Acyl-CoA_Thioesterase

Relationship

Family: Acyl-CoA_Thioesterase

Block: X

Parent Family: No family

Comment

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. ACOTs are broadly divided into two distinct subgroups, the type-I alpha/beta-hydrolase fold enzyme superfamily and the type-II 'hot dog' fold superfamily. Here only a/b hydrolases. 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 6.2.1.7). 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 2.3.1.65). 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

Sequences

Peptide in Fasta
Nucleotide in Fasta
Alignment with Multalin Text only
Seed alignment with MAFFT No colour
Alignment with MAFFT No colour
Dendrogram The dnd file

Structures (2)

Genes Proteins in Acyl-CoA_Thioesterase family (55)

Fragments of genes in Acyl-CoA_Thioesterase family (7)

Structures in Acyl-CoA_Thioesterase family (2)

Substrates in Acyl-CoA_Thioesterase family (2)

Inhibitors in Acyl-CoA_Thioesterase family (1)

References (8)

Title : Progress of the acyl-Coenzyme A thioester hydrolase family in cancer - Bai_2024_Front.Oncol_14_1374094
Author(s) : Bai L , Yang P , Han B , Kong L
Ref : Front Oncol , 14 :1374094 , 2024
PubMedID: 38562172

Title : Thioesterase enzyme families: Functions, structures, and mechanisms - Caswell_2021_Protein.Sci__
Author(s) : Caswell BT , de Carvalho CC , Nguyen H , Roy M , Nguyen T , Cantu DC
Ref : Protein Science , : , 2021
PubMedID: 34921469

Title : ThYme: a database for thioester-active enzymes - Cantu_2011_Nucleic.Acids.Res_39_D342
Author(s) : Cantu DC , Chen Y , Lemons ML , Reilly PJ
Ref : Nucleic Acids Research , 39 :D342 , 2011
PubMedID: 21045059

Title : Thioesterases: a new perspective based on their primary and tertiary structures. - Cantu_2010_Protein.Sci_19_1281
Author(s) : Cantu DC , Chen Y , Reilly PJ
Ref : Protein Science , 19 :1281 , 2010
PubMedID: 20506386

Title : Crystal structure of human mitochondrial acyl-CoA thioesterase (ACOT2) - Mandel_2009_Biochem.Biophys.Res.Commun_385_630
Author(s) : Mandel CR , Tweel B , Tong L
Ref : Biochemical & Biophysical Research Communications , 385 :630 , 2009
PubMedID: 19497300
Gene_locus related to this paper: human-ACOT2

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_2006_FASEB.J_20_1855
Author(s) : Hunt MC , Rautanen A , Westin MA , Svensson LT , Alexson SE
Ref : FASEB Journal , 20 :1855 , 2006
PubMedID: 16940157
Gene_locus related to this paper: human-ACOT1 , human-ACOT2 , human-ACOT4 , human-ACOT6 , mouse-acot1 , mouse-acot2 , mouse-acot3 , mouse-acot4 , mouse-acot5 , mouse-ACOT6

Title : The peroxisome proliferator-induced cytosolic type I acyl-CoA thioesterase (CTE-I) is a serine-histidine-aspartic acid alpha\/beta hydrolase - Huhtinen_2001_J.Biol.Chem_277_3424
Author(s) : Huhtinen K , O'Byrne J , Lindquist PJ , Contreras JA , Alexson SE
Ref : Journal of Biological Chemistry , 277 :3424 , 2001
PubMedID: 11694534
Gene_locus related to this paper: mouse-acot1

Title : Identification of PTE2, a human peroxisomal long-chain acyl-CoA thioesterase. -
Author(s) : Jones JM , Gould SJ
Ref : Biochemical & Biophysical Research Communications , 275 :233 , 2000
PubMedID: 10944470
Gene_locus related to this paper: human-ACOT2