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Information on EC 3.1.2.2 - palmitoyl-CoA hydrolase and Organism(s) Homo sapiens and UniProt Accession P49753

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.2 Thioester hydrolases
                3.1.2.2 palmitoyl-CoA hydrolase
IUBMB Comments
Also hydrolyses CoA thioesters of other long-chain fatty acids.
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P49753
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
thioesterase, palmitoyl-coa hydrolase, acot7, thioesterase ii, acot1, type ii fas, acot2, thioesterase i, mte-i, cte-i, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acyl-CoA thioesterase 2
-
acyl-coenzyme A thioester hydrolase 2a
-
long-chain acyl-CoA thioesterase 2
-
ACH1
-
-
-
-
ACH2
-
-
-
-
ACT
-
-
-
-
acyl CoA hydrolase
-
-
-
-
acyl coenzyme A hydrolase
-
-
-
-
acyl coenzyme A thioesterase
-
-
-
-
acyl-CoA thioesterase
-
-
-
-
acyl-CoA thioesterase 1
-
brain acyl-CoA hydrolase
fatty acid synthase thioesterase
-
-
fatty acyl thioesterase I
-
-
-
-
HIV-Nef associated acyl coA thioesterase
-
-
-
-
hydrolase, acyl coenzyme A
-
-
-
-
hydrolase, palmitoyl coenzyme A
-
-
-
-
LACH1
-
-
-
-
LACH2
-
-
-
-
long chain acyl-CoA hydrolase
-
-
-
-
long chain acyl-CoA thioesterase
-
-
-
-
long chain fatty-acyl-CoA hydrolase
-
-
-
-
long chain fatty-acyl-CoA thioesterase
-
-
-
-
mitochondrial acyl-CoA thioesterase
-
-
-
-
palmitoyl coenzyme A hydrolase
-
-
-
-
palmitoyl protein thioesterase-1
-
palmitoyl thioesterase
-
-
-
-
palmitoyl-CoA deacylase
-
-
-
-
palmitoyl-CoA hydrolase
-
-
-
-
palmityl coenzyme A deacylase
-
-
-
-
palmityl thioesterase
-
-
-
-
palmityl thioesterase I
-
-
-
-
palmityl thioesterase II
-
-
-
-
peroxisomal acyl-CoA thioesterase 2
-
TE
-
-
-
-
TE-II
-
-
-
-
thioesterase B
-
-
-
-
thioesterase II
-
-
-
-
very long chain acyl-CoA thioesterase
-
-
-
-
ZAP128
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of thioester
SYSTEMATIC NAME
IUBMB Comments
palmitoyl-CoA hydrolase
Also hydrolyses CoA thioesters of other long-chain fatty acids.
CAS REGISTRY NUMBER
COMMENTARY hide
37270-64-7
EC 3.1.2.2
9025-87-0
-
9025-87-0
EC 3.1.2.20
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
decanoyl-CoA + H2O
CoA + decanoate
show the reaction diagram
-
-
-
?
dodecanoyl-CoA + H2O
CoA + dodecanoate
show the reaction diagram
-
-
-
?
eicosanoyl-CoA + H2O
CoA + eicosanoic acid
show the reaction diagram
-
-
-
?
hexadecanoyl-CoA + H2O
CoA + hexadecanoate
show the reaction diagram
-
-
-
?
octadecanoyl-CoA + H2O
CoA + octadecanoate
show the reaction diagram
-
-
-
?
oleoyl-CoA + H2O
CoA + oleic acid
show the reaction diagram
-
-
-
?
palmitoleoyl-CoA + H2O
CoA + palmitoleic acid
show the reaction diagram
-
-
-
?
tetradecanoyl-CoA + H2O
CoA + tetradecanoate
show the reaction diagram
-
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
-
-
-
?
acyl-CoA + H2O
CoA + a carboxylate
show the reaction diagram
arachidonoyl-CoA + H2O
CoA + arachidonate
show the reaction diagram
decanoyl-CoA + H2O
CoA + decanoate
show the reaction diagram
dodecanoyl-CoA + H2O
CoA + dodecanoate
show the reaction diagram
eicosanoyl-CoA + H2O
CoA + eicosanoic acid
show the reaction diagram
-
-
-
?
