| IED ID | IndEnz0010000201 |
| Enzyme Type ID | esterase000201 |
| Protein Name |
Cytosolic acyl coenzyme A thioester hydrolase EC 3.1.2.2 ACH1 ACT Acyl-CoA thioesterase 7 Brain acyl-CoA hydrolase BACH CTE-IIa CTE-IIb CTE-II LACH1 Long chain acyl-CoA thioester hydrolase MTE-II |
| Gene Name | Acot7 Bach |
| 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 | MKLLARTLYLWEVGRQVASWSLTSGQECLVLRETWWASMRAVRTRAVHHKPGHCIAMGRIMRPDDANVAGNVHGGTILKMIEEAGVIISTRHCNSQNGERCVAALARVERTDFLSPMCIGEVAHVSAEITYTSKHSVEVQVHVLSENILTGTKKLTNKATLWYVPLSLKNVDKVLEVPPIVYLRQEQEEEGRKRYEAQKLERMETKWRNGDIVQPILNPEPNTVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLVDADPVVDNSQKRYRAASAFFTYVSLNQEGKPLPVPQLVPETEDEKKRFEEGKGRYLQMKAKRQGHTEPQP |
| Enzyme Length | 381 |
| Uniprot Accession Number | Q64559 |
| Absorption | |
| Active Site | ACT_SITE 67; /evidence=ECO:0000250; ACT_SITE 256; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | 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:7906114};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; Evidence={ECO:0000305|PubMed:7906114}; 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:7906114};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136; Evidence={ECO:0000305|PubMed:7906114}; 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:7906114};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120; Evidence={ECO:0000305|PubMed:7906114}; 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:7906114};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060; Evidence={ECO:0000305|PubMed:7906114}; CATALYTIC ACTIVITY: Reaction=H2O + octanoyl-CoA = CoA + H(+) + octanoate; Xref=Rhea:RHEA:30143, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386; Evidence={ECO:0000269|PubMed:7906114};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30144; Evidence={ECO:0000305|PubMed:7906114}; 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:7906114};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140; Evidence={ECO:0000305|PubMed:7906114}; 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:7906114};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140; Evidence={ECO:0000305|PubMed:7906114}; |
| DNA Binding | |
| EC Number | 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:7906114). Preferentially hydrolyzes palmitoyl-CoA, but has a broad specificity acting on other fatty acyl-CoAs with chain-lengths of C8-C18 (PubMed:7906114). May play an important physiological function in brain (PubMed:7906114). {ECO:0000269|PubMed:7906114}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305|PubMed:7906114}. |
| nucleotide Binding | |
| Features | Active site (2); Alternative sequence (1); Chain (1); Compositional bias (1); Domain (2); Modified residue (3); Region (1); Sequence conflict (8) |
| Keywords | Acetylation;Alternative splicing;Cytoplasm;Direct protein sequencing;Fatty acid metabolism;Hydrolase;Lipid metabolism;Reference proteome;Repeat;Serine esterase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:7906114}. |
| Modified Residue | MOD_RES 169; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:O00154; MOD_RES 199; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:O00154; MOD_RES 284; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:O00154 |
| Post Translational Modification | PTM: The N-terminus is blocked. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 42,735 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.9 uM for palmitoyl-CoA {ECO:0000269|PubMed:7906114}; Vmax=553 umol/min/mg enzyme with palmitoyl-CoA as substrate {ECO:0000269|PubMed:7906114}; |
| Metal Binding | |
| Rhea ID | RHEA:16645; RHEA:16646; RHEA:30135; RHEA:30136; RHEA:40119; RHEA:40120; RHEA:40059; RHEA:40060; RHEA:30143; RHEA:30144; RHEA:30139; RHEA:30140; RHEA:40139; RHEA:40140 |
| Cross Reference Brenda | 3.1.2.2;3.1.2.20; |