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
3.1.2.1
-
RECOMMENDED NAME
GeneOntology No.
acetyl-CoA hydrolase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + H2O = CoA + acetate
show the reaction diagram
-
-
-
-
acetyl-CoA + H2O = CoA + acetate
show the reaction diagram
the bifunctional enzyme is identical with a 3-ketoacyl-CoA thiolase isozyme, i.e. THL, EC 2.3.1.9, determined by internal peptide amino acid sequence comparison
-
acetyl-CoA + H2O = CoA + acetate
show the reaction diagram
as shown by proton nuclear magnetic resonance spectroscopy the disappearance of acetyl CH3 from acetyl Coenzyme A occurrs concomitantly with the appearance of a CH3 peak corresponding to that of free acetate and suggesting that folate is not acetylated during the reaction
-
acetyl-CoA + H2O = CoA + acetate
show the reaction diagram
as shown by proton nuclear magnetic resonance spectroscopy the disappearance of acetyl CH3 from acetyl Coenzyme A occurres concomitantly with the appearance of a CH3 peak corresponding to that of free acetate and suggesting that folate is not acetylated during the reaction
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of thioester
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
acetyl CoA biosynthesis
-
-
Pyruvate metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA hydrolase
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
(HUMN)NAT1
-
-
(MOUSE)NAT2
-
-
Acetate utilization protein
-
-
-
-
acetyl CoA hydrolase
-
-
acetyl coenzyme A acylase
-
-
-
-
acetyl coenzyme A deacylase
-
-
-
-
acetyl coenzyme A hydrolase
-
-
-
-
acetyl-CoA acylase
-
-
-
-
acetyl-CoA deacylase
-
-
-
-
acetyl-CoA decarbonylase synthase enzyme complex
-
-
acetyl-CoA hydrolase
-
-
-
-
acetyl-CoA hydrolase
-
-
acetyl-CoA hydrolase
-
acetyl-CoA hydrolase
-
acetyl-CoA hydrolase
-
acetyl-CoA thiol esterase
-
-
acetyl-CoA thiol esterase
Clostridium aminovalericum T2-7
-
-
-
ACH1
Saccharomyces cerevisiae SC5314
-
-
-
CACH
-
-
human arylamine N-acetyltransferase Type 1
-
-
hydrolase, acetyl coenzyme A
-
-
-
-
mouse arylamine N-acetyltransferase Type 2
-
-
rACH
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9027-54-7
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain strain BY47410
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
millet
-
-
Manually annotated by BRENDA team
rhesus
-
-
Manually annotated by BRENDA team
male Spargue-Dawley rats
-
-
Manually annotated by BRENDA team
strain SC5314
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae SC5314
strain SC5314
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
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)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-butenoyl-CoA
3-butenoate + CoA
show the reaction diagram
-
-
-
?
acetoacetyl-CoA
acetoacetate + CoA
show the reaction diagram
-
-
-
?
acetoacetyl-CoA
acetoacetate + CoA
show the reaction diagram
-
-
-
?
acetoacetyl-CoA
acetoacetate + CoA
show the reaction diagram
-
-
-
?
acetoacetyl-CoA
acetoacetate + CoA
show the reaction diagram
-
-
-
?
acetoacetyl-CoA + H2O
CoA + acetoacetate
show the reaction diagram
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
highly preferred substrate
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
Ach1p may be involved in a novel acetyl-CoA biogenesis and/or acetate utilization in mitochondria and thereby indirectly affect pseudohyphal development in yeast. Not involved in mitochondrial biogenesis
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
the enzyme is responsible for production of free acetate
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
Saccharomyces cerevisiae SC5314
-
-
-
?
acetyl-CoA + H2O
?
show the reaction diagram
-
-
-
-
-
acetyl-CoA + H2O
?
show the reaction diagram
-
-
-
-
-
acetyl-CoA + H2O
?
show the reaction diagram
-
-
-
-
-
acetyl-CoA + H2O
?
show the reaction diagram
-
-
-
-
-
acetyl-CoA + H2O
?
