Information on EC 2.3.1.9 - acetyl-CoA C-acetyltransferase

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

EC NUMBER
COMMENTARY hide
2.3.1.9
-
RECOMMENDED NAME
GeneOntology No.
acetyl-CoA C-acetyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 acetyl-CoA = CoA + acetoacetyl-CoA
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
Claisen condensation
condensation
-
-
-
-
thiolytic cleavage
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(R)- and (S)-3-hydroxybutanoate biosynthesis (engineered)
-
-
2-methylbutanoate biosynthesis
-
-
2-methylpropene degradation
-
-
3-hydroxypropanoate/4-hydroxybutanate cycle
-
-
acetoacetate degradation (to acetyl CoA)
-
-
acetyl-CoA fermentation to butanoate II
-
-
Benzoate degradation
-
-
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
butanoate fermentation
-
-
Butanoate metabolism
-
-
Carbon fixation pathways in prokaryotes
-
-
CO2 fixation in Crenarchaeota
-
-
crotonate fermentation (to acetate and cyclohexane carboxylate)
-
-
ethylmalonyl-CoA pathway
-
-
Fatty acid degradation
-
-
glutaryl-CoA degradation
-
-
Glyoxylate and dicarboxylate metabolism
-
-
isoprene biosynthesis II (engineered)
-
-
isopropanol biosynthesis (engineered)
-
-
ketogenesis
-
-
ketolysis
-
-
L-glutamate degradation V (via hydroxyglutarate)
-
-
L-isoleucine degradation I
-
-
L-lysine fermentation to acetate and butanoate
-
-
Lysine degradation
-
-
Metabolic pathways
-
-
methyl tert-butyl ether degradation
-
-
mevalonate metabolism
-
-
mevalonate pathway I
-
-
mevalonate pathway II (archaea)
-
-
mevalonate pathway III (archaea)
-
-
Microbial metabolism in diverse environments
-
-
polyhydroxybutanoate biosynthesis
-
-
Propanoate metabolism
-
-
pyruvate fermentation to acetone
-
-
pyruvate fermentation to butanoate
-
-
pyruvate fermentation to butanol I
-
-
pyruvate fermentation to butanol II (engineered)
-
-
pyruvate fermentation to hexanol (engineered)
-
-
Pyruvate metabolism
-
-
Synthesis and degradation of ketone bodies
-
-
Terpenoid backbone biosynthesis
-
-
tryptophan metabolism
-
-
Tryptophan metabolism
-
-
Valine, leucine and isoleucine degradation
-
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:acetyl-CoA C-acetyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9027-46-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene mmgA
-
-
Manually annotated by BRENDA team
L. G. Don, herbarium number LEF 920116
-
-
Manually annotated by BRENDA team
ATCC 824
-
-
Manually annotated by BRENDA team
strain ZP-6, haloarchaeon
-
-
Manually annotated by BRENDA team
strain ZP-6, haloarchaeon
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
; adzuki bean borer moth, female moths, gene Osat1
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Vitis vinifera x Vitis riparia
-
-
-
Manually annotated by BRENDA team
Vitis vinifera x Vitis vinifera
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
enzyme deficiency is a rare metabolic disease of autosomal recessive inheritance characterized by intermittent ketoacidotic episodes with onset in the infant period and decline with age, overview
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 acetyl-CoA
acetoacetyl-CoA + CoA
show the reaction diagram
2 acetyl-CoA
CoA + acetoacetyl-CoA
show the reaction diagram
2-methylacetoacetyl-CoA + CoA
acetyl-CoA + propionyl-CoA
show the reaction diagram
acetoacetyl-CoA + CoA
2 acetyl-CoA
show the reaction diagram
acetoacetyl-S-pantetheine + acetyldithio-CoA
acetyl-S-pantetheine + 3-ketobutyryldithio-CoA
show the reaction diagram
-
-
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
show the reaction diagram
acetyl-CoA + acetyldithio-CoA
CoA + 3-ketobutyryldithio-CoA
show the reaction diagram
-
-
-
r
acetyl-CoA + propionyl-CoA
CoA + 3-oxopentanoyl-CoA
show the reaction diagram
CoA + acetoacetyl-10-bis-demethylpantetheine 11-pivaloate
acetyl-CoA + acetyl-10-bis-demethylpantetheine 11-pivaloate
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
show the reaction diagram
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
CoA + acetoacetyl-S-(11-methoxymethyl)pantetheine
acetyl-CoA + acetyl-S-(11-methoxymethyl)pantetheine
show the reaction diagram
-
-
-
-
?
