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Information on EC 3.1.2.20 - acyl-CoA hydrolase and Organism(s) Homo sapiens and UniProt Accession O14734

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.2 Thioester hydrolases
                3.1.2.20 acyl-CoA hydrolase
IUBMB Comments
Broad specificity for medium- to long-chain acyl-CoA. Insensitive to NAD+ (cf. EC 3.1.2.19 ADP-dependent medium-chain-acyl-CoA hydrolase)
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: O14734
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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
acyl-coa hydrolase, them2, type ii thioesterase, them1, acot11, them4, acot13, thioesterase superfamily member 2, te ii, thioesterase 2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACH1
-
-
-
-
ACH2
-
-
-
-
ACT
-
-
-
-
acyl CoA hydrolase
-
-
-
-
acyl coenzyme A hydrolase
-
-
-
-
acyl coenzyme A thioesterase
-
-
-
-
acyl-CoA thioesterase
acyl-CoA thioesterase (ACOT2)
-
-
brain acyl-CoA hydrolase
-
-
-
-
fatty acyl thioesterase I
-
-
-
-
HIV-Nef associated acyl coA thioesterase
-
-
-
-
hTHEM2
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
-
-
-
-
long-chain acyl-CoA hydrolase
-
-
mitochondrial acyl-CoA thioesterase
-
-
-
-
palmitoyl coenzyme A hydrolase
-
-
-
-
palmitoyl thioesterase
-
-
-
-
palmitoyl-CoA deacylase
-
-
-
-
palmitoyl-CoA hydrolase
-
-
-
-
palmityl coenzyme A deacylase
-
-
-
-
palmityl thioesterase
-
-
-
-
palmityl thioesterase I
-
-
-
-
palmityl thioesterase II
-
-
-
-
TE
-
-
-
-
TE-II
-
-
-
-
thioesterase 2
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thioesterase B
-
-
-
-
thioesterase II
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-
-
-
type-II acyl-CoA thioesterase
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-
very long chain acyl-CoA thioesterase
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-
-
-
ZAP128
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acyl-CoA + H2O = CoA + a carboxylate
show the reaction diagram
based on the results of quantum mechanics/molecular mechanics metadynamics techniques simulations, it is demonstrated that hotdog-fold hTHEM2 follows a simple mechanism in which a water molecule directly attacks the carbonyl carbon atom to cleave the thioester bond without requiring an enzyme-substrate covalent intermediate the reaction, providing evidence for the formation of a tetrahedral-like transition state
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of thioester
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-
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PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA hydrolase
Broad specificity for medium- to long-chain acyl-CoA. Insensitive to NAD+ (cf. EC 3.1.2.19 ADP-dependent medium-chain-acyl-CoA hydrolase)
CAS REGISTRY NUMBER
COMMENTARY hide
37270-64-7
EC 3.1.2.2
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
-
-
-
?
2-butenoyl-CoA + H2O
CoA + 2-butenoate
show the reaction diagram
-
-
-
?
3,4-dihydroxyphenylacetyl-CoA + H2O
CoA + 3,4-dihydroxyphenylacetate
show the reaction diagram
-
-
-
?
3,5-dihydroxyphenylacetyl-CoA + H2O
CoA + 3,5-dihydroxyphenylacetate
show the reaction diagram
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + H2O
CoA + 3-hydroxy-3-methylglutarate
show the reaction diagram
-
-
-
?
3-hydroxybenzoyl-CoA + H2O
CoA + 3-hydroxybenzoate
show the reaction diagram
-
-
-
?
3-hydroxyphenylacetyl-CoA + H2O
CoA + 3-hydroxyphenylacetate
show the reaction diagram
-
-
-
?
4-chlorobenzoyl-CoA + H2O
CoA + 4-chlorobenzoate
show the reaction diagram
-
-
-
?
