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Information on EC 2.3.1.9 - acetyl-CoA C-acetyltransferase for references in articles please use BRENDA:EC2.3.1.9Word Map on EC 2.3.1.9
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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acetyl-CoA C-acetyltransferase
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2 acetyl-CoA = CoA + acetoacetyl-CoA
2 acetyl-CoA = CoA + acetoacetyl-CoA
bi bi ping pong mechanism
-
2 acetyl-CoA = CoA + acetoacetyl-CoA
mechanism
-
2 acetyl-CoA = CoA + acetoacetyl-CoA
mechanism
-
2 acetyl-CoA = CoA + acetoacetyl-CoA
mechanism; ping-pong mechanism
-
2 acetyl-CoA = CoA + acetoacetyl-CoA
ping-pong mechanism
-
2 acetyl-CoA = CoA + acetoacetyl-CoA
proposed two-step ping pong mechanism
-
2 acetyl-CoA = CoA + acetoacetyl-CoA
reaction involves 2 chemically distinct steps: acetyl group transfer from acetyl-CoA to Cys89, and transfer of this acetyl group to a second acetyl-CoA in the Claisen condensation step to form acetoacetyl-CoA
-
2 acetyl-CoA = CoA + acetoacetyl-CoA
Claisen condensation, mechanism
-
2 acetyl-CoA = CoA + acetoacetyl-CoA
Claisen condensation, mechanism
2 acetyl-CoA = CoA + acetoacetyl-CoA
Claisen condensation, mechanism
-
2 acetyl-CoA = CoA + acetoacetyl-CoA
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Acyl group transfer
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thiolytic cleavage
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-
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-
Claisen condensation
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-
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(R)- and (S)-3-hydroxybutanoate biosynthesis (engineered)
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-
2-methylpropene degradation
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-
3-hydroxypropanoate/4-hydroxybutanate cycle
-
-
4-oxopentanoate degradation
-
-
acetoacetate degradation (to acetyl CoA)
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-
acetyl-CoA fermentation to butanoate II
-
-
crotonate fermentation (to acetate and cyclohexane carboxylate)
-
-
ethylmalonyl-CoA pathway
-
-
fermentation to 2-methylbutanoate
-
-
glutaryl-CoA degradation
-
-
isoprene biosynthesis II (engineered)
-
-
isopropanol biosynthesis (engineered)
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-
L-glutamate degradation V (via hydroxyglutarate)
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-
L-isoleucine degradation I
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-
L-lysine fermentation to acetate and butanoate
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methyl tert-butyl ether degradation
-
-
mevalonate pathway II (archaea)
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-
mevalonate pathway III (archaea)
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-
polyhydroxybutanoate biosynthesis
-
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pyruvate fermentation to acetone
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pyruvate fermentation to butanoate
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pyruvate fermentation to butanol I
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pyruvate fermentation to butanol II (engineered)
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pyruvate fermentation to hexanol (engineered)
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butanoate fermentation
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CO2 fixation in Crenarchaeota
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-
mevalonate metabolism
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-
tryptophan metabolism
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Fatty acid degradation
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Synthesis and degradation of ketone bodies
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-
Valine, leucine and isoleucine degradation
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-
Tryptophan metabolism
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-
Glyoxylate and dicarboxylate metabolism
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-
Propanoate metabolism
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-
Carbon fixation pathways in prokaryotes
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Terpenoid backbone biosynthesis
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Biosynthesis of secondary metabolites
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Microbial metabolism in diverse environments
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Biosynthesis of antibiotics
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acetyl-CoA:acetyl-CoA C-acetyltransferase
-
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2-methylacetoacetyl-CoA thiolase
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3-ketoacyl-CoA (T1)-like thiolase
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-
3-ketoacyl-coenzyme A thiolase
acetoacetyl-CoA acetyltransferase
acetoacetyl-CoA C-acetyltransferase
-
acetoacetyl-CoA thiolase T2
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acetyl coenzyme A thiolase
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-
-
acetyl-CoA acetyltransferase
acetyl-CoA C-acetyltransferase
acetyl-CoA:N-acetyltransferase
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acetyltransferase, acetyl coenzyme A
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beta-acetoacetyl coenzyme A thiolase
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-
cytosolic acetoacetyl-CoA thiolase
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cytosolic acetoacetyl-CoA thiolase 1
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cytosolic acetoacetyl-CoA thiolase 2
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3-ketoacyl-CoA thiolase
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3-ketoacyl-CoA thiolase
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3-ketoacyl-CoA thiolase
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3-ketoacyl-CoA thiolase
;
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3-ketoacyl-coenzyme A thiolase
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3-ketoacyl-coenzyme A thiolase
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A1887
-
AACT
-
AACT1
-
ACAT
-
ACAT1
-
isoform
ACAT2
-
isoform
ACCT
-
-
acetoacetyl CoA thiolase
-
-
-
