| IED ID | IndEnz0010000048 |
| Enzyme Type ID | esterase000048 |
| Protein Name |
Acyl-coenzyme A thioesterase 2, mitochondrial Acyl-CoA thioesterase 2 EC 3.1.2.2 ARTISt/p43 Acyl coenzyme A thioester hydrolase MTE-I Very-long-chain acyl-CoA thioesterase |
| Gene Name | Acot2 Mte1 |
| Organism | Rattus norvegicus (Rat) |
| 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 Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MVASSFAVLRASRLCQWGWKSWTQLSGPPPLSTGGRTTFARTNATLSLEPGSRSCWDEPLSITVRGLAPEQPVTLRAALRDEKGALFRAHARYRADAGGELDLARAPALGGSFTGLEPMGLIWAMEPERPLWRLVKRDVQKPYVVELEVLDGHEPDGGQRLAQAVHERHFMAPGVRRVPVRDGRVRATLFLPPEPGPFPEIIDLFGVGGGLLEYRASLLAGKGFAVMALAYYNYDDLPKTMETMRIEYFEEAVNYLRGHPEVKGPGIGLLGISKGGELGLAMASFLKGITAAVVINGSVAAVGNTVCYKDETIPPVSLLRDKVKMTKDGLLDVVEALQSPLVDKKSFIPVERSDTTFLFLVGQDDHNWKSEFYAREASKRLQAHGKEKPQIICYPEAGHYIEPPYFPLCSAGMHLLVGANITFGGEPKPHSVAQLDAWQQLQTFFHKQLSGKS |
| Enzyme Length | 453 |
| Uniprot Accession Number | O55171 |
| Absorption | |
| Active Site | ACT_SITE 273; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P49753; ACT_SITE 365; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P49753; ACT_SITE 399; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P49753 |
| 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:7744868};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; Evidence={ECO:0000305|PubMed:7744868}; 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:7744868};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120; Evidence={ECO:0000305|PubMed:7744868}; 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:7744868};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140; Evidence={ECO:0000305|PubMed:7744868}; 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:7744868};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40148; Evidence={ECO:0000305|PubMed:7744868}; 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:7744868};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060; Evidence={ECO:0000305|PubMed:7744868}; 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:7744868};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136; Evidence={ECO:0000305|PubMed:7744868}; 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:0000250|UniProtKB:P49753};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140; Evidence={ECO:0000250|UniProtKB:P49753}; 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:0000250|UniProtKB:P49753};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40132; Evidence={ECO:0000250|UniProtKB:P49753}; 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:0000250|UniProtKB:P49753};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40724; Evidence={ECO:0000250|UniProtKB:P49753}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoyl-CoA + H2O = (9Z,12Z)-octadecadienoate + CoA + H(+); Xref=Rhea:RHEA:40143, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383; Evidence={ECO:0000250|UniProtKB:Q9QYR9};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40144; Evidence={ECO:0000250|UniProtKB:Q9QYR9}; |
| DNA Binding | |
| EC Number | 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 (By similarity). Displays higher activity toward long chain acyl CoAs (C14-C20) (PubMed:7744868). The enzyme is involved in enhancing the hepatic fatty acid oxidation in mitochondria (By similarity). {ECO:0000250|UniProtKB:Q9QYR9, ECO:0000269|PubMed:7744868}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8-9. {ECO:0000269|PubMed:7744868}; |
| Pathway | PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305|PubMed:7744868}. |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Modified residue (2); Sequence conflict (3); Transit peptide (1) |
| Keywords | Acetylation;Direct protein sequencing;Fatty acid metabolism;Hydrolase;Lipid metabolism;Mitochondrion;Reference proteome;Serine esterase;Transit peptide |
| Interact With | |
| Induction | INDUCTION: Regulated by peroxisome proliferator, via the peroxisome proliferator-activated receptors (PPARs). {ECO:0000269|PubMed:7744868}. |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:7744868}. |
| Modified Residue | MOD_RES 83; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q9QYR9; MOD_RES 447; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:Q9QYR9 |
| Post Translational Modification | PTM: The N-terminus is blocked. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12692085; 15292030; 16979414; 17438340; 18388199; 21094633; |
| Motif | |
| Gene Encoded By | |
| Mass | 49,701 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=16 uM for C10-acyl-CoA {ECO:0000269|PubMed:7744868}; KM=5 uM for C12-acyl-CoA {ECO:0000269|PubMed:7744868}; KM=3 uM for C14-acyl-CoA {ECO:0000269|PubMed:7744868}; KM=6 uM for C16-acyl-CoA {ECO:0000269|PubMed:7744868}; KM=3 uM for C18-acyl-CoA {ECO:0000269|PubMed:7744868}; KM=2 uM for C20-acyl-CoA {ECO:0000269|PubMed:7744868}; Vmax=1 umol/min/mg enzyme with C10-acyl-CoA as substrate {ECO:0000269|PubMed:7744868}; Vmax=2.2 umol/min/mg enzyme with C12-acyl-CoA as substrate {ECO:0000269|PubMed:7744868}; Vmax=4.2 umol/min/mg enzyme with C14-acyl-CoA as substrate {ECO:0000269|PubMed:7744868}; Vmax=4.5 umol/min/mg enzyme with C16-acyl-CoA as substrate {ECO:0000269|PubMed:7744868}; Vmax=3.3 umol/min/mg enzyme with C18-acyl-CoA as substrate {ECO:0000269|PubMed:7744868}; Vmax=3.1 umol/min/mg enzyme with C20-acyl-CoA as substrate {ECO:0000269|PubMed:7744868}; |
| Metal Binding | |
| Rhea ID | RHEA:16645; RHEA:16646; RHEA:40119; RHEA:40120; RHEA:30139; RHEA:30140; RHEA:40147; RHEA:40148; RHEA:40059; RHEA:40060; RHEA:30135; RHEA:30136; RHEA:40139; RHEA:40140; RHEA:40131; RHEA:40132; RHEA:40723; RHEA:40724; RHEA:40143; RHEA:40144 |
| Cross Reference Brenda | 3.1.2.2;3.1.2.20; |