gamma-linolenoyl-CoA + H2O
CoA + gamma-linolenoate
show the reaction diagram
-
best substrate
-
-
?
hexadecanoyl-CoA + H2O
CoA + hexadecanoate
show the reaction diagram
linoleoyl-CoA + H2O
CoA + linoleate
show the reaction diagram
-
-
-
-
?
n-butyryl-CoA + H2O
CoA + n-butanoate
show the reaction diagram
-
-
-
-
?
octadecanoyl-CoA + H2O
CoA + octadecanoate
show the reaction diagram
-
-
-
?
octanoyl-CoA + H2O
CoA + octanoate
show the reaction diagram
-
-
-
?
oleoyl-CoA + H2O
CoA + oleate
show the reaction diagram
oleoyl-CoA + H2O
CoA + oleic acid
show the reaction diagram
-
-
-
?
palmitoleoyl-CoA + H2O
CoA + palmitoleic acid
show the reaction diagram
-
-
-
?
palmitoyl-CoA + H2O
CoA + palmitate
show the reaction diagram
tetradecanoyl-CoA + H2O
CoA + tetradecanoate
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
arachidonoyl-CoA + H2O
CoA + arachidonate
show the reaction diagram
palmitoyl-CoA + H2O
CoA + palmitate
show the reaction diagram
-
-
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NGDA
-
isozymes CTE-I and MTE-I
orlistat
p-chloromercuribenzoic acid
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTH
-
-
-
bovine serum albumin
-
-
-
linoleic acid
-
both conjugated and gamma-linoleic acid, increase activity
additional information
-
no stimulation of activity by docosahexaenoic and eisosapentaenoic acids
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0403
decanoyl-CoA
-
0.089
dodecanoyl-CoA
-
0.0048
eicosanoyl-CoA
-
0.002
hexadecanoyl-CoA
-
0.0028
octadecanoyl-CoA
-
0.0061
oleoyl-CoA
-
0.0045
palmitoleoyl-CoA
-
0.0016
tetradecanoyl-CoA
-
0.002 - 0.0092
Arachidonoyl-CoA
0.0358
decanoyl-CoA
-
0.0036 - 0.0076
dodecanoyl-CoA
0.002
eicosanoyl-CoA
-
0.0036 - 0.0064
hexadecanoyl-CoA
0.0024
octadecanoyl-CoA
-
0.014
octanoyl-CoA
pH 7.4, 30°C
0.0041 - 0.0088
oleoyl-CoA
0.0024
palmitoleoyl-CoA
-
0.0028
tetradecanoyl-CoA
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
198
purified native enzyme, substrate palmitoyl-CoA
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
30
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
strong expression. ACOT2 is much more strongly expressed than ACOT1
Manually annotated by BRENDA team
strong expression. ACOT2 is much more strongly expressed than ACOT1
Manually annotated by BRENDA team
strong expression. ACOT2 is much more strongly expressed than ACOT1
Manually annotated by BRENDA team
-
isozyme CTE-I
Manually annotated by BRENDA team
strong expression
Manually annotated by BRENDA team
-
cytosolic acyl-CoA thioester hydrolases are deranged in hippocampus of patients with mesial temperal lobe epilepsy
Manually annotated by BRENDA team
strong expression
Manually annotated by BRENDA team
strong expression
Manually annotated by BRENDA team
weak expression
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ACOT2_HUMAN
483
0
53218
Swiss-Prot
Mitochondrion (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
gel filtration
24000
-
gel filtration
35000
-
x * 35000, SDS-PAGE
36000
x * 36000, SDS-PAGE
40000
43000
n * 43000, enzyme is a dimer or a trimer of MW 100 kDa, SDS-PAGE
70000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oligomer
n * 43000, enzyme is a dimer or a trimer of MW 100 kDa, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
