Detail Information for IndEnz0010000046
IED ID IndEnz0010000046
Enzyme Type ID esterase000046
Protein Name Acyl-coenzyme A thioesterase 1
Acyl-CoA thioesterase 1
EC 3.1.2.-
CTE-I
CTE-Ib
Inducible cytosolic acyl-coenzyme A thioester hydrolase
Long chain acyl-CoA thioester hydrolase
Long chain acyl-CoA hydrolase
Palmitoyl-coenzyme A thioesterase
EC 3.1.2.2
Gene Name ACOT1 CTE1
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 MAATLILEPAGRCCWDEPVRIAVRGLAPEQPVTLRASLRDEKGALFQAHARYRADTLGELDLERAPALGGSFAGLEPMGLLWALEPEKPLVRLVKRDVRTPLAVELEVLDGHDPDPGRLLCRVRHERYFLPPGVRREPVRAGRVRGTLFLPPEPGPFPGIVDMFGTGGGLLEYRASLLAGKGFAVMALAYYNYEDLPKTMETLHLEYFEEAVNYLLSHPEVKGPGVGLLGISKGGELCLSMASFLKGITAAVVINGSVANVGGTLRYKGETLPPVGVNRNRIKVTKDGYADIVDVLNSPLEGPDQKSFIPVERAESTFLFLVGQDDHNWKSEFYANEACKRLQAHGRRKPQIICYPETGHYIEPPYFPLCRASLHALVGSPIIWGGEPRAHAMAQVDAWKQLQTFFHKHLGGHEGTIPSKV
Enzyme Length 421
Uniprot Accession Number Q86TX2
Absorption
Active Site ACT_SITE 232; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 326; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 360; /note=Charge relay system; /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:16940157};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; 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}; 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)-hexadecenoyl-CoA + H2O = (9Z)-hexadecenoate + CoA + H(+); Xref=Rhea:RHEA:40131, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32372, ChEBI:CHEBI:57287, ChEBI:CHEBI:61540; Evidence={ECO:0000269|PubMed:16940157};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40132; Evidence={ECO:0000305|PubMed:16940157}; CATALYTIC ACTIVITY: Reaction=(9E)-octadecenoyl-CoA + H2O = (9E)-octadecenoate + CoA + H(+); Xref=Rhea:RHEA:40723, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30825, ChEBI:CHEBI:57287, ChEBI:CHEBI:77537; Evidence={ECO:0000269|PubMed:16940157};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40724; Evidence={ECO:0000305|PubMed:16940157};
DNA Binding
EC Number 3.1.2.-; 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. More active towards saturated and unsaturated long chain fatty acyl-CoAs (C12-C20). {ECO:0000269|PubMed:16940157}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305|PubMed:16940157}.
nucleotide Binding
Features Active site (3); Chain (1); Initiator methionine (1); Natural variant (1)
Keywords Cytoplasm;Direct protein sequencing;Fatty acid metabolism;Hydrolase;Lipid metabolism;Reference proteome;Serine esterase
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16940157}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11696000; 15638818; 16423998; 16934754; 19170545; 20338778; 20470824; 22465940; 23700546; 23901139; 24732803; 25002576; 26496610; 29555575; 34520261; 35215835;
Motif
Gene Encoded By
Mass 46,277
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=35.8 uM for C10-acyl-CoA {ECO:0000269|PubMed:16940157}; KM=3.6 uM for C12-acyl-CoA {ECO:0000269|PubMed:16940157}; KM=2.8 uM for C14-acyl-CoA {ECO:0000269|PubMed:16940157}; KM=3.6 uM for C16-acyl-CoA {ECO:0000269|PubMed:16940157}; KM=2.4 uM for C18-acyl-CoA {ECO:0000269|PubMed:16940157}; KM=2 uM for C20-acyl-CoA {ECO:0000269|PubMed:16940157}; KM=2.4 uM for C16:1-acyl-CoA {ECO:0000269|PubMed:16940157}; KM=4.1 uM for C18:1-acyl-CoA {ECO:0000269|PubMed:16940157}; KM=2.1 uM for C18:1-trans-acyl-CoA {ECO:0000269|PubMed:16940157}; Vmax=224 nmol/min/mg enzyme toward C10-acyl-CoA {ECO:0000269|PubMed:16940157}; Vmax=700 nmol/min/mg enzyme toward C12-acyl-CoA {ECO:0000269|PubMed:16940157}; Vmax=912 nmol/min/mg enzyme toward C14-acyl-CoA {ECO:0000269|PubMed:16940157}; Vmax=691 nmol/min/mg enzyme toward C16-acyl-CoA {ECO:0000269|PubMed:16940157}; Vmax=597 nmol/min/mg enzyme toward C18-acyl-CoA {ECO:0000269|PubMed:16940157}; Vmax=520 nmol/min/mg enzyme toward C20-acyl-CoA {ECO:0000269|PubMed:16940157}; Vmax=577 nmol/min/mg enzyme toward C16:1-acyl-CoA {ECO:0000269|PubMed:16940157}; Vmax=258 nmol/min/mg enzyme toward C18:1-acyl-CoA {ECO:0000269|PubMed:16940157}; Vmax=309 nmol/min/mg enzyme toward C18:1-trans-acyl-CoA {ECO:0000269|PubMed:16940157};
Metal Binding
Rhea ID RHEA:16645; RHEA:16646; RHEA:40059; RHEA:40060; RHEA:30135; RHEA:30136; RHEA:40119; RHEA:40120; RHEA:30139; RHEA:30140; RHEA:40147; RHEA:40148; RHEA:40139; RHEA:40140; RHEA:40131; RHEA:40132; RHEA:40723; RHEA:40724
Cross Reference Brenda 3.1.2.2;