CoA + acetoacetyl-S-(11-t-butyldimethylsilyl)pantetheine
acetyl-CoA + acetyl-S-(11-t-butyldimethylsilyl)pantetheine
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-S-(D-pantetheine) 11-pivalate
acetyl-CoA + acetyl-S-(D-pantetheine) 11-pivalate
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-S-(L-pantetheine) 11-pivalate
acetyl-CoA + acetyl-S-(L-pantetheine) 11-pivalate
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-S-homopantetheine 12-pivalate
acetyl-CoA + acetyl-S-homopantetheine 12-pivalate
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-S-pantetheine
acetyl-CoA + acetyl-S-pantetheine
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
2 acetyl-CoA
acetoacetyl-CoA + CoA
show the reaction diagram
B7XEI5
the thiolase is involved in the synthesis and catabolism of fatty acids
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
show the reaction diagram
2-methylacetoacetyl-CoA + CoA
acetyl-CoA + propionyl-CoA
show the reaction diagram
-
cleavage of 2-methylacetoacetyl-CoA in the isoleucine catabolism
-
-
?
acetoacetyl-CoA + CoA
2 acetyl-CoA
show the reaction diagram
-
interconversion of 2 acetyl-CoA into acetoacetyl-CoA in the ketone body metabolism
-
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
show the reaction diagram
CoA + acetoacetyl-CoA
2 acetyl-CoA
show the reaction diagram
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
additional information
?
-
-
the enzyme plays a more important role in the activation of ketogenesis in Squalus acanthias than in mammals and birds
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
enzyme contains selenomethionine
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
can replace Mg2+, 5 mM, 90% of activity with Mg2+, inhibition above 10 mM
Cl-
-
the crystal structures of T2 show that each T2 subunit has a binding site for a chloride ion and a potassium ion. Each of these ion binding sites is defined well by loops at the active site, resulting in the stabilization of the catalytic loops
K+
-
the crystal structures of T2 show that each T2 subunit has a binding site for a chloride ion and a potassium ion. Each of these ion binding sites is defined well by loops at the active site, resulting in the stabilization of the catalytic loops
Mg2+
-
maximal activity at 5-10 mM, inhibition above
Mn2+
-
can replace Mg2+, 5 mM, 90% of activity with Mg2+, inhibition above
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11-Chloro-10-oxoundecanoic acid
-
acetyl-CoA or CoA protect
11-chloro-10-oxoundecanoyl-CoA
-
acetyl-CoA or CoA protect
-
2,3-pentadienoyl-S-pantetheine 11-pivalate
-
half-life for inactivation: 1.9 min
2-Butynoyl-CoA
-
0.1 mM, 74% inactivation after 10 min
2-Oxo-5-(1-hydroxy-2,4,6-heptatriynyl)-1,3-dioxolone-4-heptanoic acid
-
natural product isolated from actinomycete culture L-660,631, IC50: 0.00001 mM,
3-butynoyl-CoA
-
0.01 mM, 95% inactivation after 10 min, acetoacetyl-CoA or 0.8 mM CoA protect
3-hydroxybutyryl-CoA
-
-
3-Pentenoyl-S-pantetheine 11-pivalate
-
half-life for inactivation: 0.26 min
3-Pentynoyl-CoA
-
0.1 mM, complete inactivation after 10 min, acetoacetyl-CoA or 0.8 mM CoA protect
3-Pentynoylpantetheine
-
1 mM, complete inactivation after 10 min
4-Bromocrotonyl-CoA
-
0.1 mM, complete inactivation after 10 min, acetoacetyl-CoA protects
4-bromocrotonylpantetheine
-
1 mM, complete inactivation after 10 min
5,5'-dithiobis(2-nitrobenzoate)
-
0.4 mM, 87% inhibition
5-chloro-4-oxopentanoyl-CoA
-
acetyl-CoA or CoA protect
7-Chloro-6-oxoheptanoic acid
-
acetyl-CoA or CoA protect
7-chloro-6-oxoheptanoyl-CoA
-
