Information on EC 3.1.2.1 - acetyl-CoA hydrolase

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

EC NUMBER
COMMENTARY hide
3.1.2.1
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RECOMMENDED NAME
GeneOntology No.
acetyl-CoA hydrolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + H2O = CoA + acetate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of thioester
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
acetyl CoA biosynthesis
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Pyruvate metabolism
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA hydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
9027-54-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain strain BY47410
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
millet
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
rhesus
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain SC5314
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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complementation of an ach1 mutant with the coaT gene reverses the growth defect on acetate confirming the in vivo function of Ach1p as a CoA-transferase. Growth of an ach1p deletion mutant on the carboxylic acids lactate and pyruvate reveals no phenotype
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-butenoyl-CoA
3-butenoate + CoA
show the reaction diagram
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?
acetoacetyl-CoA
acetoacetate + CoA
show the reaction diagram
acetoacetyl-CoA + H2O
CoA + acetoacetate
show the reaction diagram
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-
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?
acetyl-CoA + H2O
?
show the reaction diagram
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
butanoyl-CoA + H2O
CoA + butanoate
show the reaction diagram
about 20% of the activity with acetyl-CoA
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?
butyryl-CoA + H2O
butanoate + CoA
show the reaction diagram
butyryl-CoA + H2O
CoA + butanoate
show the reaction diagram
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?
crotonyl-CoA
trans-2-butenoate + CoA
show the reaction diagram
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-
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?
decanoyl-CoA
decanoate + CoA
show the reaction diagram
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?
glutaryl-CoA
glutarate + CoA
show the reaction diagram
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?
H2 + CO2 + CH3-H4SPt + CoASH
acetyl-CoA + H4SPt + H2O
show the reaction diagram
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?
hexanoyl-CoA
hexanoate + CoA
show the reaction diagram
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?
hexanoyl-CoA + H2O
CoA + hexanoate
show the reaction diagram
about 10% of the activity with acetyl-CoA
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?
lauroyl-CoA
lauroate + CoA
show the reaction diagram
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-
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?
malonyl-CoA
malonate + CoA
show the reaction diagram
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?
octanoyl-CoA
octanoate + CoA
show the reaction diagram
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?
oleoyl-CoA
oleate + CoA
show the reaction diagram
palmitoyl-CoA
palmitate + CoA
show the reaction diagram
propionyl-CoA + H2O
CoA + propionate
show the reaction diagram
succinyl-CoA
succinate + CoA
show the reaction diagram
valeryl-CoA
pentanoate + CoA
show the reaction diagram
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?
additional information
?
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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
acetyl-CoA + H2O
?
show the reaction diagram
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
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enzyme is dependent on
folate
NADH
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activates
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CaCl2
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more pronounced stimulation
MgCl2
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slight stimulation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2-dimyristoyl phosphatidylglycerol
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1-oleoyl-2-lysophosphatidic acid
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2,3-Butanedione
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AMP
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inhibits at 50 mM the stimulation of the enzyme by ATP
DL-lipoic acid
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EDTA
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enhances the inactivation of the enzyme in the presence of iron and L-ascorbic acid
glucose
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enzyme activity is reduced in glucose-containing medium, the expression of ACH1 gene is repressed by glucose
Hydroxycitrate
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L-ascorbic acid
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inactivation of the purified enzyme by incubation at 37C, enhancing by addition of Cu2+, Fe2+ and Fe3+
NADH
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0.001 mM inhibits
naphthoquinone
palmitoyl-CoA
Phenylglyoxal
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phosphate
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50% inhibition
phosphatidic acid
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Triton X-100
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valeryl-CoA
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2-dimyristoylphosphatidylglycerol
activates mutant form lacking START domain
1-oleoyl-2-lysophosphatidylglycerol
activates mutant form lacking START domain
3-thiadicarboxylic acid
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activity increases
acetate
acetyl-CoA
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at time of rewarming 0.5 mM acetyl-CoA restores the activity about 50%
adenosine 5'-[beta,gamma-imido]triphosphate
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with adoPP[CH2]P a 2.5fold activation of the cold-labile cytosolic enzyme at 2 mM, with adoPP[NH]P a 3.7fold activation respectively
ADP
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0.0001 mM activates
albumin
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albumin enhances the reactivation of the monomeric form
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alpha-(p-chlorophenoxy)isobutyric acid
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high activity of the enzyme for over 72h
CTP
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counteracts the inhibition of the cold-labile cytosolic enzyme by ADP
cystamine
diacetylcystamine
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activation
diphosphate
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450 mM pyrophosphate restores the activity about 80% at time of rewarming
disulfide peptides
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activation
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dithiothreitol
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oxidized, activation
DL-beta-hydroxy-butyrate
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hydrolase increases 50-70% by 100 mM DL-beta-hydroxy-butyrate
Dopa
activates mutant form lacking START domain
ethyl chlorophenoxyisobutyrate
Ferredoxin
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dependent on
