Detail Information for IndEnz0010000340
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