-
acetoacetyl CoA thiolase
-
acetoacetyl CoA thiolase
-
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acetoacetyl-CoA acetyltransferase
-
-
acetoacetyl-CoA acetyltransferase
-
-
-
acetoacetyl-CoA thiolase
-
-
-
-
acetoacetyl-CoA thiolase
-
acetoacetyl-CoA thiolase
-
-
acetoacetyl-CoA thiolase
-
acetoacetyl-CoA thiolase
-
acetoacetyl-CoA thiolase
-
acetoacetyl-CoA thiolase
;
-
acetoacetyl-CoA thiolase
-
-
acetoacetyl-CoA thiolase
-
-
-
acetoacetyl-CoA thiolase
-
-
acetoacetyl-CoA thiolase
-
-
acetoacetyl-CoA thiolase
-
-
-
acetoacetyl-CoA thiolase
-
-
acetoacetyl-CoA thiolase
-
-
acetoacetyl-CoA thiolase
Vitis vinifera x Vitis vinifera
-
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acetyl-CoA acetyltransferase
-
-
-
-
acetyl-CoA acetyltransferase
-
acetyl-CoA C-acetyltransferase
-
-
acetyl-CoA C-acetyltransferase
-
-
-
ACTRANS
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-
ACTRANS
Vitis vinifera x Vitis vinifera
-
-
beta-ketothiolase
-
ERG10
-
-
HFX_1022
locus name, subunit PhaAbeta
HFX_1022
locus name, subunit PhaAbeta
-
HFX_1023
locus name, subunit PhaAalpha
HFX_1023
locus name, subunit PhaAalpha
-
HFX_6003
locus name, subunit BktBbeta
HFX_6003
locus name, subunit BktBbeta
-
HFX_6004
locus name, subunit BktBalpha
HFX_6004
locus name, subunit BktBalpha
-
KACT
-
Msed_0656
locus name
thiolase II
-
-
-
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Tneu_0249
locus name
type II thiolase
-
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gene mmgA
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brenda
-
UniProt
brenda
-
-
-
brenda
L. G. Don, herbarium number LEF 920116
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-
brenda
-
-
-
brenda
-
UniProt
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
haloarchaeon
-
-
brenda
haloarchaeon
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
-
-
-
brenda
; adzuki bean borer moth, female moths, gene Osat1
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
Vitis vinifera x Vitis vinifera
-
-
-
brenda
cytosolic acetoacetyl-CoA thiolase 1
UniProt
brenda
cytosolic acetoacetyl-CoA thiolase 2
UniProt
brenda
cytosolic isozyme AACT2; ecotype Columbia, gene ACT2
UniProt
brenda
isozyme AACT1; ecotype Columbia, gene ACT1
UniProt
brenda
-
-
-
brenda
2 forms: A and B
-
-
brenda
3 forms: I, A, B
-
-
brenda
-
-
-
brenda
-
Uniprot
brenda
ATCC 20336
-
-
brenda
-
UniProt
brenda
ATCC 824
-
-
brenda
gene H16_A1887; gene H16_A1887
UniProt
brenda
gene H16_B0759; gene H16_B0759
UniProt
brenda
gene H16_A1887; gene H16_A1887
UniProt
brenda
gene H16_B0759; gene H16_B0759
UniProt
brenda
-
UniProt
brenda
-
-
-
brenda
-
-
-
brenda
wild-type and constitutive mutant
-
-
brenda
I3R3D1: catalytic subunit PhaAalpha, I3RA71: subunit PhaAbeta
UniProt
brenda
I3RA72: catalytic subunit BktBalpha, I3RA71: subunit BktBbeta
UniProt
brenda
I3R3D1: catalytic subunit PhaAalpha, I3RA71: subunit PhaAbeta
UniProt
brenda
I3RA72: catalytic subunit BktBalpha, I3RA71: subunit BktBbeta
UniProt
brenda
-
UniProt
brenda
sunflower
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-
brenda
-
Uniprot
brenda
-
-
-
brenda
patient with enzyme deficiency
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-
brenda
-
-
-
brenda
2 forms: A and B
-
-
brenda
-
-
-
brenda
cicer, strain CC 1192
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brenda
-
-
-
brenda
-
SwissProt
brenda
-
Uniprot
brenda
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malfunction
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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
malfunction
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mutants with deletion of isoform Acat1 exhibit defect in virulence only, while mutants of isoform Acat2 are characterized by reduction in growth and virulence
malfunction
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mutants with deletion of isoform Acat1 exhibit defect in virulence only, while mutants of isoform Acat2 are characterized by reduction in growth and virulence
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metabolism
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the enzyme shows degradative thiolase activity catalyzing the fourth step of beta-oxidation degradative pathways by converting 3-oxoacyl-CoA to acyl-CoA
metabolism
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the enzyme shows degradative thiolase activity catalyzing the fourth step of beta-oxidation degradative pathways by converting 3-ketoacyl-CoA to acyl-CoA
metabolism
-
the enzyme shows degradative thiolase activity catalyzing the fourth step of beta-oxidation degradative pathways by converting 3-ketoacyl-CoA to acyl-CoA; the enzyme shows degradative thiolase activity catalyzing the fourth step of beta-oxidation degradative pathways by converting 3-ketoacyl-CoA to acyl-CoA; the enzyme shows degradative thiolase activity catalyzing the fourth step of beta-oxidation degradative pathways by converting 3-oxoacyl-CoA to acyl-CoA
-
physiological function
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involved in terpenoid metabolism
physiological function
Vitis vinifera x Vitis vinifera
-
involved in terpenoid metabolism
physiological function
over-expressing transgenic plants show salinity tolerance comparable with empty vector transformed plants and enhanced production of squalene without alteration in the 3-hydroxy-3-methylglutaryl-CoA reductase activity in salt-stress conditions
physiological function
isoform AACT2 function is required for embryogenesis and for normal male gamete transmission. RNAi lines that express reduced levels of isoform AACT2 show pleiotropic phenotypes, including reduced apical dominance, elongated life span and flowering duration, sterility, dwarfing, reduced seed yield and shorter root length. The reduced stature is caused by a reduction in cell size and fewer cells, and male sterility is caused by loss of the pollen coat and premature degeneration of the tapetal cells. The roots of AACT2 RNAi plants show quantitative and qualitative alterations in phytosterol profiles. These phenotypes and biochemical alterations are reversed when AACT2 RNAi plants are grown in the presence of mevalonate; plants lacking isoform AACT1 function are completely viable and show no apparent growth phenotypes
physiological function
the enzyme is responsible for supplying the precursors for biosynthesis of poly(3-hydroxybutyrate-co-3-hydroxyvalerate)