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fluoroacetate
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hydrolase increases 50-70% by 100 mM fluoroacetate
galactose
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higher activity
GDP
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at 0.5 mM nucleoside phosphate 100% stimulation in Trypanosoma brucei brucei MIAG 103 and 75% in Trypanosoma brucei brucei 427
glycerol
GSH
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activation
GSSG
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activation
L(-)-carnitine
NADH
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stimulation
Oxytocin
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activation
penicillamine disulfide
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activation
phosphate
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920 mM phosphate restores the activity about 80% at time of rewarming
phosphatidic acid
activates mutant form lacking START domain
pressinoic acid
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activation
Propionate
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hydrolase increases 50-70% by 250 mM propionate
Somatostatin
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like[tyr1]somatostatin and tyr-somatostatin the most potent activator
sulfur substituted fatty acids
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rats fed a high-carbohydrate diet
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tetradecylthioacetic acid
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activity increases
triiodothyronine
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activity increases
Tyr-somatostatin
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activation
Vasopressin
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activation
[arg8]vasotocin
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activation
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[tyr1]somatostatin
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activation
additional information
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the enzyme is induced in mitochondria by di(2-ethylhexyl)phthalate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.33
acetoacetyl-CoA
pH 8, 37C, Vmax: 30 micromol/min/mg, wild-type
0.00006 - 15
acetyl-CoA
0.41
Butyryl-CoA
pH 8, 37C, Vmax: 44 micromol/min/mg, wild-type
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.99 - 7.26
acetyl-CoA
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.017
CoA
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pH 7.4
0.0145
GDP
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15
pH 8, 37C, mutant form lacking START domain
74.4
pH 8, 37C, wild-type
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.3
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
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activity enhanced at higher pH
7.5 - 8.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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most of the Ach1p activity is distributed with mitochondria and little in the cytoplasm
Manually annotated by BRENDA team
additional information
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extramitochondrial
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
58370
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cDNA sequence
68000
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SDS-PAGE gel electrophoresis, the cold labile cytosolic acetyl-CoA hydrolase
88000
gel filtration, mutant form lacking START domain, pre-incubation with ATP, dimer
124000
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gel filtration
135000
136000
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gel filtration, cytosolic native enzyme in the presence of 2 mM ATP, dimeric form
155000
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gel filtration
157000
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gel filtration, mitochondrial enzyme
160000
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sedimentation velocity in a sucrose density gradient
182000
gel filtration, mutant form lacking START domain, pre-incubation with ATP, tetramer
232000
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gel filtration
240000
245000
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gel filtration, cytosolic native enzyme in the presence of 2 mM ATP, tetrameric form
322000
gel filtration, wild-type, pre-incubation with ATP, tetramer
340000
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equilibrium centrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 43000, SDS-PAGE
hexamer
crystal structure
monomer
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sucrose density gradient centrifugation
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA hydrolase is crystallized using the hanging-drop vapour-diffusion technique at pH 8.5 and 17C using ammonium phosphate as a precipitant. Optimized crystals diffract to 2.0 A resolution
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
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purified dimeric enzyme fairly stable in potassium phosphate buffer of pH 7.0-8.0
94477
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
sulfhydryl compounds, glycerol and high ionic strength in the range of 0.2-0.4 mM enhances stability during purification
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
L-ascorbic acid and Cu2+, inactivation irreversible
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94480
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4 months, 4C
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2.4fold; 4fold
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27.2fold from liver mitochondria in a 5-step chromatographical procedure
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; 1375fold
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; 14000fold
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; 4600fold
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recombinant enzyme
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using Ni-NTA chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acu-8 gene mutant, sequence resembles Saccharomyces cerevisiae glucose-repressible acetyl-CoA-hydrolase
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expressed in Escherichia coli as a His-tagged fusion protein
expression in Escherichia coli
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expression in Sf9 cells
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expression in Spodoptera frugiperda
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functional overexpression of the enzyme in Nicotiana tabacum cv. Samsun mitochondria using the Agrobacterium transfection system
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functionally expressed in Sf9 insect cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ACOT12 mRNA and protein levels in rat primary hepatocytes decrease following treatment with insulin
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G277S/G279S
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mutant enzyme shows less than 5% of the activity of the wild-type enzyme
G393E/G395S
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mutant enzyme shows less than 5% of the activity of the wild-type enzyme
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
from cold inactivation
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Show AA Sequence (273 entries)
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