acetyl-CoA or CoA protect
9-Chloro-8-oxononanoic acid
-
acetyl-CoA or CoA protect
9-chloro-8-oxononanoyl-CoA
-
acetyl-CoA or CoA protect
acetoacetyl-CoA
acetyl-CoA
-
-
Acryl-S-pantetheine 11-pivalate
-
-
ATP
-
10 mM, 41% inhibition
bromoacetyl oxoester
-
acetyl-pantetheine 11-pivalate analog
-
Bromoacetyl thioester
-
acetyl-pantetheine 11-pivalate analog
Bromoacetylamide
-
acetyl-pantetheine 11-pivalate analog
Butyryl-CoA
-
1 mM, 42% inhibition
Ca2+
-
10 and 25 mM, 25 and 50% inhibition of thiolysis
citraconic anhydride
-
-
dec-3-ynoic acid
-
irreversible inhibition
Dithionitrobenzoate
-
low but significant inhibition
iodoacetamide
N-ethylmaleimide
p-chloromercuribenzoate
Sodium borohydride
sulfhydryl reagents
-
-
thiolactomycin
-
0.36 mM, 50% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KCl
-
maximal activity at 4.5 M
lovostatin
-
1.9fold activity increase in rats treated with lovostatin
NaCl
-
maximal activity at 4.5 M
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.023 - 0.025
acetoacatyl-CoA
0.21
acetoacetyl-10-bis-demethylpantetheine 11-pivalate
-
-
0.0038 - 0.18
acetoacetyl-CoA
0.12
acetoacetyl-S-(11-methoxymethyl)pantetheine
-
-
0.074
acetoacetyl-S-(11-t-butyldimethylsilyl)pantetheine
-
cosubstrate CoA
0.073
acetoacetyl-S-(D-pantetheine) 11-pivalate
-
-
0.25
acetoacetyl-S-homopantetheine 12-pivalate
-
-
0.46
acetoacetyl-S-pantetheine
-
-
0.0062 - 1.06
acetyl-CoA
0.0048 - 0.154
CoA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
14
3-ketobutyryldithio-CoA
Zoogloea ramigera
-
-
266
acetoacetyl-10-bis-demethylpantetheine 11-pivaloate
Zoogloea ramigera
-
-
-
0.0767 - 1000
acetoacetyl-CoA
353
acetoacetyl-S-(11-methoxymethyl)pantetheine
Zoogloea ramigera
-
-
434
acetoacetyl-S-(11-t-butyldimethylsilyl)pantetheine
Zoogloea ramigera
-
-
469
acetoacetyl-S-(D-pantetheine) 11-pivalate
Zoogloea ramigera
-
-
256
acetoacetyl-S-(L-pantetheine) 11-pivalate
Zoogloea ramigera
-
-
177
acetoacetyl-S-homopantetheine 12-pivalate
Zoogloea ramigera
-
-
14 - 174
acetoacetyl-S-pantetheine
2.1
acetyl-CoA
Zoogloea ramigera
-
-
29.5
CoA
Gallus gallus
-
presence of Mg2+
900
thiolytic cleavage
Gallus gallus
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5600
acetoacetyl-CoA
Metallosphaera sedula
A4YEH9
pH 7.5, 70C
187
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.028
11-Chloro-10-oxoundecanoic acid
-
-
0.0025
11-chloro-10-oxoundecanoyl-CoA
-
-
-
1.54
2,3-pentadienoyl-S-pantetheine 11-pivalate
-
-
1.25
3-Pentenoyl-S-pantetheine 11-pivalate
-
-
0.025
3-Pentynoyl-CoA
-
-
0.013
4-Bromocrotonyl-CoA
-
-
0.015
5-chloro-4-oxopentanoyl-CoA
-
-
11.4
7-Chloro-6-oxoheptanoic acid
-
-
0.002
7-chloro-6-oxoheptanoyl-CoA
-
-
0.49
9-Chloro-8-oxononanoic acid
-
-
0.0014
9-chloro-8-oxononanoyl-CoA
0.0016
acetoacetyl-CoA
-
isoenzyme A
0.006 - 0.12
CoA
10
dec-3-ynoic acid
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00001
2-Oxo-5-(1-hydroxy-2,4,6-heptatriynyl)-1,3-dioxolone-4-heptanoic acid
Rattus norvegicus
-
natural product isolated from actinomycete culture L-660,631, IC50: 0.00001 mM,
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.05
-
-
0.16
-
acetoacetyl-CoA synthesis
13.2
purified native enzyme
15.78
purified recombinant enzyme
58.2
-
-
100 - 130
-
peroxisomal thiolase, thiolysis
412
-
thiolysis of acetoacetyl-CoA
506
-
thiolase II
additional information
-
assay method
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
assay at
7
-
condensation
8.1 - 8.4
-
isoenzyme A and B, acetoacetyl-CoA synthesis
8.3
-
cytosolic and peroxisomal thiolase I
8.4
-
cleavage of acetoacetyl-CoA, 85% of maximal activity between pH 8.0 and pH 9.0