physiological function
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
physiological function
the enzyme is involved in autotrophic carbon fixation
physiological function
-
the activity of isoform Acat1 promotes virulence in the rice blast fungus
physiological function
the enzyme is involved in fatty acid metabolism, for energy or physical requirements to adapt to the host
physiological function
-
the enzyme is responsible for supplying the precursors for biosynthesis of poly(3-hydroxybutyrate-co-3-hydroxyvalerate)
-
physiological function
-
the activity of isoform Acat1 promotes virulence in the rice blast fungus
-
physiological function
-
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
-
physiological function
-
the enzyme is involved in autotrophic carbon fixation
-
additional information
-
the enzyme functions as a dimer, and the monomer comprises three subdomains I, II, and III. The structural comparison between the apoform and the CoA-bound form reveals that the enzyme undergoes a structural change in the lid-subdomain III upon the binding of the CoA substrate. The CoA molecule is stabilized by hydrogen bonding with positively charged residues Lys18, Arg210, and Arg217, and residues Thr213 and Gln151 aid its binding as well. At the enzyme's active site highly conserved residues, Cys91, His348, and Cys378, are located near the thiol-group of CoA, indicating that enzyme ReH16_A1887 might catalyze the thiolase reaction in a way similar to other thiolases. In the vicinity of the covalent nucleophile Cys91, a hydrophobic hole that might serve as a binding site for the acyl-group of 3-oxoacyl-CoA. Subdomains I and II harbor the active site residues: Cys91 in subdomain I, and His348 and Cys378 in subdomain II
additional information
similar to other degradative thiolases, enzyme ReH16_B0759 functions as a dimer, and the monomer comprises three subdomains. Unlike enzyme ReH16_A1887, a substantial structural change is not observed upon the binding of the CoA substrate in enzyme ReH16_B0759. At the active site of the enzyme highly conserved residues Cys89, His347, and Cys377are located near the thiol-group of CoA
additional information
-
similar to other degradative thiolases, enzyme ReH16_B0759 functions as a dimer, and the monomer comprises three subdomains. Unlike enzyme ReH16_A1887, a substantial structural change is not observed upon the binding of the CoA substrate in enzyme ReH16_B0759. At the active site of the enzyme highly conserved residues Cys89, His347, and Cys377are located near the thiol-group of CoA; the enzyme functions as a dimer, and the monomer comprises three subdomains I, II, and III. The structural comparison between the apoform and the CoA-bound form reveals that the enzyme undergoes a structural change in the lid-subdomain III upon the binding of the CoA substrate. The CoA molecule is stabilized by hydrogen bonding with positively charged residues Lys18, Arg210, and Arg217, and residues Thr213 and Gln151 aid its binding as well. At the enzyme's active site highly conserved residues, Cys91, His348, and Cys378, are located near the thiol-group of CoA, indicating that enzyme ReH16_A1887 might catalyze the thiolase reaction in a way similar to other thiolases. In the vicinity of the covalent nucleophile Cys91, a hydrophobic hole that might serve as a binding site for the acyl-group of 3-oxoacyl-CoA. Subdomains I and II harbor the active site residues: Cys91 in subdomain I, and His348 and Cys378 in subdomain II
-
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2 acetyl-CoA
acetoacetyl-CoA + CoA
2 acetyl-CoA
CoA + acetoacetyl-CoA
2-methylacetoacetyl-CoA + CoA
acetyl-CoA + propionyl-CoA
acetoacetyl-CoA + CoA
2 acetyl-CoA
acetoacetyl-S-pantetheine + acetyldithio-CoA
acetyl-S-pantetheine + 3-ketobutyryldithio-CoA
-
-
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
acetyl-CoA + acetyldithio-CoA
CoA + 3-ketobutyryldithio-CoA
-
-
-
r
acetyl-CoA + propionyl-CoA
CoA + 3-oxopentanoyl-CoA
CoA + acetoacetyl-10-bis-demethylpantetheine 11-pivaloate
acetyl-CoA + acetyl-10-bis-demethylpantetheine 11-pivaloate
-
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-S-(11-methoxymethyl)pantetheine
acetyl-CoA + acetyl-S-(11-methoxymethyl)pantetheine
-
-
-
-
?
CoA + acetoacetyl-S-(11-t-butyldimethylsilyl)pantetheine
acetyl-CoA + acetyl-S-(11-t-butyldimethylsilyl)pantetheine
-
-
-
?
CoA + acetoacetyl-S-(D-pantetheine) 11-pivalate
acetyl-CoA + acetyl-S-(D-pantetheine) 11-pivalate
-
-
-
?
CoA + acetoacetyl-S-(L-pantetheine) 11-pivalate
acetyl-CoA + acetyl-S-(L-pantetheine) 11-pivalate
-
-
-
?
CoA + acetoacetyl-S-homopantetheine 12-pivalate
acetyl-CoA + acetyl-S-homopantetheine 12-pivalate
-
-
-
?
CoA + acetoacetyl-S-pantetheine
acetyl-CoA + acetyl-S-pantetheine
-
-
-
?
additional information
?
-
2 acetyl-CoA
acetoacetyl-CoA + CoA
-
-
-
?
2 acetyl-CoA
acetoacetyl-CoA + CoA
the thiolase is involved in the synthesis and catabolism of fatty acids
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
r
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
r
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
r
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
r
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
r
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
the enzyme is responsible for supplying the precursors for biosynthesis of poly(3-hydroxybutyrate-co-3-hydroxyvalerate)
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
the enzyme is responsible for supplying the precursors for biosynthesis of poly(3-hydroxybutyrate-co-3-hydroxyvalerate)
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
ir
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
?
2-methylacetoacetyl-CoA + CoA
acetyl-CoA + propionyl-CoA
-
-
-
-
?
2-methylacetoacetyl-CoA + CoA
acetyl-CoA + propionyl-CoA
-
cleavage of 2-methylacetoacetyl-CoA in the isoleucine catabolism
-
-
?
acetoacetyl-CoA + CoA
2 acetyl-CoA
-
the enzyme shows preference for the thiolytic reaction direction
-
-
r
acetoacetyl-CoA + CoA
2 acetyl-CoA
-
-
-
?
acetoacetyl-CoA + CoA
2 acetyl-CoA
coupled reaction assay in which the product of the thiolase reaction, acetyl-CoA, becomes the substrate for citrate synthase
-
-
r
acetoacetyl-CoA + CoA
2 acetyl-CoA
-
-
-
-
r
acetoacetyl-CoA + CoA
2 acetyl-CoA
-
interconversion of 2 acetyl-CoA into acetoacetyl-CoA in the ketone body metabolism
-
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
?
