Detail Information for IndEnz0010000047
IED ID IndEnz0010000047
Enzyme Type ID esterase000047
Protein Name Acyl-coenzyme A thioesterase 1
Acyl-CoA thioesterase 1
EC 3.1.2.-
CTE-I
Inducible cytosolic acyl-coenzyme A thioester hydrolase
Long chain acyl-CoA thioester hydrolase
Long chain acyl-CoA hydrolase
Palmitoyl-coenzyme A thioesterase
EC 3.1.2.2
Gene Name Acot1 Cte1
Organism Mus musculus (Mouse)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MEATLNLEPSGRSCWDEPLSIAVRGLAPEQPVTLRSVLRDEKGALFRAHARYRADSHGELDLARTPALGGSFSGLEPMGLLWAMEPDRPFWRLVKRDVQTPFVVELEVLDGHEPDGGQRLAHAVHERHFLAPGVRRVPVREGRVRATLFLPPEPGPFPGIIDLFGVGGGLLEYRASLLAGKGFAVMALAYYNYDDLPKNMETMHMEYFEEAVNYLRSHPEVKGPGIGLLGISKGGELGLAMASFLKGITAAVVINGSVAAVGNTISYKDETIPPVTILRNQVKMTKDGLKDVVDALQSPLVDKKSFIPVERSDTTFLFLVGQDDHNWKSEFYADEISKRLQAHGKEKPQIICYPAAGHYIEPPYFPLCSAGMHLLVGANITFGGEPKPHAMAQLDAWQQLQTFFHKQLGSECLHVSPKI
Enzyme Length 419
Uniprot Accession Number O55137
Absorption
Active Site ACT_SITE 232; /note=Charge relay system; /evidence=ECO:0000269|PubMed:11694534; ACT_SITE 324; /note=Charge relay system; /evidence=ECO:0000269|PubMed:11694534; ACT_SITE 358; /note=Charge relay system; /evidence=ECO:0000269|PubMed:11694534
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate; Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2; Evidence={ECO:0000269|PubMed:11694534};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; Evidence={ECO:0000305|PubMed:11694534}; CATALYTIC ACTIVITY: Reaction=decanoyl-CoA + H2O = CoA + decanoate + H(+); Xref=Rhea:RHEA:40059, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430; Evidence={ECO:0000269|PubMed:11694534};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060; Evidence={ECO:0000305|PubMed:11694534}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+); Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375; Evidence={ECO:0000269|PubMed:11694534};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136; Evidence={ECO:0000305|PubMed:11694534}; CATALYTIC ACTIVITY: Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate; Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385; Evidence={ECO:0000269|PubMed:11694534};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120; Evidence={ECO:0000305|PubMed:11694534}; CATALYTIC ACTIVITY: Reaction=H2O + octadecanoyl-CoA = CoA + H(+) + octadecanoate; Xref=Rhea:RHEA:30139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394; Evidence={ECO:0000269|PubMed:11694534};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140; Evidence={ECO:0000305|PubMed:11694534}; CATALYTIC ACTIVITY: Reaction=eicosanoyl-CoA + H2O = CoA + eicosanoate + H(+); Xref=Rhea:RHEA:40147, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32360, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380; Evidence={ECO:0000269|PubMed:11694534};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40148; Evidence={ECO:0000305|PubMed:11694534}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + H2O = (9Z)-octadecenoate + CoA + H(+); Xref=Rhea:RHEA:40139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387; Evidence={ECO:0000269|PubMed:11694534};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140; Evidence={ECO:0000305|PubMed:11694534}; CATALYTIC ACTIVITY: Reaction=(9Z)-hexadecenoyl-CoA + H2O = (9Z)-hexadecenoate + CoA + H(+); Xref=Rhea:RHEA:40131, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32372, ChEBI:CHEBI:57287, ChEBI:CHEBI:61540; Evidence={ECO:0000269|PubMed:11694534};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40132; Evidence={ECO:0000305|PubMed:11694534}; CATALYTIC ACTIVITY: Reaction=(9E)-octadecenoyl-CoA + H2O = (9E)-octadecenoate + CoA + H(+); Xref=Rhea:RHEA:40723, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30825, ChEBI:CHEBI:57287, ChEBI:CHEBI:77537; Evidence={ECO:0000269|PubMed:11694534};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40724; Evidence={ECO:0000305|PubMed:11694534};
DNA Binding
EC Number 3.1.2.-; 3.1.2.2
Enzyme Function FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels. More active towards saturated and unsaturated long chain fatty acyl-CoAs (C12-C20). {ECO:0000269|PubMed:11694534}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305|PubMed:11694534}.
