IED ID | IndEnz0010000340 |
Enzyme Type ID | esterase000340 |
Protein Name |
Peroxisomal succinyl-coenzyme A thioesterase EC 3.1.2.3 Acyl-coenzyme A thioesterase 4 Acyl-CoA thioesterase 4 PTE-2b Peroxisomal acyl coenzyme A thioester hydrolase Ib Peroxisomal long-chain acyl-CoA thioesterase Ib PTE-Ib |
Gene Name | Acot4 Pte1b Pte2b |
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 | MAATLSVEPTGRSCWDEPLSIAVRGLAPEQPVTLRSVLRDEKGALFRAHARYRADSHGELDLARVPALGGSFSGLEPMGLLWAMEPDRPFWRLIKRDVQTPFLVELEVLDGHEPDGGRRLARTVHERHFMAPGVRRVPVREGRVRATLFLPPGQGPFPGIIDVYGVGGGLLEYRAGLVAGHGFATLALAFYDFEDLPKELNVIEVDYFEEAVRYMLRHPKVKGPDIGLLGLSLGADVCLIMASFLNNVSATVSINGSAFSGNRHIKYKQTMIPPLGHDLRRMKVAFSGILDIVDIRNDAVGGCENPSMIPIEKAKGPILFVAGQDDHCWRSELYTQIASDRLQAHGKERPQVLSYPGTGHYIEPPYFPMCPASLHKIVNEAVIWGGEVKAHSKAQIDAWKQILFFFGKHLGSTHSRASCRL |
Enzyme Length | 421 |
Uniprot Accession Number | Q8BWN8 |
Absorption | |
Active Site | ACT_SITE 232; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P49753; ACT_SITE 326; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P49753; ACT_SITE 360; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P49753 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O + succinyl-CoA = CoA + H(+) + succinate; Xref=Rhea:RHEA:11516, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30031, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=3.1.2.3; Evidence={ECO:0000269|PubMed:16141203, ECO:0000269|PubMed:16940157};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11517; Evidence={ECO:0000305|PubMed:16141203, ECO:0000305|PubMed:16940157}; CATALYTIC ACTIVITY: Reaction=glutaryl-CoA + H2O = CoA + glutarate + H(+); Xref=Rhea:RHEA:40575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30921, ChEBI:CHEBI:57287, ChEBI:CHEBI:57378; Evidence={ECO:0000269|PubMed:16141203, ECO:0000269|PubMed:16940157};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40576; Evidence={ECO:0000305|PubMed:16141203, ECO:0000305|PubMed:16940157}; |
DNA Binding | |
EC Number | 3.1.2.3 |
Enzyme Function | FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels (PubMed:16141203, PubMed:16940157). In contrast to its human ortholog, functions essentially as a succinyl-CoA thioesterase with no activity with medium to long chain saturated acyl-CoAs and with a low activity toward glutaryl-CoA (PubMed:16141203, PubMed:16940157). {ECO:0000269|PubMed:16141203, ECO:0000269|PubMed:16940157}. |
Temperature Dependency | |
PH Dependency | |
Pathway | PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305|PubMed:16141203, ECO:0000305|PubMed:16940157}. |
nucleotide Binding | |
Features | Active site (3); Chain (1); Modified residue (1); Motif (1); Sequence conflict (3) |
Keywords | Fatty acid metabolism;Hydrolase;Lipid metabolism;Peroxisome;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:10567408}. |
Subcellular Location | SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:16141203}. |
Modified Residue | MOD_RES 313; /note=N6-succinyllysine; /evidence=ECO:0007744|PubMed:23806337 |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 12466851; 14561759; 14681479; 15007068; 21267068; 21677750; 23260145; 24194600; 27626380; |
Motif | MOTIF 419..421; /note=Microbody targeting signal; /evidence=ECO:0000255 |
Gene Encoded By | |
Mass | 46,481 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13.3 uM for succinyl-CoA {ECO:0000269|PubMed:16141203}; KM=37.1 uM for glutaryl-CoA {ECO:0000269|PubMed:16141203}; Vmax=3.98 umol/min/mg enzyme with succinyl-CoA as substrate {ECO:0000269|PubMed:16141203}; Vmax=1.14 umol/min/mg enzyme with glutaryl-CoA as substrate {ECO:0000269|PubMed:16141203}; |
Metal Binding | |
Rhea ID | RHEA:11516; RHEA:11517; RHEA:40575; RHEA:40576 |
Cross Reference Brenda |