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
-
enzyme deficiency affects isoleucine and ketone body metabolism
-
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
involved in fatty acid synthesis
-
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
r
acetyl-CoA + propionyl-CoA
CoA + 3-oxopentanoyl-CoA
-
-
-
?
acetyl-CoA + propionyl-CoA
CoA + 3-oxopentanoyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
-
-
-
r
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
CoA binding mode, overview
-
-
r
CoA + acetoacetyl-CoA
2 acetyl-CoA
CoA substrate binding structure, overview
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
CoA substrate binding structure, overview
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
-
-
-
r
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
CoA binding mode, overview
-
-
r
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
the enzyme is involved in autotrophic carbon fixation
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
the enzyme is involved in autotrophic carbon fixation
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
rate of synthesis is 0.31 and 0.08 the rate of thiolysis for isoenzyme A and B, respectively
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
specific for acetoacetyl-CoA, no activity with ketodecanoyl-CoA, dithiothreitol and 2-mercaptoethanol
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
cytosolic thiolase I is essential for the mevalonate pathway
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?, r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?, r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?, r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
enzyme of fatty acid oxidation cycle
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
enzyme has both thiolase and 3-hydroxy-3-methylglutaryl-CoA reductase activity
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?, r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
thiolase II from constitutive mutant is specific for acetoacetyl-CoA
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?, r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?, r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?, ir
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
thiolysis is strongly preferred
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
peroxisomal thiolase most probably catalyzes the first reaction in peroxisomal cholesterol and dolichol synthesis
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
liver mitochondrial isoenzyme catalyzes the first step in biosynthesis of ketone bodies
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
enzyme has both thiolase and acetyl-CoA:acyl carrier protein transacylase activity
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
thiolysis is preferred, highly specific for acetoacetyl-CoA
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
most active in thiolysis
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
involved in generation of acetoacetyl-CoA for poly-beta-hydroxybutyrate synthesis
-
?
additional information
?
-
-
the enzyme shows degradative thiolase activity by converting 3-ketoacyl-CoA to acyl-CoA
-
-
-
additional information
?
-
the enzyme shows degradative thiolase activity by converting 3-ketoacyl-CoA to acyl-CoA
-
-
-
additional information
?
-
the enzyme shows degradative thiolase activity by converting 3-ketoacyl-CoA to acyl-CoA
-
-
-
additional information
?
-
-
the enzyme shows degradative thiolase activity by converting 3-oxoacyl-CoA to acyl-CoA
-
-
-
additional information
?
-
the bound CoA substrate is located within the deep cleft formed by subdomains I, II, and III. The thiol group of CoA is located in the vicinity of the catalytic site for the degradation reaction, whereas,the adenosine nucleotide moiety is exposed on the surface. Unlike enzyme ReH16_A1887, that shows substantial structural changeupon the binding of CoA, the CoA-bound form of enzyme ReH16_B0759 exhibits quite similar structure to the apoform of the protein except for residual movement of Arg220. Moreover, the CoA binding mode of enzyme ReH16_B0759 is quite different from that of enzyme ReH16_A1887
-
-
-
additional information
?
-
the enzyme shows degradative thiolase activity by converting 3-ketoacyl-CoA to acyl-CoA
-
-
-
additional information
?
-
the bound CoA substrate is located within the deep cleft formed by subdomains I, II, and III. The thiol group of CoA is located in the vicinity of the catalytic site for the degradation reaction, whereas,the adenosine nucleotide moiety is exposed on the surface. Unlike enzyme ReH16_A1887, that shows substantial structural changeupon the binding of CoA, the CoA-bound form of enzyme ReH16_B0759 exhibits quite similar structure to the apoform of the protein except for residual movement of Arg220. Moreover, the CoA binding mode of enzyme ReH16_B0759 is quite different from that of enzyme ReH16_A1887
-
-
-
additional information
?
-
the enzyme shows degradative thiolase activity by converting 3-ketoacyl-CoA to acyl-CoA
-
-
-
additional information
?
-
-
the enzyme shows degradative thiolase activity by converting 3-oxoacyl-CoA to acyl-CoA
-
-
-
additional information
?
-
-
the catalytic triad of BktBalpha is likely to be Ser-His-His
-
-
-
additional information
?
-
the catalytic triad of BktBalpha is likely to be Ser-His-His
-
-
-
additional information
?
-
the catalytic triad of BktBalpha is likely to be Ser-His-His
-
-
-
additional information
?
-
-
the catalytic triad of PhaAalpha is likely to be Ser-His-His
-
-
-
additional information
?
-
the catalytic triad of PhaAalpha is likely to be Ser-His-His
-
-
-
additional information
?
-
the catalytic triad of PhaAalpha is likely to be Ser-His-His
-
-
-
additional information
?
-
the catalytic triad of PhaAalpha is likely to be Ser-His-His
-
-
-
additional information
?
-
the catalytic triad of PhaAalpha is likely to be Ser-His-His
-
-
-
additional information
?
-
the catalytic triad of BktBalpha is likely to be Ser-His-His
-
-
-
additional information
?
-
the catalytic triad of BktBalpha is likely to be Ser-His-His
-
-
-
additional information
?
-
-
no activity is observed with acetyl-CoA
-
-
-
additional information
?
-
-
the enzyme plays a more important role in the activation of ketogenesis in Squalus acanthias than in mammals and birds
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 acetyl-CoA
acetoacetyl-CoA + CoA
B7XEI5
the thiolase is involved in the synthesis and catabolism of fatty acids
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
2-methylacetoacetyl-CoA + CoA
acetyl-CoA + propionyl-CoA
-
cleavage of 2-methylacetoacetyl-CoA in the isoleucine catabolism
-
-
?
acetoacetyl-CoA + CoA
2 acetyl-CoA
-
interconversion of 2 acetyl-CoA into acetoacetyl-CoA in the ketone body metabolism
-
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
CoA + acetoacetyl-CoA
2 acetyl-CoA
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
additional information
?
-
2 acetyl-CoA
CoA + acetoacetyl-CoA
D9U856
-
-
-
r
2 acetyl-CoA
CoA + acetoacetyl-CoA
G7YHN5
-
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
P45359
-
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
Q0KAI3
-
-
-
r
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
r
2 acetyl-CoA
CoA + acetoacetyl-CoA
Q0KAI3
-
-
-
r
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
r
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
I3R3D1 and I3R3D0, I3RA72 and I3RA71
the enzyme is responsible for supplying the precursors for biosynthesis of poly(3-hydroxybutyrate-co-3-hydroxyvalerate)
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
I3R3D1 and I3R3D0, I3RA72 and I3RA71
the enzyme is responsible for supplying the precursors for biosynthesis of poly(3-hydroxybutyrate-co-3-hydroxyvalerate)
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
ir
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
?