docking studies to the pocket of the catalytic triad Ser 2308, His 2481, and Asp 2338, using palmitate, and fatty acids with chain lengths of 12 to 20 carbon atoms. The ligand binding pocket of the thioesterase domain is a decisive factor in chain length specificity. Binding of palmitate results in the most favorable binding free enrgy among the fatty acids tested. The experimentally amino acids of the catalytic triad Ser2308, His2481, and Asp2338 are located very close to the carboxyl group of palmitate. The close location of Arg2482 to the carboxyl group of palmitate and the catalytic triad implies an important role of this residue in catalysis
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol and palmitoyl-CoA stabilize
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, 1 week
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
22fold
-
recombinant as His-tagged or GST-fusion protein from bacteria
-
recombinant GST-tagged isozymes CTE-I and MTE-I, this one also His-tagged, from Escherichia coli, to homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, chromosome mapping 1p36.2, expression in Escherichia coli
DNA sequence determination and analysis, subcloning in Escherichia coli, expression fused to maltose-binding-protein in Escherichia coli strain DH10B
expression as His-tagged enzyme in Escherichia coli and as GST-fusion protein in bacteria
-
expression in Escherichia coli
-
gene BACH comprises 13 exons through alternative use of exons and splicing, DNA and amino acid sequence determination, expression as green-fluorescent-protein fusion protein in Neuro-2a cells
isozyme PTE-2, DNA sequence determination and analysis
isozymes MTE-I, His-tagged, and CTE-I, both GST-fusion proteins
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bronfman, M.; Leighton, F.
Carnitine acyltransferase and acyl-coenzyme A hydrolase activities in human liver. Quantitative analysis of their subcellular localization
Biochem. J.
224
721-730
1984
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Berge, R.K.; Hagen, L.E.; Farstad, M.
Isolation of palmitoyl-CoA hydrolases from human blood platelets
Biochem. J.
199
639-547
1981
Homo sapiens
Manually annotated by BRENDA team
Poupon, V.; Begue, B.; Gagnon, J.; Dautry-Varsat, A.; Cerf-Bensussan, N.; Benmerah, A.
Molecular cloning and characterization of MT-ACT48, a novel mitochondrial acyl-CoA thioesterase
J. Biol. Chem.
274
19188-19194
1999
Arabidopsis thaliana, Bacillus subtilis, Caenorhabditis elegans, Drosophila melanogaster, Escherichia coli, Haemophilus influenzae, Helicobacter pylori, Homo sapiens, Mus musculus (Q9R0X4), Mus musculus, Oryctolagus cuniculus, Rattus norvegicus
Manually annotated by BRENDA team
Broustas, C.G.; Larkins, L.K.; Uhler, M.D.; Hajra, A.K.
Molecular cloning and expression of cDNA encoding rat brain cytosolic acyl-coenzyme A thioester hydrolase
J. Biol. Chem.
271
10470-10476
1996
Homo sapiens, Rattus norvegicus (Q64559)
Manually annotated by BRENDA team
Yamada, J.; Kurata, A.; Hirata, M.; Taniguchi, T.; Takama, H.; Furihata, T.; Shiratori, K.; Iida, N.; Takagi-Sakuma, M.; Watanabe, T.; Kurosaki, K.; Endo, T.; Suga, T.
Purification, molecular cloning, and genomic organization of human brain long-chain acyl-CoA hydrolase
J. Biochem.
126
1013-1019
1999
Homo sapiens (O00154), Homo sapiens
Manually annotated by BRENDA team
Yamada, J.; Furihata, T.; Tamura, H.; Watanabe, T.; Suga, T.
Long-chain acyl-CoA hydrolase from rat brain cytosol: purification, characterization, and immunohistochemical localization
Arch. Biochem. Biophys.
326
106-114
1996
Bos taurus, Canis lupus familiaris, Cavia porcellus, Homo sapiens, Mesocricetus auratus, Oryctolagus cuniculus, Platyrrhini, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Maloberti, P.; Lozano, R.C.; Mele, P.G.; Cano, F.; Colonna, C.; Mendez, C.F.; Paz, C.; Podesta, E.J.
