; KM=8.8 uM for chenodeoxycholoyl-CoA; Note=In summary, KM for medium- to long-chain acyl CoAs is in the order 1.4-6.7 uM, and with short-chain acyl CoAs range from 8 to 30 uM. KM for bile acid-CoA esters is in the range 6-15 uM.;
Catalytic ActivityCholoyl-CoA + H(2)O = cholate + CoA.
Enzyme RegulationInhibited by CoASH (IC(50)= 10-15uM). Also inhibited by cysteine-reactive agents.
FunctionAcyl-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. Major thioesterase in peroxisomes. Competes with BAAT (Bile acid CoA: amino acid N-acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a preference for medium- length fatty acyl-CoAs. May be involved in the metabolic regulation of peroxisome proliferation.
InductionInduced in the liver, by peroxisome proliferator or fasting via the peroxisome proliferator-activated receptors (PPARs). Diurnal regulation of its expression.
MiscellaneousConstitutes about 1% of total peroxisomal protein.
SimilarityBelongs to the C/M/P thioester hydrolase family. {ECO:0000305}.
Subcellular LocationPeroxisome.
Tissue SpecificityUbiquitous.