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Family Report for: Acyl-CoA_Thioesterase


Block X
Acyl-CoA thioester hydrolase/bile acid-CoA amino acid N-acetyltransferase. Long chain acyl CoA thioesterases hydrolyze long chain acyl-CoAs to the corresponding free fatty acid and CoASH. The major solutes in bile are N-acyl conjugates of cholanoates (C24 bile acids) with glycine or taurine. These bile acid-amino acid conjugates serve as detergents in the gastrointestinal tract. Bile acid-amino acid conjugates are formed in the liver via a 2-step pathway. The first reaction converts a bile acid to an acyl-CoA thioester and is catalyzed by the microsomal enzyme, cholyl-CoA synthetase (EC The second reaction transfers the bile acid moiety from the acyl-CoA thioester to either glycine or taurine, and is catalyzed by bile acid-CoA:amino acid N-acyltransferase (BAAT; EC Some homologies to Dienelactone_hydrolase and AlphaBeta-hydrolases (PF08840 BAAT only C-term PIRSF019303) The mouse ACOT gene cluster comprises six genes with localizations in cytosol (ACOT1), mitochondria (ACOT2), and peroxisomes (ACOT3-6). The corresponding human gene cluster contains only three genes (ACOT1, ACOT2, and ACOT4) coding for full-length thioesterase proteins only ACOT4 is peroxisomal. Family TE2 in ThYme database
1 Disease(s)

IPR006862 (Acyl-CoA thioester hydrolase/bile acid-CoA amino acid N-acetyltransferase), IPR016662 (Structures: Acyl-CoA thioesterase, long chain)
PF04775 (Bile_Hydr_Trans Acyl-CoA thioester hydrolase/BAAT N-terminal region), PF08840 (BAAT_C BAAT / Acyl-CoA thioester hydrolase C terminal)

Peptide in
Nucleotide in
Alignment with Multalin
|Text only/graphic display
Seed alignment with MAFFT
|No colour/coloured with Mview
Alignment with MAFFT
|No colour/coloured with Mview
|Graphical display, obtained with the dnd file produced by Clustalw

4 more
    Title: 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
    Hunt MC, Rautanen A, Westin MA, Svensson LT, Alexson SE
    Ref: FASEB Journal, 20:1855, 2006 : PubMed


    Title: The peroxisome proliferator-induced cytosolic type I acyl-CoA thioesterase (CTE-I) is a serine-histidine-aspartic acid alpha/beta hydrolase
    Huhtinen K, O'Byrne J, Lindquist PJ, Contreras JA, Alexson SE
    Ref: Journal of Biological Chemistry, 277:3424, 2001 : PubMed


    Title: Identification of PTE2, a human peroxisomal long-chain acyl-CoA thioesterase.
    Jones JM, Gould SJ
    Ref: Biochemical & Biophysical Research Communications, 275:233, 2000 : PubMed


Other Papers

No structure scheme yet for this family

Structures in Acyl-CoA_Thioesterase family (2)

Genes Proteins in Acyl-CoA_Thioesterase family (55)

Fragments of genes in Acyl-CoA_Thioesterase family (7)

Substrates of some enzymes in the Acyl-CoA_Thioesterase family (2)

Inhibitors of some enzymes in the Acyl-CoA_Thioesterase family (1)

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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