show the reaction diagram
-
-
-
-
-
butanoyl-CoA + H2O
CoA + butanoate
show the reaction diagram
about 20% of the activity with acetyl-CoA
-
?
butyryl-CoA + H2O
butanoate + CoA
show the reaction diagram
-
-
-
?
butyryl-CoA + H2O
butanoate + CoA
show the reaction diagram
-
-
-
?
butyryl-CoA + H2O
butanoate + CoA
show the reaction diagram
-
-
-
?
butyryl-CoA + H2O
butanoate + CoA
show the reaction diagram
-
-
-
?
butyryl-CoA + H2O
butanoate + CoA
show the reaction diagram
-
-
-
?
butyryl-CoA + H2O
butanoate + CoA
show the reaction diagram
-
-
-
?
butyryl-CoA + H2O
butanoate + CoA
show the reaction diagram
-
-
-
?
butyryl-CoA + H2O
butanoate + CoA
show the reaction diagram
-
-
-
?
butyryl-CoA + H2O
butanoate + CoA
show the reaction diagram
-
-
-
?
butyryl-CoA + H2O
CoA + butanoate
show the reaction diagram
-
-
?
crotonyl-CoA
trans-2-butenoate + CoA
show the reaction diagram
-
-
-
?
decanoyl-CoA
decanoate + CoA
show the reaction diagram
-
-
-
?
glutaryl-CoA
glutarate + CoA
show the reaction diagram
-
-
-
?
H2 + CO2 + CH3-H4SPt + CoASH
acetyl-CoA + H4SPt + H2O
show the reaction diagram
-
-
-
?
hexanoyl-CoA
hexanoate + CoA
show the reaction diagram
-
-
-
?
hexanoyl-CoA + H2O
CoA + hexanoate
show the reaction diagram
about 10% of the activity with acetyl-CoA
-
?
lauroyl-CoA
lauroate + CoA
show the reaction diagram
-
-
-
?
octanoyl-CoA
octanoate + CoA
show the reaction diagram
-
-
-
?
octanoyl-CoA
octanoate + CoA
show the reaction diagram
-
-
-
?
oleoyl-CoA
oleate + CoA
show the reaction diagram
-
-
-
?
oleoyl-CoA
oleate + CoA
show the reaction diagram
-
-
-
?
palmitoyl-CoA
palmitate + CoA
show the reaction diagram
-
-
-
?
palmitoyl-CoA
palmitate + CoA
show the reaction diagram
-
-
-
?
propionyl-CoA + H2O
CoA + propionate
show the reaction diagram
-
-
-
?
propionyl-CoA + H2O
CoA + propionate
show the reaction diagram
-
-
-
?
propionyl-CoA + H2O
CoA + propionate
show the reaction diagram
-
-
-
?
propionyl-CoA + H2O
CoA + propionate
show the reaction diagram
-
-
-
?
propionyl-CoA + H2O
CoA + propionate
show the reaction diagram
-
-
-
?
succinyl-CoA
succinate + CoA
show the reaction diagram
-
-
-
?
succinyl-CoA
succinate + CoA
show the reaction diagram
-
-
-
?
succinyl-CoA
succinate + CoA
show the reaction diagram
-
-
-
?
valeryl-CoA
pentanoate + CoA
show the reaction diagram
-
-
-
?
malonyl-CoA
malonate + CoA
show the reaction diagram
-
-
-
?
additional information
?
-
-
substrate and chain-length specificity of the mitochondrial enzyme, overview
-
-
-
additional information
?