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
-
enzyme deficiency affects isoleucine and ketone body metabolism
-
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
Q9BWD1
involved in fatty acid synthesis
-
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
r
CoA + acetoacetyl-CoA
2 acetyl-CoA
Q0KAI3
-
-
-
r
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
-
-
-
r
CoA + acetoacetyl-CoA
2 acetyl-CoA
Q0K368
-
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
Q0K368
-
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
Q0KAI3
-
-
-
r
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
-
-
-
r
CoA + acetoacetyl-CoA
2 acetyl-CoA
A4YEH9
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
A4YEH9
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
B1YB71
the enzyme is involved in autotrophic carbon fixation
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
B1YB71
the enzyme is involved in autotrophic carbon fixation
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
Q12598
cytosolic thiolase I is essential for the mevalonate pathway
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
enzyme of fatty acid oxidation cycle
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
peroxisomal thiolase most probably catalyzes the first reaction in peroxisomal cholesterol and dolichol synthesis
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
liver mitochondrial isoenzyme catalyzes the first step in biosynthesis of ketone bodies
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
P07256
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
P07097
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
involved in generation of acetoacetyl-CoA for poly-beta-hydroxybutyrate synthesis
-
?
additional information
?
-
-
the enzyme shows degradative thiolase activity by converting 3-ketoacyl-CoA to acyl-CoA
-
-
-
additional information
?
-
Q0KAI3
the enzyme shows degradative thiolase activity by converting 3-ketoacyl-CoA to acyl-CoA
-
-
-
additional information
?
-
Q0K368
the enzyme shows degradative thiolase activity by converting 3-ketoacyl-CoA to acyl-CoA
-
-
-
additional information
?
-
-
the enzyme shows degradative thiolase activity by converting 3-oxoacyl-CoA to acyl-CoA
-
-
-
additional information
?
-
Q0K368
the enzyme shows degradative thiolase activity by converting 3-ketoacyl-CoA to acyl-CoA
-
-
-
additional information
?
-
Q0KAI3
the enzyme shows degradative thiolase activity by converting 3-ketoacyl-CoA to acyl-CoA
-
-
-
additional information
?
-
-
the enzyme shows degradative thiolase activity by converting 3-oxoacyl-CoA to acyl-CoA
-
-
-
additional information
?
-
-
no activity is observed with acetyl-CoA
-
-
-
additional information
?
-
-
the enzyme plays a more important role in the activation of ketogenesis in Squalus acanthias than in mammals and birds
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
-
enzyme contains selenomethionine
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Mn2+
-
can replace Mg2+, 5 mM, 90% of activity with Mg2+, inhibition above
additional information
not stimulated by Ni2+, Ca2+ and Zn2+
Mg2+
maximal activity at 5 mM
Mg2+
-
maximal activity at 5-10 mM, inhibition above
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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-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
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
dec-3-ynoic acid
-
irreversible inhibition
Dithionitrobenzoate
-
low but significant inhibition
thiolactomycin
-
0.36 mM, 50% inhibition
acetoacetyl-CoA
-
-
acetoacetyl-CoA
-
substrate inhibition above 0.105 mM
acetoacetyl-CoA
-
substrate inhibition beyond 0.0225 mM
acetoacetyl-CoA
-
isoenzyme A: above 0.015 mM, isoenzyme B: above 0.01 mM
CoA
-
both directions
CoA
-
inhibition in condensation direction
CoA
-
higher than 0.03 mM, inhibition in cleavage direction
CoA
-
competitive vs. acetoacetyl-CoA in thiolysis
CoA
-
substrate inhibition above 0.05 mM, 50% inhibition of synthesis at 0.06 mM in bacteroids
iodoacetamide
-
0.5 mM, 96% inhibition, acetoacetyl-CoA partly protects
iodoacetamide
-
0.3 mM, 93% inhibition after 30 min
iodoacetamide
-
2 mM, complete inactivation after approx. 60 min, 0.3 mM acetoacetyl-CoA or 1.6 mM acetyl-CoA protect
iodoacetamide
-
0.005 mM, inactivation half-life: 3 min
iodoacetamide
-
0.4 mM, 36% inhibition
iodoacetamide
-
125fold molar excess, rapid inactivation
iodoacetamide
-
reacts with Cys89
Mg2+
inhibitory at concentrations higher than 5 mM
Mg2+
-
60 mM, 45% inhibition of thiolysis, 69% inhibition of synthesis
Mg2+
-
inhibits the rate of acetoacetyl-CoA thiolysis but not the rate of synthesis of acetoacetyl-CoA
Mg2+
-
2 and 5 mM, 20 and 40% inhibition of synthesis, respectively
N-ethylmaleimide
-
-
N-ethylmaleimide
-
0.4 mM, 53% inhibition
NADH
-
inhibition of thiolysis
NADH
-
inhibition of thiolysis
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
0.4 mM, 95% inhibition
Sodium borohydride
-
-
Sodium borohydride
-
inactivation in the presence of either acetoacetyl-CoA or acetyl-CoA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KCl
-
maximal activity at 4.5 M
lovostatin
-
1.9fold activity increase in rats treated with lovostatin
NaCl
-
maximal activity at 4.5 M
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
additional information
additional information
Michaelis-Menten kinetics
-
0.0038
acetoacetyl-CoA
-
native thiolase
0.004
acetoacetyl-CoA
-
isoenzyme B, thiolysis
0.005
acetoacetyl-CoA
-
E252del mutant enzyme; wild-type enzyme
0.006
acetoacetyl-CoA
-
isoenzyme A, thiolysis
0.0062
acetoacetyl-CoA
-
C92S mutant thiolase
0.009
acetoacetyl-CoA
-
peroxisomal thiolase, thiolysis
0.0098
acetoacetyl-CoA
-
recombinant thiolase
0.01
acetoacetyl-CoA
