| IED ID | IndEnz0010000329 |
| Enzyme Type ID | esterase000329 |
| Protein Name |
Acetyl-coenzyme A thioesterase EC 3.1.2.1 Acyl-CoA thioester hydrolase 12 Acyl-coenzyme A thioesterase 12 Acyl-CoA thioesterase 12 Cytoplasmic acetyl-CoA hydrolase 1 CACH-1 rACH rCACH-1 |
| Gene Name | Acot12 Cach Cach1 |
| 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 | MEPTVAPGEVLMSQAIQPAHADSRGELSAGQLLKWMDTTACLAAEKHAGISCVTASMDDILFEDTARIGQIVTIRAKVTRAFSTSMEISIKVRVQDKFTGIQKLLCVAFSTFVVKPLGKEKVHLKPVLLQTEQEQVEHRLASERRKVRLQHENTFSNIMKESNWLRDPVCNEEEGTATTMATSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCHGHPFLKSVDMFKFRGPSTVGDRLVFNAIVNNTFQNSVEVGVRVEAFDCREWAEGQGRHINSAFLIYNAVDDQEELITFPRIQPISKDDFRRYQGAIARRRIRLGRKYVISHKKEVPLGTQWDISKKGSISNTNVEALKNLASKSGWEITTTLEKIKIYTLEEQDAISVKVEKQVGSPARVAYHLLSDFTKRPLWDPHYISCEVIDQVSEDDQIYYITCSVVNGDKPKDFVVLVSQRKPLKDDNTYIVALMSVVLPSVPPSPQYIRSQVICAGFLIQPVDSSSCTVAYLNQMSDSILPYFAGNIGGWSKSIEEAAASCIKFIENATHDGLKSVL |
| Enzyme Length | 556 |
| Uniprot Accession Number | Q99NB7 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Allosterically regulated by ATP (activator) and ADP (inhibitor) (PubMed:11322891). Cold labile, it dissociates into inactive monomers at low temperature (PubMed:6136404). {ECO:0000269|PubMed:11322891, ECO:0000269|PubMed:6136404}. |
| Binding Site | BINDING 145; /note=Coenzyme A; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H2O = acetate + CoA + H(+); Xref=Rhea:RHEA:20289, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=3.1.2.1; Evidence={ECO:0000269|PubMed:11322891};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20290; Evidence={ECO:0000305|PubMed:11322891}; CATALYTIC ACTIVITY: Reaction=butanoyl-CoA + H2O = butanoate + CoA + H(+); Xref=Rhea:RHEA:40111, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371; Evidence={ECO:0000269|PubMed:11322891};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40112; Evidence={ECO:0000305|PubMed:11322891}; CATALYTIC ACTIVITY: Reaction=H2O + hexanoyl-CoA = CoA + H(+) + hexanoate; Xref=Rhea:RHEA:40115, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17120, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620; Evidence={ECO:0000269|PubMed:11322891};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40116; Evidence={ECO:0000305|PubMed:11322891}; |
| DNA Binding | |
| EC Number | 3.1.2.1 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels. Preferentially hydrolyzes acetyl-CoA. {ECO:0000269|PubMed:11322891}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305|PubMed:11322891}. |
| nucleotide Binding | |
| Features | Binding site (1); Chain (1); Domain (3); Modified residue (4); Region (3) |
| Keywords | Allosteric enzyme;Cytoplasm;Direct protein sequencing;Fatty acid metabolism;Hydrolase;Lipid metabolism;Reference proteome;Repeat;Serine esterase |
| Interact With | |
| Induction | INDUCTION: By 2-(p-chlorophenoxy)isobutyric acid (CPIB). |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11322891}. |
| Modified Residue | MOD_RES 34; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:Q9DBK0; MOD_RES 97; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:Q9DBK0; MOD_RES 160; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:Q9DBK0; MOD_RES 229; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:Q9DBK0 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 2566591; 2857646; |
| Motif | |
| Gene Encoded By | |
| Mass | 62,018 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=153 uM for acetyl-CoA {ECO:0000269|PubMed:11322891}; |
| Metal Binding | |
| Rhea ID | RHEA:20289; RHEA:20290; RHEA:40111; RHEA:40112; RHEA:40115; RHEA:40116 |
| Cross Reference Brenda | 3.1.2.1; |