-
-
isoform Ach1p catalyzes CoASH transfer from succinyl-CoA to acetate and shows only a minor acetyl-CoA-hydrolase activity. When the activity with different substrate couples is compared to that with propionyl-CoA and acetate, CoA-transferase activity increases by a factor of 3.6 with the couple succinyl-CoA and propionate and by a factor of 7.4 with the couple succinyl-CoA and acetate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
-
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
Ach1p may be involved in a novel acetyl-CoA biogenesis and/or acetate utilization in mitochondria and thereby indirectly affect pseudohyphal development in yeast. Not involved in mitochondrial biogenesis
-
?
acetyl-CoA + H2O
CoA + acetate
show the reaction diagram
-
the enzyme is responsible for production of free acetate
-
?
acetyl-CoA + H2O
?
show the reaction diagram
-
-
-
-
-
acetyl-CoA + H2O
?
show the reaction diagram
-
-
-
-
-
acetyl-CoA + H2O
?
show the reaction diagram
-
-
-
-
-
acetyl-CoA + H2O
?
show the reaction diagram
-
-
-
-
-
acetyl-CoA + H2O
?
show the reaction diagram
-
-
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
enzyme is dependent on
folate
-
folate binds at the enzyme's active site, and facilitate acetyl coenzyme A hydrolysis
NADH
-
activates
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CaCl2
-
more pronounced stimulation
MgCl2
-
slight stimulation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,2-dimyristoyl phosphatidylglycerol
-
-
1-oleoyl-2-lysophosphatidic acid
-
-
2,3-Butanedione
-
-
ADP
-
0.5 mM nucleoside phosphate inhibits for 32% in Trypanosoma brucei brucei MIAG 103 and for 31% in Trypanosoma brucei brucei 427
ADP
-
1-10 mM inhibits
ADP
-
complete inhibition by 2 mM
ADP
-
50% inhibition of the cold-labile cytosolic enzyme at 0.0145 mM
AMP
-
inhibits at 50 mM the stimulation of the enzyme by ATP
ATP
-
0.5 mM nucleoside phosphate inhibits 49% in Trypanosoma brucei brucei 427
ATP
-
0.5 mM nucleoside phosphate inhibits 49% in Trypanosoma brucei brucei 427; 1-10 mM inhibits the enzyme
ATP
-
0.5 mM nucleoside phosphate inhibits 49% in Trypanosoma brucei brucei 427
CoA
-
; competitive
CoA
-
0.1 mM causes over 50% inhibition
CoA
-
-
CoA
-
80% inhibition of the cold-labile cytosolic enzyme at 0.04 mM
DL-lipoic acid
-
-
EDTA
-
enhances the inactivation of the enzyme in the presence of iron and L-ascorbic acid
GDP
-
50% inhibition of the cold-labile cytosolic enzyme at 0.0145 mM
glucose
-
enzyme activity is reduced in glucose-containing medium, the expression of ACH1 gene is repressed by glucose
Hydroxycitrate
-
-
L-ascorbic acid
-
inactivation of the purified enzyme by incubation at 37C, enhancing by addition of Cu2+, Fe2+ and Fe3+
NADH
-
0.001 mM inhibits
naphthoquinone
-
-
palmitoyl-CoA
-
0.0001 mM strongly inhibits
palmitoyl-CoA
-
-
palmitoyl-CoA
-
-
Phenylglyoxal
-
-
phosphate
-
50% inhibition
phosphatidic acid
-
Triton X-100
-
-
valeryl-CoA
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,2-dimyristoylphosphatidylglycerol
activates mutant form lacking START domain
1-oleoyl-2-lysophosphatidylglycerol
activates mutant form lacking START domain
3-thiadicarboxylic acid
-
activity increases
acetate
-
hydrolase increased 3fold by 100-250 mM acetate
acetyl-CoA
-
at time of rewarming 0.5 mM acetyl-CoA restores the activity about 50%
adenosine 5'-[beta,gamma-imido]triphosphate
-
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
-
0.0001 mM activates
albumin
-
albumin enhances the reactivation of the monomeric form
-
alpha-(p-chlorophenoxy)isobutyric acid
-
high activity of the enzyme for over 72h
ATP
-
2 mM increases the hydrolytic rate
ATP
-
at time of rewarming ATP greatly enhances the restoration of the activity, 2 mM ATP restores the enzyme activity about 70%
ATP
-
14fold activation of the cold-labile enzyme at 2 mM
ATP
-