-
isoenzyme A, thiolysis
0.01
acetoacetyl-CoA
-
mutant enzyme E252del; wild-type enzyme
0.011
acetoacetyl-CoA
-
-
0.016
acetoacetyl-CoA
-
cytosolic thiolase, thiolysis
0.019
acetoacetyl-CoA
-
-
0.02067
acetoacetyl-CoA
at pH 8.9 and 25°C
0.023
acetoacetyl-CoA
-
recombinant cytosolic thiolase I, thiolysis
0.024
acetoacetyl-CoA
-
-
0.025
acetoacetyl-CoA
-
-
0.025
acetoacetyl-CoA
-
peroxisomal thiolase I, thiolysis
0.032
acetoacetyl-CoA
-
isoenzyme B, thiolysis
0.032
acetoacetyl-CoA
-
-
0.035
acetoacetyl-CoA
-
peroxisomal thiolase, synthesis
0.0385
acetoacetyl-CoA
-
-
0.042
acetoacetyl-CoA
-
cytosolic thiolase I, thiolysis
0.042
acetoacetyl-CoA
-
thiolysis
0.05
acetoacetyl-CoA
-
pH 6.0, 37°C
0.057
acetoacetyl-CoA
-
recombinant peroxisomal thiolase I, thiolysis
0.08
acetoacetyl-CoA
-
cytosolic thiolase, synthesis
0.088
acetoacetyl-CoA
-
thiolysis
0.15
acetoacetyl-CoA
pH 7.8, 85°C
0.158
acetoacetyl-CoA
-
pH 8.3, 30°C, recombinant enzyme
0.18
acetoacetyl-CoA
pH 7.5, 70°C
0.0062
acetyl-CoA
-
isoenzyme A
0.0258
acetyl-CoA
at pH 8.9 and 25°C
0.03
acetyl-CoA
-
isoenzyme A, in the presence of 3.5 mM NH4+
0.08
acetyl-CoA
-
enzyme B
0.091
acetyl-CoA
-
isoenzyme A, synthesis; isoenzyme B, synthesis
0.38
acetyl-CoA
-
enzyme from bacteroids
0.47
acetyl-CoA
-
synthesis
0.6
acetyl-CoA
-
synthesis
0.69
acetyl-CoA
-
recombinant cytosolic thiolase I, thiolysis
0.74
acetyl-CoA
-
recombinant peroxisomal thiolase I, thiolysis
0.77
acetyl-CoA
-
cytosolic thiolase I, thiolysis
1.05
acetyl-CoA
-
peroxisomal thiolase I, thiolysis
1.06
acetyl-CoA
-
synthesis
0.0048
CoA
-
-
0.008
CoA
-
peroxisomal thiolase, thiolysis
0.02
CoA
-
cytosolic thiolase, thiolysis
0.025
CoA
-
isoenzyme A, thiolysis
0.028
CoA
-
wild-type enzyme
0.03
CoA
-
peroxisomal thiolase I, thiolysis
0.032
CoA
-
recombinant peroxisomal thiolase I, thiolysis
0.037
CoA
-
cytosolic thiolase I, thiolysis
0.05
CoA
-
recombinant cytosolic thiolase I, thiolysis
0.05
CoA
-
E252del mutant enzyme; mutant enzyme E252del
0.154
CoA
-
isoenzyme B, thiolysis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
14
3-ketobutyryldithio-CoA
-
-
266
acetoacetyl-10-bis-demethylpantetheine 11-pivaloate
-
-
-
0.0767 - 5000000
acetoacetyl-CoA
353
acetoacetyl-S-(11-methoxymethyl)pantetheine
-
-
434
acetoacetyl-S-(11-t-butyldimethylsilyl)pantetheine
-
-
469
acetoacetyl-S-(D-pantetheine) 11-pivalate
-
-
256
acetoacetyl-S-(L-pantetheine) 11-pivalate
-
-
177
acetoacetyl-S-homopantetheine 12-pivalate
-
-
14 - 174
acetoacetyl-S-pantetheine
29.5
CoA
-
presence of Mg2+
900
thiolytic cleavage
-
-
-
0.0767
acetoacetyl-CoA
-
C92S mutant thiolase
36.2
acetoacetyl-CoA
-
native thiolase
40.1
acetoacetyl-CoA
-
recombinant thiolase
80
acetoacetyl-CoA
-
pH 6.0, 37°C
1000
acetoacetyl-CoA
pH 7.5, 70°C
3833
acetoacetyl-CoA
at pH 8.9 and 25°C
5000000
acetoacetyl-CoA
-
pH 8.3, 30°C, recombinant enzyme
14
acetoacetyl-S-pantetheine
-
-
174
acetoacetyl-S-pantetheine
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5600 - 31650
acetoacetyl-CoA
5600
acetoacetyl-CoA
pH 7.5, 70°C
31650
acetoacetyl-CoA
-
pH 8.3, 30°C, recombinant enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
0.0014 - 0.0016
acetoacetyl-CoA
0.0014
acetoacetyl-CoA
-
isoenzyme A
0.0016
acetoacetyl-CoA
-
isoenzyme A
0.006
CoA
-
enzyme from bacteroids
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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,
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.16
-
acetoacetyl-CoA synthesis
0.9
crude enzyme, at pH 8.9 and 25°C
13.2
purified native enzyme
15.78
purified recombinant enzyme
56
after 62.22fold purification, at pH 8.9 and 25°C
100 - 130
-
peroxisomal thiolase, thiolysis
412
-
thiolysis of acetoacetyl-CoA
additional information
-
assay method
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
8.1 - 8.4
-
isoenzyme A and B, acetoacetyl-CoA synthesis
8.4
-
cleavage of acetoacetyl-CoA, 85% of maximal activity between pH 8.0 and pH 9.0
7.5
-
7.8
-
thiolysis
7.8
-
thiolysis, more than 90% of maximal activity between pH 7.5 and pH 8.3
8.1
-
cytosolic and peroxisomal thiolase I, synthesis
8.1
-
synthesis, more than 90% of maximal activity between pH 7.5 and pH 8.5
8.3
-
cytosolic and peroxisomal thiolase I
8.5
-
505 of maximal activity at pH 7.5 and pH 9.5, no activity below pH 6.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
30
-
assay at
37
-
assay at
37
-
acetoacetyl-CoA synthesis and thiolysis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
6.2
calculated from amino acid sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
isoform AACT! is highly expressed in root tips, young leaf, top stem and anther
brenda
-
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
brenda
-
-
brenda
-
brenda
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
brenda
; low ACT1 expression
brenda
-
brenda
highest expression in roots and petals
brenda
-
brenda
-
brenda
-
brenda
etiolated
brenda
-
brenda
-
brenda
isoform AACT! is primarily expressed in the vascular system
brenda
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
brenda
-
brenda
isoform AACT! is highly expressed in root tips, young leaf, top stem and anther
brenda
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
acetoacetyl-CoA thiolase activity in isolated liver mitochondria is markedly increased in the ketotic dogfish compared to the recently captured fish
brenda
; low ACT1 expression
brenda
isoform AACT! is highly expressed in root tips, young leaf, top stem and anther
brenda
highest expression in roots and petals
brenda
isoform AACT! is highly expressed in root tips, young leaf, top stem and anther
brenda
-
brenda
-
-
brenda
additional information
ACT2 is expressed at relatively high level in all plant tissues; the expression of ACT1 is restricted to roots and inflorescences and its transcript is present at very low levels