9.5
-
thiolysis
10.5
-
synthesis
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 9
-
69% of maximal activity at pH 9.0
6 - 9
-
approx. 80% of maximal activity at pH 6.0, approx. 40% at pH 9.0
6.5 - 9.2
-
approx. 50% of maximal activity at pH 6.5 and pH 9.2, thiolysis
7 - 9
significant decrease in activiy below pH 7.0 or above pH 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
isoform AACT! is highly expressed in root tips, young leaf, top stem and anther
Manually annotated by BRENDA team
-
mitochondrial acetoacetyl CoA thiolase is decreased by 80% in ulcerative colitis compared with control. Mitochondrial thiolase activity in ulcerative colitis does not correlate with clinical, endoscopic or histological indices of disease severity. Mitochondrial thiolase activity is reduced in the normal right colon mucosa of patients with left-sided ulcerative colitis
Manually annotated by BRENDA team
; low ACT1 expression
Manually annotated by BRENDA team
isoform AACT! is primarily expressed in the vascular system
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Clostridium acetobutylicum (strain EA 2018)
Clostridium acetobutylicum (strain EA 2018)
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Escherichia coli (strain K12)
Mycobacterium avium (strain 104)
Peptoclostridium difficile (strain 630)
Peptoclostridium difficile (strain 630)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80000
-
gel filtration
84000
-
about, recombinant His-tagged enzyme, gel filtration
147600
-
isoenzyme B, sedimentation analysis
150000
-
isoenzyme A, gel filtration
151000
-
gel filtration, isoenzyme A and B
152000
154600
-
isoenzyme A, sedimentation analysis
155000
156000
-
sucrose density gradient sedimentation
160000
-
peroxisomal thiolase, gel filtration
164000
-
gel filtration
166000
-
gel filtration
169000
-
sedimentation equilibrium
170000
-
gel filtration
180000
185000
-
native thiolase, gel filtration
187000
-
recombinant thiolase, gel filtration
188000
-
gel filtration
190000
-
gel filtration
193000
-
native PAGE
240000
-
peroxisomal thiolase I, gel filtration
250000
-
cytosolic thiolase I, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
tetramer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method at 4C. Unliganded and liganded (with CoA and with K+) structures of the human mitochondrial recombinant tetrameric thiolase
-
only successful in the presence of CoA
hangig-drop vapor diffusion at 21C, crystal structure at 2.0 A resolution
-
wild-type thiolase and acetylated thiolase complexed with CoA, C89A mutant thiolase complexed with acetyl-CoA and acetoacetyl-CoA, Q64A mutant thiolase
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0
-
1 h, complete loss of activity
37
-
wild-type T2 protein is stable even after chasing for 48 h at 37C. The amount of E252del mutant protein at 48 h incubation with cycloheximide is estimated to be 50% of that observed at 0 h. E252del mutant T2 is unstable compared to the wild-type protein at 37C
63
-
5 min, stable
70
-
10 h, 4 M KCl, 20% loss of activity
85
-
10 h, 4 M KCl, 35% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dithiothreitol stabilizes
-
glycerol stabilizes
-
labile enzyme, partially stabilized by 1-2 mM dithiothreitol and 20% ethylene glycol
-
more than 10% sucrose, 2-mercaptoethanol or dithiothreitol are necessary to maintain activity
-
unstable in dilute solution, less than 0.5 mg/ml protein
-
urea: 2.5 M, 17 h, 50% loss of activity, 5 M, 45 min, 50% loss of activity, 7 M, 1 min, 50% loss of activity
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