4-hydroxyphenylacetyl-CoA + H2O
CoA + 4-hydroxyphenylacetate
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
beta-hydroxybutyryl-CoA + H2O
CoA + beta-hydroxybutyrate
show the reaction diagram
-
-
-
?
beta-methylcrotonyl-CoA + H2O
CoA + beta-methylcrotonate
show the reaction diagram
-
-
-
?
crotonyl-CoA + H2O
CoA + crotonate
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
-
-
?
glutaryl-CoA + H2O
CoA + glutarate
show the reaction diagram
-
-
-
?
hexadecanoyl-CoA + H2O
CoA + hexadecanoate
show the reaction diagram
hexanoyl-CoA + H2O
CoA + hexanoate
show the reaction diagram
-
molecular dynamic simulations are carried out on the X-ray structure 3F5O with hexanoyl-CoA as the substrate
-
-
?
lauroyl-CoA + H2O
CoA + laurate
show the reaction diagram
-
-
-
?
linolenoyl-CoA + H2O
CoA + linolenoate
show the reaction diagram
-
-
-
?
linoleoyl-CoA + H2O
CoA + linolate
show the reaction diagram
-
-
-
?
linoleoyl-CoA + H2O
CoA + linoleate
show the reaction diagram
malonyl-CoA + H2O
CoA + malonate
show the reaction diagram
-
-
-
?
methylmalonyl-CoA + H2O
CoA + methylmalonate
show the reaction diagram
-
-
-
?
myristoyl-CoA + H2O
CoA + myristate
show the reaction diagram
-
-
-
?
myristoyl-CoA + H2O
CoA + myristic acid
show the reaction diagram
-
-
-
?
n-butyryl-CoA + H2O
CoA + n-butanoate
show the reaction diagram
-
-
-
-
?
n-butyryl-CoA + H2O
CoA + n-butyrate
show the reaction diagram
-
-
-
?
n-decanoyl-CoA + H2O
CoA + n-decanoate
show the reaction diagram
-
-
-
?
n-hexanoyl-CoA + H2O
CoA + n-hexanoate
show the reaction diagram
-
-
-
?
n-octanoyl-CoA + H2O
CoA + n-octanoate
show the reaction diagram
-
-
-
?
n-propionyl-CoA + H2O
CoA + n-propionate
show the reaction diagram
-
-
-
?
nafamostat + H2O
6-hydroxynaphthalene-2-carboximidamide + 4-carbamidamidobenzoic acid
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
palmitoleoyl-CoA + H2O
CoA + palmitoleate
show the reaction diagram
-
-
-
?
palmitoleoyl-CoA + H2O
CoA + palmitoleoate
show the reaction diagram
-
-
-
?
palmitoyl-CoA + H2O
CoA + palmitate
show the reaction diagram
phenylacetyl-CoA + H2O
CoA + phenylacetate
show the reaction diagram
-
-
-
?
stearoyl-CoA + H2O
CoA + stearate
show the reaction diagram
succinyl-CoA + H2O
CoA + succinate
show the reaction diagram
-
-
-
?
tetradecanoyl-CoA + H2O
CoA + tetradecanoate
show the reaction diagram
-
-
-
?
tiglyl-CoA + H2O
CoA + (2E)-2-methylbut-2-enoate
show the reaction diagram
-
-
-
?