nucleotide Binding
Features Active site (3); Chain (1); Modified residue (1); Mutagenesis (4)
Keywords Cytoplasm;Fatty acid metabolism;Hydrolase;Lipid metabolism;Phosphoprotein;Reference proteome;Serine esterase
Interact With
Induction INDUCTION: In the liver, by peroxisome proliferator (Clofibrate) treatment, via the peroxisome proliferator-activated receptors (PPARs) or fasting for 24 hours. {ECO:0000269|PubMed:11330065}.
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O88267}.
Modified Residue MOD_RES 416; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:O88267
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 12149437; 12466851; 14681479; 16103133; 16940157; 17485727; 18614015; 18725516; 21267068; 22967998; 23226270; 25209997; 26518651; 27694478; 28364022; 8288233; 8631881; 8798769; 8827514;
Motif
Gene Encoded By
Mass 46,136
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.6 uM for C16:0-acyl-CoA {ECO:0000269|PubMed:11694534}; KM=15.2 uM for C10:0-acyl-CoA {ECO:0000269|PubMed:11694534}; KM=2.6 uM for C12:0-acyl-CoA {ECO:0000269|PubMed:11694534}; KM=3.5 uM for C14:0-acyl-CoA {ECO:0000269|PubMed:11694534}; KM=0.5 uM for C20:0-acyl-CoA {ECO:0000269|PubMed:11694534}; KM=1.5 uM for C14:1-acyl-CoA {ECO:0000269|PubMed:11694534}; KM=1.1 uM for C16:1-acyl-CoA {ECO:0000269|PubMed:11694534}; KM=2.4 uM for C18:1(cis)-acyl-CoA {ECO:0000269|PubMed:11694534}; KM=1.8 uM for C18:1(trans)-acyl-CoA {ECO:0000269|PubMed:11694534}; KM=4.5 uM for C18:2-acyl-CoA {ECO:0000269|PubMed:11694534}; KM=3.0 uM for C20:4-acyl-CoA {ECO:0000269|PubMed:11694534}; Vmax=1.2 umol/min/mg enzyme with C16:0-acyl-CoA as substrate {ECO:0000269|PubMed:11694534}; Vmax=0.192 umol/min/mg enzyme with C10:0-acyl-CoA as substrate {ECO:0000269|PubMed:11694534}; Vmax=0.780 umol/min/mg enzyme with C12:0-acyl-CoA as substrate {ECO:0000269|PubMed:11694534}; Vmax=1.68 umol/min/mg enzyme with C14:0-acyl-CoA as substrate {ECO:0000269|PubMed:11694534}; Vmax=0.692 umol/min/mg enzyme with C18:0-acyl-CoA as substrate {ECO:0000269|PubMed:11694534}; Vmax=0.245 umol/min/mg enzyme with C20:0-acyl-CoA as substrate {ECO:0000269|PubMed:11694534}; Vmax=0.745 umol/min/mg enzyme with C14:1-acyl-CoA as substrate {ECO:0000269|PubMed:11694534}; Vmax=0.621 umol/min/mg enzyme with C16:1-acyl-CoA as substrate {ECO:0000269|PubMed:11694534}; Vmax=0.176 umol/min/mg enzyme with C18:1(cis)-acyl-CoA as substrate {ECO:0000269|PubMed:11694534}; Vmax=0.188 umol/min/mg enzyme with C18:1(trans)-acyl-CoA as substrate {ECO:0000269|PubMed:11694534}; Vmax=0.316 umol/min/mg enzyme with C18:2-acyl-CoA as substrate {ECO:0000269|PubMed:11694534}; Vmax=0.007 umol/min/mg enzyme with C20:4-acyl-CoA as substrate {ECO:0000269|PubMed:11694534};
Metal Binding
Rhea ID RHEA:16645; RHEA:16646; RHEA:40059; RHEA:40060; RHEA:30135; RHEA:30136; RHEA:40119; RHEA:40120; RHEA:30139; RHEA:30140; RHEA:40147; RHEA:40148; RHEA:40139; RHEA:40140; RHEA:40131; RHEA:40132; RHEA:40723; RHEA:40724
Cross Reference Brenda 3.1.2.2;