Concerted regulation of free arachidonic acid and hormone-induced steroid synthesis by acyl-CoA thioesterases and acyl-CoA synthetases in adrenal cells
Eur. J. Biochem.
269
5599-5607
2002
Homo sapiens
Manually annotated by BRENDA team
Jones, J.M.; Nau, K.; Geraghty, M.T.; Erdmann, R.; Gould, S.J.
Identification of peroxisomal acyl-CoA thioesterases in yeast and humans
J. Biol. Chem.
274
9216-9223
1999
Homo sapiens (O14734), Homo sapiens, Saccharomyces cerevisiae (P41903), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Duttaroy, A.K.; Crozet, D.; Taylor, J.; Gordon, M.J.
Acyl-CoA thioesterase activity in human placental choriocarcinoma (BeWo), cells: effects of fatty acids
Prostaglandins
68
43-48
2003
Homo sapiens
Manually annotated by BRENDA team
Cohen, G.B.; Rangan, V.S.; Chen, B.K.; Smith, S.; Baltimore, D.
The human thioesterase II protein binds to a site on HIV-1 Nef critical for CD4 down-regulation
J. Biol. Chem.
275
23097-23105
2000
Homo sapiens
Manually annotated by BRENDA team
Hunt, M.C.; Solaas, K.; Kase, B.F.; Alexson, S.E.
Characterization of an acyl-coA thioesterase that functions as a major regulator of peroxisomal lipid metabolism
J. Biol. Chem.
277
1128-1138
2002
Homo sapiens (O14734), Mus musculus (P58137), Mus musculus
Manually annotated by BRENDA team
Yamada, J.; Kuramochi, Y.; Takagi, M.; Watanabe, T.; Suga, T.
Human brain acyl-CoA hydrolase isoforms encoded by a single gene
Biochem. Biophys. Res. Commun.
299
49-56
2002
Homo sapiens (O00154), Homo sapiens
Manually annotated by BRENDA team
Yang, J.W.; Czech, T.; Yamada, J.; Csaszar, E.; Baumgartner, C.; Slavc, I.; Lubec, G.
Aberrant cytosolic acyl-CoA thioester hydrolase in hippocampus of patients with mesial temporal lobe epilepsy
Amino Acids
27
269-275
2004
Homo sapiens
Manually annotated by BRENDA team
Takagi, M.; Suto, F.; Suga, T.; Yamada, J.
Sterol regulatory element-binding protein-2 modulates human brain acyl-CoA hydrolase gene transcription
Mol. Cell. Biochem.
275
199-206
2005
Homo sapiens
Manually annotated by BRENDA team
Hunt, M.C.; Rautanen, A.; Westin, M.A.; Svensson, L.T.; Alexson, S.E.
Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs
FASEB J.
20
1855-1864
2006
Homo sapiens (P49753), Homo sapiens (Q86TX2), Homo sapiens
Manually annotated by BRENDA team
Kim, S.J.; Zhang, Z.; Sarkar, C.; Tsai, P.C.; Lee, Y.C.; Dye, L.; Mukherjee, A.B.
Palmitoyl protein thioesterase-1 deficiency impairs synaptic vesicle recycling at nerve terminals, contributing to neuropathology in humans and mice
J. Clin. Invest.
118
3075-3086
2008
Mus musculus, Homo sapiens (P50897)
Manually annotated by BRENDA team
Cheng, F.; Wang, Q.; Chen, M.; Quiocho, F.A.; Ma, J.
Molecular docking study of the interactions between the thioesterase domain of human fatty acid synthase and its ligands
Proteins
70
1228-1234
2008
Homo sapiens
Manually annotated by BRENDA team
Cheng, F.; Wang, Q.; Chen, M.; Quiocho, F.A.; Ma, J.
Molecular docking study of the interactions between the thioesterase domain of human fatty acid synthase and its ligands
Proteins Struct. Funct. Bioinform.
70
1228-1234
2008
Homo sapiens
Manually annotated by BRENDA team