vaccenoyl-CoA + H2O
CoA + vaccenoate
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
desulfoCoA
-
Nafamostat
-
competitive inhibition of palmitoyl-CoA hydrolytic activity
NGDA
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isozymes CTE-I and MTE-I
p-chloromercuribenzoic acid
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palmitoyl-CoA
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0.1 mM, 67% inhibition of nafamostat
phenylacetylmethyl-CoA
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phenylmethylsulfonyl fluoride
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0.1 mM, 43% inhibition of nafamostat hydrolysis
undecan-2-one-CoA
-
additional information
-
no inhibition by acetyl-CoA, diisopropyl fluorophosphate and bis(p-nitrophenyl)phosphate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTH
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-
-
bovine serum albumin
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-
-
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
0.22
2-butenoyl-CoA
wild-type protein, pH7.5, 25°C
0.01
3,4-dihydroxyphenylacetyl-CoA
wild-type protein, pH7.5, 25°C
0.025
3,5-dihydroxyphenylacetyl-CoA
wild-type protein, pH7.5, 25°C
2.9
3-hydroxy-3-methylglutaryl-CoA
wild-type protein, pH7.5, 25°C
0.032
3-hydroxybenzoyl-CoA
wild-type protein, pH7.5, 25°C
0.026 - 0.9
3-hydroxyphenylacetyl-CoA
0.13
4-chlorobenzoyl-CoA
wild-type protein, pH7.5, 25°C
0.049
4-hydroxyphenylacetyl-CoA
wild-type protein, pH7.5, 25°C
0.29
acetyl-CoA
wild-type protein, pH7.5, 25°C
0.002 - 0.02
Arachidonoyl-CoA
0.11
beta-hydroxybutyryl-CoA
wild-type protein, pH7.5, 25°C
0.12
beta-methylcrotonyl-CoA
wild-type protein, pH7.5, 25°C
0.18
crotonyl-CoA
wild-type protein, pH7.5, 25°C
0.0076
dodecanoyl-CoA
pH 7.4, 30°C
0.67
glutaryl-CoA
wild-type protein, pH7.5, 25°C
0.0064
hexadecanoyl-CoA
pH 7.4, 30°C
0.0099
lauroyl-CoA
wild-type protein, pH7.5, 25°C
0.0154
linolenoyl-CoA
pH 7.5, 37°C, wild-type
0.0042 - 0.31
linoleoyl-CoA
0.28
malonyl-CoA
wild-type protein, pH7.5, 25°C
0.21
methylmalonyl-CoA
wild-type protein, pH7.5, 25°C
0.005 - 0.009
myristoyl-CoA
0.6
n-butyryl-CoA
wild-type protein, pH7.5, 25°C
0.0049
n-decanoyl-CoA
wild-type protein, pH7.5, 25°C
0.07
n-hexanoyl-CoA
wild-type protein, pH7.5, 25°C
0.026
n-octanoyl-CoA
wild-type protein, pH7.5, 25°C
0.19
n-propionyl-CoA
wild-type protein, pH7.5, 25°C
0.014
octanoyl-CoA
pH 7.4, 30°C
0.0088 - 0.009
oleoyl-CoA
0.009 - 0.026
palmitoleoyl-CoA
0.0024 - 0.016
palmitoyl-CoA
0.24
phenylacetyl-CoA
wild-type protein, pH7.5, 25°C
0.0042 - 0.02
stearoyl-CoA
0.014
succinyl-CoA
-
0.25
tiglyl-CoA
wild-type protein, pH7.5, 25°C
0.0029
vaccenoyl-CoA
pH 7.5, 37°C, wild-type
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.014
2-butenoyl-CoA
wild-type protein, pH7.5, 25°C
0.19
3,4-dihydroxyphenylacetyl-CoA
wild-type protein, pH7.5, 25°C
0.19
3,5-dihydroxyphenylacetyl-CoA
wild-type protein, pH7.5, 25°C
0.079
3-hydroxy-3-methylglutaryl-CoA
wild-type protein, pH7.5, 25°C
0.011
3-hydroxybenzoyl-CoA
wild-type protein, pH7.5, 25°C
0.007 - 1.4
3-hydroxyphenylacetyl-CoA
0.0032
4-chlorobenzoyl-CoA
wild-type protein, pH7.5, 25°C
0.14
4-hydroxyphenylacetyl-CoA
wild-type protein, pH7.5, 25°C
0.054
acetyl-CoA
wild-type protein, pH7.5, 25°C
0.022 - 1.4
Arachidonoyl-CoA
0.18
beta-hydroxybutyryl-CoA