cytosolic enzyme is stimulated, the mitochondrial enzyme seems unaffected
CTP
-
counteracts the inhibition of the cold-labile cytosolic enzyme by ADP
cystamine
-
10 mM activates by a mechanism of disulfide exchange
cystamine
-
-
diacetylcystamine
-
activation
diphosphate
-
450 mM pyrophosphate restores the activity about 80% at time of rewarming
disulfide peptides
-
activation
-
dithiothreitol
-
oxidized, activation
DL-beta-hydroxy-butyrate
-
hydrolase increases 50-70% by 100 mM DL-beta-hydroxy-butyrate
Dopa
activates mutant form lacking START domain
ethyl chlorophenoxyisobutyrate
-
in rats on diet containing 0.5% clofibrate the activity increases 2-3fold
ethyl chlorophenoxyisobutyrate
-
no markable increase on clofibrate treatment
Ferredoxin
-
dependent on
-
fluoroacetate
-
hydrolase increases 50-70% by 100 mM fluoroacetate
galactose
-
higher activity
GDP
-
at 0.5 mM nucleoside phosphate 100% stimulation in Trypanosoma brucei brucei MIAG 103 and 75% in Trypanosoma brucei brucei 427
glycerol
-
-
GSH
-
activation
GSSG
-
activation
GTP
-
4.6fold activation of the cold-labile cytosolic enzyme at 2 mM
NADH
-
stimulation
Oxytocin
-
activation
penicillamine disulfide
-
activation
phosphate
-
920 mM phosphate restores the activity about 80% at time of rewarming
phosphatidic acid
activates mutant form lacking START domain
pressinoic acid
-
activation
Propionate
-
hydrolase increases 50-70% by 250 mM propionate
Somatostatin
-
like[tyr1]somatostatin and tyr-somatostatin the most potent activator
sulfur substituted fatty acids
-
rats fed a high-carbohydrate diet
-
tetradecylthioacetic acid
-
activity increases
triiodothyronine
-
activity increases
Tyr-somatostatin
-
activation
Vasopressin
-
activation
[arg8]vasotocin
-
activation
-
[tyr1]somatostatin
-
activation
additional information
-
the enzyme is induced in mitochondria by di(2-ethylhexyl)phthalate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.33
acetoacetyl-CoA
pH 8, 37C, Vmax: 30 micromol/min/mg, wild-type
0.00006
acetyl-CoA
-
tetrameric enzyme, in presence of 2mM ATP
0.00006
acetyl-CoA
-
-
0.00017
acetyl-CoA
-
dimeric enzyme, in presence of 2mM ATP
0.00017
acetyl-CoA
-
-
0.051
acetyl-CoA
-
-
0.074
acetyl-CoA
-
-
0.075
acetyl-CoA
-
pH 7.4
0.153
acetyl-CoA
-
25C, recombinant enzyme
0.22
acetyl-CoA
-
25C, native enzyme
0.36
acetyl-CoA
pH 8, 37C, Vmax: 125 micromol/min/mg, wild-type; pH 8, 37C, Vmax: 23.4 micromol/min/mg, mutant form lacking START domain
0.4
acetyl-CoA
-
-
0.5
acetyl-CoA
-
in liver mitochondria
15
acetyl-CoA
-
in lysosomes
0.41
Butyryl-CoA
pH 8, 37C, Vmax: 44 micromol/min/mg, wild-type
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.99
acetyl-CoA
Mus musculus
Q9DBK0
pH 8, 37C, mutant form lacking START domain
7.26
acetyl-CoA
Mus musculus
Q9DBK0
pH 8, 37C, wild-type
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.017
CoA
-
pH 7.4
0.0145
GDP
-
cold-labile cytosolic enzyme
0.0145
GDP
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15
pH 8, 37C, mutant form lacking START domain
74.4
pH 8, 37C, wild-type
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.3
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8.5
-
activity enhanced at higher pH
7.5 - 8.5
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
assay at
37
assay at
37
-
warming at 37C after cold exposure is optimal for reactivation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
ACH1 is present at low levels in D-glucose-containing medium, ACH1 expression is almost undetectable when lactate is the sole carbon source
Manually annotated by BRENDA team
additional information
Saccharomyces cerevisiae SC5314
-
ACH1 is present at low levels in D-glucose-containing medium, ACH1 expression is almost undetectable when lactate is the sole carbon source
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
58370
-
cDNA sequence
94486
68000
-