sensitive to borohydride reduction
-
487690
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10C, less than 0.2 mg/ml protein, 50 mM Tris, pH 7.2, 0.5 mM dithiothreitol, 8 d, 60-70% loss of activity
-
-20C, 20 mM Tris-HCl, pH 7.8, 0.5 mM 1 mM, EDTA, 15 d, loss of more than 50% activity
-
-20C, 20 mM Tris-HCl, pH 7.8, 0.5 mM dithiothreitol, 1 mM, EDTA, 15 d, loss of 20% activity
-
-20C, 20 mM Tris-HCl, pH 7.8, 0.5 mM dithiothreitol, 1 mM, EDTA, 20% glycerol, 60 d, loss of less than 20% activity
-
-20C, 50 mM Tris-HCl, pH 8.0, 0.5 mM dithiothreitol, glycerol
-
-20C, in dilute solution, less than 0.5 mg/ml protein, 24 h, complete loss of activity
-
-90C, 12 months
-
0C, 0.05 M Tris-HCl, pH 7.8, 2 mM dithiothreitol, 1 mM EDTA, 20% glycerol, 6 weeks, 50% loss of activity
-
25C, 1 week, 4.5 M KCl, no loss of activity
-
25C, 72 h, 200 mM KCl, 90% loss of activity
-
4C, 1 mM dithiothreitol, 10% v/v glycerol, N2 atmosphere, 1 month, less than 10% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 forms: A and B
-
ammonium sulfate, acetone, acid treatment, CM-Sephadex, Sepharose 6B
-
ammonium sulfate, calcium phosphate gel, ethanol, partial purification
-
ammonium sulfate, DEAE-Sephacel, Blue Sepharose, AX 300 column
-
ammonium sulfate, DEAE-Sepharose, hydroxyapatite, phosphocellulose, Blue Sepharose
-
ammonium sulfate, Econo-Q, Superose 6, Mono Q, HA-Ultrogel, Mono Q
-
ammonium sulfate, hydroxylapatite, phosphocellulose
-
ammonium sulfate, Sephacryl S-200, superose 6, Mono Q
-
ammonium sulfate, Sephadex G-150, DEAE-Sephadex, QAE-Sephadex; constitutive mutant, thiolase II, heat treatment, phosphocellulose
-
CM-Sephadex; single-step purification
-
cytosolic enzyme
-
cytosolic thiolase I
-
DEAE-cellulose, ammonium sulfate, gel filtration, DEAE-cellulose, Matrex gel green A
-
DEAE-Sepharose, butyl-Toyopearl, Cellulofine
-
hydroxyapatite, Superdex, Fractogel
-
isoenzymes A and B, ammonium sulfate, cellulose phosphate column, crystallization
-
liver enzyme, ammonium sulfate, calcium phosphate gel, phosphocellulose column, DEAE-cellulose, hydroxylapatite, Sephadex G-200
-
peroxisomal thiolase, DEAE-cellulose, phosphocellulose column, Blue-Sepharose
-
pH 5.5, DEAE-cellulose, calcium phosphate column, celulose phosphate column
-
poly ethylene glycol 6000, DEAE-cellulose 52, benzyl-Sepharose, hydroxylapatite
-
protamine sulfate, DEAE-cellulose, phosphocellulose, Sephadex G-200
-
Q-Sepharose, ammonium sulfate, Sephacryl S-200, Mono Q, FPLC S-300
-
Q-Sepharose, S-Sepharose, Superose 6, partially purifed
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recombinant enzyme
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recombinant His-tagged AACT 88fold to homogeneity by nickel affinity chromatography from Escherichia coli TOP10 cells
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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recombinant His-tagged thiolase, Ni-affinity column
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recombinant protein
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
AACT, DNA and amino acid sequence determination and analysis, sequence comparison with Arabidopsis thaliana, expression of the active His-tagged enzyme in Escherichia coli TOP10 cells
expression in Escherichia coli
expression in Sf9 cell; gene OSAT1, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of the His-tagged enzyme in Spodoptera frugiperda Sf9 cells using a baculovirus expression system, expression in the cytosol, rather than nucleus and mitochondria