wild-type protein, pH7.5, 25°C
0.023
beta-methylcrotonyl-CoA
wild-type protein, pH7.5, 25°C
0.0076
crotonyl-CoA
wild-type protein, pH7.5, 25°C
0.05
glutaryl-CoA
wild-type protein, pH7.5, 25°C
0.019
lauroyl-CoA
wild-type protein, pH7.5, 25°C
13.3
linolenoyl-CoA
pH 7.5, 37°C, wild-type
0.017 - 12.2
linoleoyl-CoA
0.066
malonyl-CoA
wild-type protein, pH7.5, 25°C
0.083
methylmalonyl-CoA
wild-type protein, pH7.5, 25°C
0.02 - 19.7
myristoyl-CoA
0.047
n-butyryl-CoA
wild-type protein, pH7.5, 25°C
0.016
n-decanoyl-CoA
wild-type protein, pH7.5, 25°C
0.022
n-hexanoyl-CoA
wild-type protein, pH7.5, 25°C
0.0047
n-octanoyl-CoA
wild-type protein, pH7.5, 25°C
0.036
n-propionyl-CoA
wild-type protein, pH7.5, 25°C
0.011
oleoyl-CoA
wild-type protein, pH7.5, 25°C
0.017 - 11.5
palmitoleoyl-CoA
0.0044 - 16.6
palmitoyl-CoA
0.084
phenylacetyl-CoA
wild-type protein, pH7.5, 25°C
0.011 - 1.2
stearoyl-CoA
0.02
tiglyl-CoA
wild-type protein, pH7.5, 25°C
1.8
vaccenoyl-CoA
pH 7.5, 37°C, wild-type
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.064
2-butenoyl-CoA
wild-type protein, pH7.5, 25°C
18
3,4-dihydroxyphenylacetyl-CoA
wild-type protein, pH7.5, 25°C
7.9
3,5-dihydroxyphenylacetyl-CoA
wild-type protein, pH7.5, 25°C
0.027
3-hydroxy-3-methylglutaryl-CoA
wild-type protein, pH7.5, 25°C
0.35
3-hydroxybenzoyl-CoA
wild-type protein, pH7.5, 25°C
0.023 - 35
3-hydroxyphenylacetyl-CoA
0.025
4-chlorobenzoyl-CoA
wild-type protein, pH7.5, 25°C
2.9
4-hydroxyphenylacetyl-CoA
wild-type protein, pH7.5, 25°C
0.18
acetyl-CoA
wild-type protein, pH7.5, 25°C
1.1 - 73
Arachidonoyl-CoA
1.6
beta-hydroxybutyryl-CoA
wild-type protein, pH7.5, 25°C
0.19
beta-methylcrotonyl-CoA
wild-type protein, pH7.5, 25°C
0.47
crotonyl-CoA
wild-type protein, pH7.5, 25°C
0.75
glutaryl-CoA
wild-type protein, pH7.5, 25°C
1.9
lauroyl-CoA
wild-type protein, pH7.5, 25°C
860
linolenoyl-CoA
pH 7.5, 37°C, wild-type
0.054 - 2900
linoleoyl-CoA
0.24
malonyl-CoA
wild-type protein, pH7.5, 25°C
0.39
methylmalonyl-CoA
wild-type protein, pH7.5, 25°C
4 - 2300
myristoyl-CoA
0.078
n-butyryl-CoA
wild-type protein, pH7.5, 25°C
3.3
n-decanoyl-CoA
wild-type protein, pH7.5, 25°C
0.31
n-hexanoyl-CoA
wild-type protein, pH7.5, 25°C
0.18
n-octanoyl-CoA
wild-type protein, pH7.5, 25°C
0.19
n-propionyl-CoA
wild-type protein, pH7.5, 25°C
1.3
oleoyl-CoA
wild-type protein, pH7.5, 25°C
1.9 - 430
palmitoleoyl-CoA
0.28 - 6900
palmitoyl-CoA
0.35
phenylacetyl-CoA
wild-type protein, pH7.5, 25°C
5.5 - 290
stearoyl-CoA
0.082
tiglyl-CoA
wild-type protein, pH7.5, 25°C
540
vaccenoyl-CoA
pH 7.5, 37°C, wild-type
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.009
desulfoCoA
-
0.164
Nafamostat
-
-
0.5
phenylacetylmethyl-CoA
-
0.003 - 0.0033
undecan-2-one-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
37
assay at
25
-
assay at
30
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
isozyme CTE-I
Manually annotated by BRENDA team
weak expression
Manually annotated by BRENDA team
strongest expression in liver and kidney
Manually annotated by BRENDA team
weak expression
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ACOT8_HUMAN
319
0
35914
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36000
x * 36000, SDS-PAGE
100000
gel filtration
24000
-
gel filtration
35000
-
x * 35000, 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
?
