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; |