brenda
additional information
ACT2 is expressed at relatively high level in all plant tissues; the expression of ACT1 is restricted to roots and inflorescences and its transcript is present at very low levels
brenda
additional information
mRNA is ubiquitously expressed in 6 adult tissues including pheromone gland; Osat1 is expressed in all adult tissues
brenda
additional information
-
mRNA is ubiquitously expressed in 6 adult tissues including pheromone gland; Osat1 is expressed in all adult tissues
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
isozyme AACT2
brenda
-
-
brenda
-
-
-
brenda
isozyme AACT2
brenda
N-terminal sequence targets thiolase I to the peroxisome
brenda
-
cytosolic thiolase I
brenda
-
-
brenda
-
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
-
brenda
-
-
brenda
-
isoform Acat1
brenda
-
isoform Acat1
-
brenda
-
-
brenda
isozyme AACT1, its peroxisomal localisation depends on the presence of a C-terminal peroxisomal targeting sequence, PTS1, motif, Ser-Ala-Leu
brenda
-
-
brenda
-
peroxisomal thiolase I
brenda
-
-
brenda
-
-
-
brenda
-
-
brenda
additional information
-
not detected in peroxisomes
-
brenda
additional information
-
not detected in peroxisomes
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
P45855
Bacillus subtilis (strain 168);
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787);
A0A0R4I970
Clostridium acetobutylicum (strain EA 2018);
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337);
A0A077EEP0
Elizabethkingia anophelis NUHP1;
Escherichia coli (strain K12);
A0A0H2ZTN6
Mycobacterium avium (strain 104);
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100);
Peptoclostridium difficile (strain 630);
Saccharomyces cerevisiae (strain ATCC 204508 / S288c);
P45359
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787);
P45359
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787);
P14611
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337);
P14611
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337);
P14611
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337);
P76461
Escherichia coli (strain K12);
P76461
Escherichia coli (strain K12);
P76461
Escherichia coli (strain K12);
Q9BWD1
Homo sapiens;
Q4WCL5
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100);
Q4WCL5
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100);
Q4WCL5
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100);
Q4WCL5
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100);
Q4WCL5
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100);
Q4WCL5
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100);
Q4WCL5
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100);
Q18AR0
Peptoclostridium difficile (strain 630);
Q183B0
Peptoclostridium difficile (strain 630);
P41338
Saccharomyces cerevisiae (strain ATCC 204508 / S288c);
P41338
Saccharomyces cerevisiae (strain ATCC 204508 / S288c);
P07097
Zoogloea ramigera;
P07097
Zoogloea ramigera;
P07097
Zoogloea ramigera;
P07097
Zoogloea ramigera;
P07097
Zoogloea ramigera;
P07097
Zoogloea ramigera;
P07097
Zoogloea ramigera;
P07097
Zoogloea ramigera;
P07097
Zoogloea ramigera;
P07097
Zoogloea ramigera;
P07097
Zoogloea ramigera;
P07097
Zoogloea ramigera;
P07097
Zoogloea ramigera;
P07097
Zoogloea ramigera;
P07097
Zoogloea ramigera;
P07097
Zoogloea ramigera;
P07097
Zoogloea ramigera;
P07097
Zoogloea ramigera;
P07097
Zoogloea ramigera;
P07097
Zoogloea ramigera;
P07097
Zoogloea ramigera;
P07097
Zoogloea ramigera;
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
30000
x * 30000, SDS-PAGE
39000
-
4 * 39000, SDS-PAGE
40495
-
4 * 40495, electrospray ionization mass spectroscopy
40598
4 * 40598, deduced from nucleotide sequence
41200
x * 41200, calculated, x * 40000, SDS-PAGE
41320
x * 41320, calculated from amino acid sequence
42444
x * 42444, calculated from sequence
43445
x * 43445, calculated, x * 43000, SDS-PAGE
45000
-
x * 45000, SDS-PAGE
47000
x * 47000, recombinant enzyme, SDS-PAGE
53000
x * 53000, SDS-PAGE
60000
-
2 * 60000, SDS-PAGE
63000
-
x * 63000, SDS-PAGE
84000
-
about, recombinant His-tagged enzyme, gel filtration
86496
-
x * 86496, deduced from nucleotide sequence
88712
-
x * 88712, MALDI-mass spectrometry
147600
-
isoenzyme B, sedimentation analysis
150000
-
isoenzyme A, gel filtration
151000
-
gel filtration, isoenzyme A and B
154600
-
isoenzyme A, sedimentation analysis
156000
-
sucrose density gradient sedimentation
160000
-
peroxisomal thiolase, gel filtration
169000
-
sedimentation equilibrium
185000
-
native thiolase, gel filtration
187000
-
recombinant thiolase, gel filtration
240000
-
peroxisomal thiolase I, gel filtration
250000
-
cytosolic thiolase I, gel filtration
40000
-
4 * 40000, enzyme A and B, SDS-PAGE
40000
x * 41200, calculated, x * 40000, SDS-PAGE
40000
-
2 * 40000, recombinant His-tagged enzyme, SDS-PAGE
41000
-
4 * 41000, SDS-PAGE
41000
-
6 * 41000, SDS-PAGE
41000
-
4 * 41000, SDS-PAGE
41000
-
6 * 41000, cytosolic and peroxisomal thiolase I, SDS-PAGE
42000
-
4 * 42000, SDS-PAGE
42000
-
4 * 42000, peroxisomal thiolase, SDS-PAGE
42000
-
2 * 42000, recombinant His-tagged enzyme, SDS-PAGE
43000
-
2 * 43000, CTAB-PAGE
43000
x * 43445, calculated, x * 43000, SDS-PAGE
43000
-
x * 43000, SDS-PAGE
43000
x * 43000, SDS-PAGE
44000
-
4 * 44000, SDS-PAGE
44000
-
4 * 44000, SDS-PAGE
44000
-
4 * 44000, SDS-PAGE
44000
-
4 * 44000, SDS-PAGE
80000
-
gel filtration
80000
-
recombinant His-tagged enzyme, gel filtration
152000
-
isoenzyme B, gel filtration
152000
-
analytical ultracentrifugation
155000
-
gel filtration
155000
-
isoenzyme I, gel filtration
180000
-
gel filtration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
homotetramer
-
x-ray crystallography
?