x * 36000, SDS-PAGE
dimer
gel filtration
homodimer
gel filtration
homotetramer
oligomer
n * 43000, enzyme is a dimer or a trimer of MW 100 kDa, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme forms homodimers in crystals. DELTA1-34 deletion mutant is crystallized to 1.45 A resolution
enzyme forms homodimers in crystals. DELTA1-34 deletion mutant is crystallized to 1.6 A resolution
hanging drop vapor diffusion method
sitting-drop vapor diffusion method
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D167A
D167 is a key catalytic residue. D167A no longer displays catalytic activity
D65A
active site residue
D65E
active site residue
D65N
active site residue
DELTA1-37
mutant lacking the first 37 N-terminal amino acids is excluded from mitochondria
H134A
reduction in catalytic efficiency
H137A
conserved among vertebrate homologues
H56A
active site residue
K136A
relatively small perturbation in catalytic efficiency
N50A
active site residue
S83A
active site residue
T69A
active site residue
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
-
immobilized metal ion affinity chromatography (Ni2+), gelfiltration
-
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
-
using Ni-NTA chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, subcloning in Escherichia coli, expression fused to maltose-binding-protein in Escherichia coli strain DH10B
analysis carried out with a deletion mutant lacking the first 35 amino acids DELTA1-34. Expressed in Escherichia coli as a His-tagged fusion protein
DNA sequence determination and analysis, chromosome mapping 1p36.2, expression in Escherichia coli
expression as His-tagged enzyme in Escherichia coli and as GST-fusion protein in bacteria
-
expression in Escherichia coli
-
His-tagged version expressed in Escherichia coli BL21(DE3)
His-taggend version of residue 46-483 expressed in Escherichia coli BL21 (DE3 Rosetta)
-
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), 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
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), Saccharomyces cerevisiae (P41903)
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.; Ruiter, J.; Mooyer, P.; van Roermond, C.W.T.; Ofman, R.; Ijlst, L.; Wanders, R.J.A.
Identification of fatty acid oxidation disorder patients with lowered acyl-CoA thioesterase activity in human skin fibroblasts
Eur. J. Clin. Invest.
35
38-46
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 (Q3I5F7)
Manually annotated by BRENDA team
Yamaori, S.; Ukena, E.; Fujiyama, N.; Funahashi, T.; Kimura, T.; Yamamoto, I.; Ohshima, T.; Matsumura, K.; Oda, M.; Watanabe, K.
Nafamostat is hydrolysed by human liver cytosolic long-chain acyl-CoA hydrolase
Xenobiotica
37
260-270
2007
Homo sapiens
Manually annotated by BRENDA team
Mandel, C.R.; Tweel, B.; Tong, L.
Crystal structure of human mitochondrial acyl-CoA thioesterase (ACOT2)
Biochem. Biophys. Res. Commun.
385
630-633
2009
Homo sapiens
Manually annotated by BRENDA team
Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.
The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis
Biochemistry
48
1293-1304
2009
Homo sapiens (Q9NPJ3), Homo sapiens
Manually annotated by BRENDA team
Cantu, D.C.; Ardevol, A.; Rovira, C.; Reilly, P.J.
Molecular mechanism of a hotdog-fold acyl-CoA thioesterase
Chemistry
20
9045-9051
2014
Homo sapiens
Manually annotated by BRENDA team
Zhuravleva, E.; Gut, H.; Hynx, D.; Marcellin, D.; Bleck, C.K.; Genoud, C.; Cron, P.; Keusch, J.J.; Dummler, B.; Esposti, M.D.; Hemmings, B.A.
Acyl coenzyme A thioesterase Them5/Acot15 is involved in cardiolipin remodeling and fatty liver development
Mol. Cell. Biol.
32
2685-2697
2012
Mus musculus, Homo sapiens (Q5T1C6)
Manually annotated by BRENDA team