| IED ID | IndEnz0010001574 |
| Enzyme Type ID | esterase001574 |
| Protein Name |
Peroxisomal succinyl-coenzyme A thioesterase EC 3.1.2.3 Acyl-coenzyme A thioesterase 4 Acyl-CoA thioesterase 4 EC 3.1.2.2 PTE-2b Peroxisomal acyl coenzyme A thioester hydrolase Ib Peroxisomal long-chain acyl-CoA thioesterase Ib PTE-Ib |
| Gene Name | ACOT4 PTE2B PTEIB |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MSATLILEPPGRCCWNEPVRIAVRGLAPEQRVTLRASLRDEKGALFRAHARYCADARGELDLERAPALGGSFAGLEPMGLLWALEPEKPFWRFLKRDVQIPFVVELEVLDGHDPEPGRLLCQAQHERHFLPPGVRRQSVRAGRVRATLFLPPGPGPFPGIIDIFGIGGGLLEYRASLLAGHGFATLALAYYNFEDLPNNMDNISLEYFEEAVCYMLQHPQVKGPGIGLLGISLGADICLSMASFLKNVSATVSINGSGISGNTAINYKHSSIPPLGYDLRRIKVAFSGLVDIVDIRNALVGGYKNPSMIPIEKAQGPILLIVGQDDHNWRSELYAQTVSERLQAHGKEKPQIICYPGTGHYIEPPYFPLCPASLHRLLNKHVIWGGEPRAHSKAQEDAWKQILAFFCKHLGGTQKTAVPKL |
| Enzyme Length | 421 |
| Uniprot Accession Number | Q8N9L9 |
| 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:16940157};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11517; Evidence={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:16940157};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40576; Evidence={ECO:0000305|PubMed:16940157}; 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:16940157};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; Evidence={ECO:0000305|PubMed:16940157}; 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:16940157};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140; Evidence={ECO:0000305|PubMed:16940157}; 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:0000269|PubMed:16940157};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40144; Evidence={ECO:0000305|PubMed:16940157}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + CoA + H(+); Xref=Rhea:RHEA:40151, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368; Evidence={ECO:0000269|PubMed:16940157};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40152; Evidence={ECO:0000305|PubMed:16940157}; 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:16940157};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060; Evidence={ECO:0000305|PubMed:16940157}; 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:16940157};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136; Evidence={ECO:0000305|PubMed:16940157}; 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:16940157};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120; Evidence={ECO:0000305|PubMed:16940157}; 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:16940157};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140; Evidence={ECO:0000305|PubMed:16940157}; 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:16940157};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40148; Evidence={ECO:0000305|PubMed:16940157}; |
| DNA Binding | |
| EC Number | 3.1.2.3; 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 (PubMed:16940157). Functions as a peroxisomal succinyl-coenzyme A thioesterase that can also hydrolyze glutaryl-CoA and long chain saturated acyl-CoAs (PubMed:16940157). {ECO:0000269|PubMed:16940157}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000305|PubMed:16940157}. |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (23); Chain (1); Helix (9); Modified residue (1); Motif (1); Natural variant (2); Sequence conflict (2); Turn (3) |
| Keywords | 3D-structure;Fatty acid metabolism;Hydrolase;Lipid metabolism;Peroxisome;Reference proteome;Serine esterase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:16940157}. |
| Modified Residue | MOD_RES 313; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:Q8BWN8 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 3K2I; |
| Mapped Pubmed ID | 10022913; 11101887; 11673457; 12456682; 12559034; 12578380; 12885776; 16141203; 17007944; 18712838; 19197237; 19584060; 19632994; 20178365; 21976670; 22002062; 22747494; 23963456; 24235149; 25854684; 25961151; 26220973; 28765278; 28787099; 33148467; 7719337; 7790377; 8824437; 8858165; 9653144; 9668159; 9837948; |
| Motif | MOTIF 419..421; /note=Microbody targeting signal; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 46,327 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=14 uM for succinyl-CoA {ECO:0000269|PubMed:16940157}; KM=147 uM for glutaryl-CoA {ECO:0000269|PubMed:16940157}; KM=3.4 uM for C14-acyl-CoA {ECO:0000269|PubMed:16940157}; Vmax=581 nmol/min/mg enzyme with succinyl-CoA as substrate {ECO:0000269|PubMed:16940157}; Vmax=132 nmol/min/mg enzyme with glutaryl-CoA as substrate {ECO:0000269|PubMed:16940157}; Vmax=137 nmol/min/mg enzyme with C14-acyl-CoA as substrate {ECO:0000269|PubMed:16940157}; |
| Metal Binding | |
| Rhea ID | RHEA:11516; RHEA:11517; RHEA:40575; RHEA:40576; RHEA:16645; RHEA:16646; RHEA:40139; RHEA:40140; RHEA:40143; RHEA:40144; RHEA:40151; RHEA:40152; RHEA:40059; RHEA:40060; RHEA:30135; RHEA:30136; RHEA:40119; RHEA:40120; RHEA:30139; RHEA:30140; RHEA:40147; RHEA:40148 |
| Cross Reference Brenda |