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

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This record set is specific for:
Homo sapiens


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota


The taxonomic range for the selected organisms is: Homo sapiens

EC NUMBER
COMMENTARY hide
3.1.2.2
-
RECOMMENDED NAME
GeneOntology No.
palmitoyl-CoA hydrolase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of thioester
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
bacterial bioluminescence
-
-
acyl-CoA hydrolysis
-
-
stearate biosynthesis III (fungi)
-
-
stearate biosynthesis I (animals and fungi)
-
-
suberin monomers biosynthesis
-
-
oleate biosynthesis II (animals and fungi)
-
-
palmitate biosynthesis I (animals and fungi)
-
-
cutin biosynthesis
-
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sporopollenin precursors biosynthesis
-
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Fatty acid elongation
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Biosynthesis of unsaturated fatty acids
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Biosynthesis of secondary metabolites
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-
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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 SUBSTRATES
NATURAL PRODUCTS
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
?
-
INHIBITORS
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
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both conjugated and gamma-linoleic acid, increase activity
additional information
-
no stimulation of activity by docosahexaenoic and eisosapentaenoic acids
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002 - 0.0041
Arachidonoyl-CoA
0.0092
arachidoyl-CoA
pH 7.4, 30°C
0.0358 - 0.0403
decanoyl-CoA
0.0036 - 0.089
Dodecanoyl-CoA
0.002 - 0.0048
eicosanoyl-CoA
0.002 - 0.0064
hexadecanoyl-CoA
0.0024 - 0.0028
Octadecanoyl-CoA
0.014
Octanoyl-CoA
pH 7.4, 30°C
0.0041 - 0.0088
oleoyl-CoA
0.0024 - 0.0045
palmitoleoyl-CoA
0.0016 - 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
8
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
30
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
isozyme CTE-I
Manually annotated by BRENDA team
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i.e. BeWo cells; placental
Manually annotated by BRENDA team
strong expression; strong expression. ACOT2 is much more strongly expressed than ACOT1
Manually annotated by BRENDA team
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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; strong expression. ACOT2 is much more strongly expressed than ACOT1
Manually annotated by BRENDA team
weak expression
Manually annotated by BRENDA team
additional information
palmitoyl-CoA hydrolase activity is widespread in all tissues
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
Homo sapiens;
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24000
-
gel filtration
35000
-
x * 35000, SDS-PAGE
36000
x * 36000, SDS-PAGE
43000
n * 43000, enzyme is a dimer or a trimer of MW 100 kDa, SDS-PAGE
70000
-
gel filtration
100000
gel filtration
SUBUNITS
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
-
from brain
recombinant as His-tagged or GST-fusion protein from bacteria
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recombinant GST-tagged isozymes CTE-I and MTE-I, this one also His-tagged, from Escherichia coli, to homogeneity
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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
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expression in Escherichia coli
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expression in Escherichia coli; isozymes MTE-I, His-tagged, and CTE-I, both GST-fusion proteins
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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