| IED ID | IndEnz0010000202 |
| Enzyme Type ID | esterase000202 |
| Protein Name |
Acyl-coenzyme A thioesterase 6 Acyl-CoA thioesterase 6 EC 3.1.2.- |
| Gene Name | Acot6 |
| 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 | MAATLSVEPAGRSCWDEPLSIAVRGLAPEQPVTLRSVLRDEKGMLFRAHARYRADSHGELDLARTPALGGSFSGLEPMGLLWAMEPDRPFWRLIKRDVQIPFVVELEVLDGHEPDGGQRLARAVHERHFMAPGVRRVPVREGRVRATLFLPPGKGQFPGIIDLYGSIGGLCEHRASLLAGHGFAVLALAYFQFEDLPENLSDVRLEYFEEALALMLRHPQVKGPNIGLIGVSKGADLCLSMAAFLKDNITATVLINACVANTLVPLYYKDLFVPELGCDQTKNKSGLMDLRDMWNNPLEEPNHQSLIPLEKAQGPFLFLVGMDDHNWKSDVYARIACERLQAHGKDRPQIIYYPETGHCIEPPYFPPPIATVHFVLGEAVFNGGKPRAQSRAQLDAWQRIQTFFQKYLNGEKPARHSKL |
| Enzyme Length | 419 |
| Uniprot Accession Number | Q32Q92 |
| Absorption | |
| Active Site | ACT_SITE 232; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:O55137; ACT_SITE 324; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:O55137; ACT_SITE 358; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:O55137 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O + pristanoyl-CoA = 2,6,10,14-tetramethylpentadecanoate + CoA + H(+); Xref=Rhea:RHEA:40415, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:77250, ChEBI:CHEBI:77268; Evidence={ECO:0000269|PubMed:17613526};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40416; Evidence={ECO:0000305|PubMed:17613526}; CATALYTIC ACTIVITY: Reaction=H2O + phytanoyl-CoA = 3,7,11,15-tetramethylhexadecanoate + CoA + H(+); Xref=Rhea:RHEA:40419, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37257, ChEBI:CHEBI:57287, ChEBI:CHEBI:57391; Evidence={ECO:0000269|PubMed:17613526};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40420; Evidence={ECO:0000305|PubMed:17613526}; |
| DNA Binding | |
| EC Number | 3.1.2.- |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels. Catalyzes the hydrolysis of phytanoyl-CoA and pristanoyl-CoA, two methyl-branched fatty acids derived from phytol, that enter the body via the diet. {ECO:0000269|PubMed:17613526}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305|PubMed:17613526}. |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (2); Chain (1); Erroneous initiation (1); Frameshift (1); Motif (1); Sequence caution (1) |
| Keywords | Alternative splicing;Fatty acid metabolism;Hydrolase;Lipid metabolism;Peroxisome;Reference proteome;Serine esterase |
| Interact With | |
| Induction | INDUCTION: Up-regulated in liver upon treatment with peroxisome proliferator. {ECO:0000269|PubMed:17613526}. |
| Subcellular Location | SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:17613526}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11217851; 12466851; 16940157; 21267068; 21677750; 24652767; |
| Motif | MOTIF 417..419; /note=Peroxisome targeting signal; /evidence=ECO:0000305|PubMed:17613526 |
| Gene Encoded By | |
| Mass | 46,769 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=24 uM for pristanoyl-CoA {ECO:0000269|PubMed:17613526}; Vmax=3.2 umol/min/mg enzyme with pristanoyl-CoA as substrate {ECO:0000269|PubMed:17613526}; |
| Metal Binding | |
| Rhea ID | RHEA:40415; RHEA:40416; RHEA:40419; RHEA:40420 |
| Cross Reference Brenda |