IED Industry Enzyme Database

Detail Information for IndEnz0010000338
IED ID IndEnz0010000338
Enzyme Type ID esterase000338
Protein Name Acyl-coenzyme A thioesterase 2, mitochondrial
Acyl-CoA thioesterase 2
EC 3.1.2.2
Acyl-coenzyme A thioester hydrolase 2a
CTE-Ia
Long-chain acyl-CoA thioesterase 2
ZAP128
Gene Name ACOT2 PTE2 PTE2A
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 MSNKLLSPHPHSVVLRSEFKMASSPAVLRASRLYQWSLKSSAQFLGSPQLRQVGQIIRVPARMAATLILEPAGRCCWDEPVRIAVRGLAPEQPVTLRASLRDEKGALFQAHARYRADTLGELDLERAPALGGSFAGLEPMGLLWALEPEKPLVRLVKRDVRTPLAVELEVLDGHDPDPGRLLCQTRHERYFLPPGVRREPVRVGRVRGTLFLPPEPGPFPGIVDMFGTGGGLLEYRASLLAGKGFAVMALAYYNYEDLPKTMETLHLEYFEEAMNYLLSHPEVKGPGVGLLGISKGGELCLSMASFLKGITAAVVINGSVANVGGTLHYKGETLPPVGVNRNRIKVTKDGYADIVDVLNSPLEGPDQKSFIPVERAESTFLFLVGQDDHNWKSEFYANEACKRLQAHGRRKPQIICYPETGHYIEPPYFPLCRASLHALVGSPIIWGGEPRAHAMAQVDAWKQLQTFFHKHLGGHEGTIPSKV
Enzyme Length 483
Uniprot Accession Number P49753
Absorption
Active Site ACT_SITE 294; /note=Charge relay system; /evidence=ECO:0000303|PubMed:19497300; ACT_SITE 388; /note=Charge relay system; /evidence=ECO:0000303|PubMed:19497300; ACT_SITE 422; /note=Charge relay system; /evidence=ECO:0000303|PubMed:19497300
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:10944470, ECO:0000269|PubMed:16940157};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; 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:10944470, 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:10944470, 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:10944470, ECO:0000269|PubMed:16940157};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40148; 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:10944470, 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=(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}; 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:0000250|UniProtKB:Q9QYR9};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40144; Evidence={ECO:0000250|UniProtKB:Q9QYR9};
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:16940157, PubMed:10944470). Displays higher activity toward long chain acyl CoAs (C14-C20) (PubMed:16940157, PubMed:10944470). The enzyme is involved in enhancing the hepatic fatty acid oxidation in mitochondria (By similarity). {ECO:0000250|UniProtKB:Q9QYR9, ECO:0000269|PubMed:10944470, ECO:0000269|PubMed:16940157}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305|PubMed:10944470, ECO:0000305|PubMed:16940157}.
nucleotide Binding
Features Active site (3); Alternative sequence (2); Beta strand (22); Chain (1); Frameshift (1); Helix (9); Modified residue (2); Motif (1); Natural variant (2); Sequence conflict (10); Transit peptide (1); Turn (2)
Keywords 3D-structure;Acetylation;Alternative splicing;Fatty acid metabolism;Hydrolase;Lipid metabolism;Mitochondrion;Reference proteome;Serine esterase;Transit peptide
Interact With Q9NZ94-2
Induction
Subcellular Location SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16940157}.
Modified Residue MOD_RES 104; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q9QYR9; MOD_RES 470; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:Q9QYR9
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 3HLK;
Mapped Pubmed ID 10022913; 11101887; 12456682; 12559034; 12578380; 12885776; 17007944; 18712838; 19197237; 19584060; 19632994; 20178365; 20379614; 20470824; 20877624; 21976670; 22002062; 22465940; 22586271; 22747494; 22871024; 23700546; 23963456; 24235149; 25854684; 26220973; 28765278; 28787099; 35215835; 7719337; 7790377; 8824437; 8858165; 9653144; 9668159; 9837948;
Motif MOTIF 481..483; /note=Microbody targeting signal; /evidence=ECO:0000255
Gene Encoded By
Mass 53,218
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=40.3 uM for C10-acyl-CoA {ECO:0000269|PubMed:16940157}; KM=8.9 uM for C12-acyl-CoA {ECO:0000269|PubMed:16940157}; KM=1.6 uM for C14-acyl-CoA {ECO:0000269|PubMed:16940157}; KM=2.0 uM for C16-acyl-CoA {ECO:0000269|PubMed:16940157}; KM=2.8 uM for C18-acyl-CoA {ECO:0000269|PubMed:16940157}; KM=4.8 uM for C20-acyl-CoA {ECO:0000269|PubMed:16940157}; KM=4.5 uM for C16:1-acyl-CoA {ECO:0000269|PubMed:16940157}; KM=6.1 uM for C18:1-acyl-CoA {ECO:0000269|PubMed:16940157}; KM=4.3 uM for C18:1-trans-acyl-CoA {ECO:0000269|PubMed:16940157}; Vmax=212 nmol/min/mg enzyme with C10-acyl-CoA as substrate {ECO:0000269|PubMed:16940157}; Vmax=681 nmol/min/mg enzyme with C12-acyl-CoA as substrate {ECO:0000269|PubMed:16940157}; Vmax=766 nmol/min/mg enzyme with C14-acyl-CoA as substrate {ECO:0000269|PubMed:16940157}; Vmax=656 nmol/min/mg enzyme with C16-acyl-CoA as substrate {ECO:0000269|PubMed:16940157}; Vmax=488 nmol/min/mg enzyme with C18-acyl-CoA as substrate {ECO:0000269|PubMed:16940157}; Vmax=408 nmol/min/mg enzyme with C20-acyl-CoA as substrate {ECO:0000269|PubMed:16940157}; Vmax=661 nmol/min/mg enzyme with C16:1-acyl-CoA as substrate {ECO:0000269|PubMed:16940157}; Vmax=304 nmol/min/mg enzyme with C18:1-acyl-CoA as substrate {ECO:0000269|PubMed:16940157}; Vmax=418 nmol/min/mg enzyme with C18:1-trans-acyl-CoA as substrate {ECO:0000269|PubMed:16940157};
Metal Binding
Rhea ID RHEA:16645; RHEA:16646; RHEA:40119; RHEA:40120; RHEA:30139; RHEA:30140; RHEA:40147; RHEA:40148; RHEA:40059; RHEA:40060; RHEA:30135; RHEA:30136; RHEA:40139; RHEA:40140; RHEA:40131; RHEA:40132; RHEA:40723; RHEA:40724; RHEA:40143; RHEA:40144
Cross Reference Brenda 3.1.2.2;