SDS-PAGE gel electrophoresis, the cold labile cytosolic acetyl-CoA hydrolase
94479
88000
gel filtration, mutant form lacking START domain, pre-incubation with ATP, dimer
732297
124000
-
gel filtration
651098
135000
-
gel filtration, dialysis of the enzyme, dimeric form
94475
135000
-
-
94477, 94482
136000
-
gel filtration, cytosolic native enzyme in the presence of 2 mM ATP, dimeric form
94479
155000
-
gel filtration
94468
157000
-
gel filtration, mitochondrial enzyme
94479
160000
-
sedimentation velocity in a sucrose density gradient
94468
182000
gel filtration, mutant form lacking START domain, pre-incubation with ATP, tetramer
732297
232000
-
gel filtration
94487
240000
-
gel filtration
94472
240000
-
-
94475
245000
-
gel filtration, cytosolic native enzyme in the presence of 2 mM ATP, tetrameric form
94479
322000
gel filtration, wild-type, pre-incubation with ATP, tetramer
732297
340000
-
equilibrium centrifugation
94472
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 43000, SDS-PAGE
dimer
-
2 * 62000, SDS-PAGE; 2 * 62017, calculation from nucleotide sequence
dimer
55.7% of mutant form lacking START domain form a mixture of active tetramers (31%) and dimers (23.9%)
dimer
-
2 * 63000, SDS-PAGE
hexamer
crystal structure
monomer
-
sucrose density gradient centrifugation
tetramer
4 * 77000 kDa, 45% of wild-type form active tetramers. 55.7% of mutant form lacking START domain form a mixture of active tetramers (31%) and dimers 23.9%
tetramer
-
4 * 64000, SDS-PAGE
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
LITERATURE
7 - 8
-
purified dimeric enzyme fairly stable in potassium phosphate buffer of pH 7.0-8.0
94477
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4
-
60 min, about 75% loss of activity. Cold-inactivation can partially be abolished through incubation at 37C in presence of 0.16 mM Triton X-100
649087
4
-
-
94472
4
-
unstable
94475
4
-
-
94482
25
-
-
94475
25 - 37
-
-
94472, 94475, 94476, 94482
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
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
L-ascorbic acid and Cu2+, inactivation irreversible
-
94480
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4 months, 4C
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2.4fold; 4fold
-
using Ni-NTA chromatography
using Ni-NTA chromatography
27.2fold from liver mitochondria in a 5-step chromatographical procedure
-
; 1375fold
-
; 14000fold
-
; 4600fold
-
recombinant enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
functionally expressed in Sf9 insect cells
expressed in Escherichia coli as a His-tagged fusion protein
expression in Spodoptera frugiperda
-
expressed in Escherichia coli as a His-tagged fusion protein
acu-8 gene mutant, sequence resembles Saccharomyces cerevisiae glucose-repressible acetyl-CoA-hydrolase
-
expression in Sf9 cells
-
functional overexpression of the enzyme in Nicotiana tabacum cv. Samsun mitochondria using the Agrobacterium transfection system
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ACOT12 mRNA and protein levels in rat primary hepatocytes decrease following treatment with insulin
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G277S/G279S
-
mutant enzyme shows less than 5% of the activity of the wild-type enzyme
additional information
mutant form of ACOT12 lacking the START domain is not inhibited by lipids. Mutant forms both dimers and tetramers whereas wild-type forms only tetramers after addition of ATP
G393E/G395S
-
mutant enzyme shows less than 5% of the activity of the wild-type enzyme
additional information
-
construction of transgenic tobacco plants overexpressing the enzyme in mitochondria, detailed analysis of effects on the tobacco plant primary metabolism, plants show a strong phenotype with reduced growth of plant organs, overview
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
from cold inactivation
-