expression of cytosolic and peroxisomal thiolase I in Saccharomyces cerevisiae
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gene ACT1, DNA and amino acid sequence determination and analysis, expression, expression analysis, phylogenetic analysis, overexpression in transgenic Arabidopsis thaliana plants using transfection with Agrobacterium tumefaciens; gene ACT2, DNA and amino acid sequence determination and analysis, expression analysis, phylogenetic analysis, overexpression in transgenic Arabidopsis thaliana plants using transfection with Agrobacterium tumefaciens
gene mmgA, encoded in the mmg operon, DNA and amino acid sequence determination and analysis, overexpression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
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overexpressed as soluble N-terminal His10-tagged protein in Escherichia coli
recombinantly expressed in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is highly increased in roots and leaves under cold and salinity stress
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E252del
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25% of wild-type activity at 37C, 40% of wild-type activity at 30C. Mutant is unstable compared to the wild-type protein at 37C. KM-value for acetoacetyl-CoA is 2fold higher than wild-type value. Km-value for CoA is 1.8fold lower than wild-type value; no residual activity under any condition; relative protein amount and enzyme activity of 30% and 25% respectively, in comparison to the wild-type at 37C. 2fold Km-elevation for substrates coenzyme A and acetoacetyl-CoA compared to wild-type values. Vmax is comparable to wild-type value
M193T
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naturally occuring mutation leading to enzyme deficiency and to the ketoacidotic episode phenotype, but with differing clinical severity, overview
N158D
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inactive mutant protein; no residual activity under any condition
N158S
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inactive mutant protein; no residual activity under any condition
N282H
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inactive mutant protein; no residual activity under any condition
N353K
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cDNAs yield neither residual T2 protein nor enzyme activity; no residual activity under any condition
Q272X
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no residual activity under any condition
Q73P
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cDNAs yield neither residual T2 protein nor enzyme activity; no residual activity under any condition
R208Q
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inactive mutant protein; no residual activity under any condition
Y219H
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inactive mutant protein; no residual activity under any condition
C92S
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kcat decreases to 0.2% of that for the recombinant thiolase
C378G
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mutation eliminates the ability of thiolase to catalyze proton abstraction from C2 of acetyl-CoA
C89A
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no thiolytic activity towards acetoacetyl-CoA
Q64A
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30% lower kcat than that of the wild-type
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
assay based on the specific absorbance at 303 nm of the Mg2+-enolate complex of acetoacetyl-Coa
synthesis
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