x * 41320, calculated from amino acid sequence; x * 43000, SDS-PAGE
?
x * 43445, calculated, x * 43000, SDS-PAGE
?
-
x * 43000, SDS-PAGE
-
?
-
x * 86496, deduced from nucleotide sequence; x * 88712, MALDI-mass spectrometry
?
composed of two different types of subunits: catalytic subunit PhaAalpha, and subunit PhaABbeta
?
-
composed of two different types of subunits: catalytic subunit PhaAalpha, and subunit PhaABbeta
-
?
x * 47000, recombinant enzyme, SDS-PAGE
?
x * 41200, calculated, x * 40000, SDS-PAGE; x * 42100
?
x * 42444, calculated from sequence
?
-
x * 42444, calculated from sequence
-
dimer
-
2 * 42000, recombinant His-tagged enzyme, SDS-PAGE
dimer
-
2 * 43000, CTAB-PAGE; 2 * 60000, SDS-PAGE
dimer
-
2 * 43000, CTAB-PAGE; 2 * 60000, SDS-PAGE
-
hexamer
-
6 * 41000, SDS-PAGE
hexamer
-
6 * 41000, cytosolic and peroxisomal thiolase I, SDS-PAGE
homodimer
-
2 * 40000, recombinant His-tagged enzyme, SDS-PAGE
homodimer
-
enzyme ReH16_A1887 exists as a dimer both in the crystal and in solution. The interaction between alpha3 and alpha5 from the other chain also mediates the dimerization through hydrophobic interactions with residues Glu30, Leu74, Val71, Ile192, Ser139, Met140, Arg143 and Tyr 144
homodimer
-
2 * 40000, recombinant His-tagged enzyme, SDS-PAGE; enzyme ReH16_A1887 exists as a dimer both in the crystal and in solution. The interaction between alpha3 and alpha5 from the other chain also mediates the dimerization through hydrophobic interactions with residues Glu30, Leu74, Val71, Ile192, Ser139, Met140, Arg143 and Tyr 144
-
tetramer
-
4 * 39000, SDS-PAGE
tetramer
-
4 * 44000, SDS-PAGE
tetramer
-
4 * 44000, SDS-PAGE
tetramer
-
4 * 41000, SDS-PAGE
tetramer
-
4 * 38000-40000, SDS-PAGE
tetramer
-
4 * 42000, SDS-PAGE
tetramer
-
4 * 41000, SDS-PAGE
tetramer
four identical subunits
tetramer
-
4 * 40000, enzyme A and B, SDS-PAGE
tetramer
-
4 * 42000, peroxisomal thiolase, SDS-PAGE
tetramer
-
4 * 44000, SDS-PAGE
tetramer
-
4 * 45000-47000, native thiolase, SDS-PAGE; 4 * 46000-48000, recombinant thiolase, SDS-PAGE
tetramer
-
4 * 44000, SDS-PAGE
tetramer
; 4 * 40598, deduced from nucleotide sequence
tetramer
-
4 * 40495, electrospray ionization mass spectroscopy
additional information
-
composed of two different types of subunits: catalytic subunit BktBalpha, and BktBbeta
additional information
composed of two different types of subunits: catalytic subunit BktBalpha, and BktBbeta
additional information
composed of two different types of subunits: catalytic subunit BktBalpha, and BktBbeta
additional information
-
composed of two different types of subunits: catalytic subunit BktBalpha, and BktBbeta
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
hanging drop vapor diffusion method, using 100 mM phosphate-citrate pH 4.2, 10% (w/v) polyethylene glycol 3350, 200 mM sodium chloride
purified recombinant enzyme in apoform and with bound CoA, hanging drop vapor diffusion method, mixing 0.001 ml of 40 mg/ml protein in 40 mM Tris-HCl, pH 8.0, and 5 mM 2-mercaptoethanol, with 0.001 ml of reservoir solution containing 1.0 M ammonium sulfate, 0.1 M HEPES, pH 7.25, and equilibration against 0.5 ml of reservoir solution, 20°C, 3 days, X-ray diffraction structure determination and analysis at 2.0-2.3 A resolution, molecular replacement method using the structure of Mycobacterium tuberculosis thiolase Mttt0182, PDB ID1ULQ, as a search model, structure modeling
purified recombinant enzyme in apoform or with bound CoA, hanging drop vapor diffusion method, mixing 0.0012 ml of 25 mg/ml protein in 40 mM Tris-HCl, pH 8.0, with 0.0012 ml of reservoir solution containing 17% PEG 8000, 0.1 M HEPES pH 7.0, and equilibration against 0.5 ml of reservoir solution, 20-22°C, 7 days, X-ray diffraction structure determination and analysis at 1.4-1.5 A resolution, molecular replacement method using the structure of Mycobacterium tuberculosis thiolase MtFadA5, PDB ID 4UBU as a search model, structure modeling
-
purified recombinant enzyme, sitting drop vapour diffusion method, mixing of 0.001 ml of 140 mg/ml protein in 40 mM Tris-HCl, pH 8.0, with 0.001 ml of reservoir solution containing 17% PEG 8000, 0.1 M HEPES pH 7.0, and equilibration against 0.5 ml of reservoir solution, 20°C, 7 days, X-ray diffraction structure determination and analysis at 1.4 A resolution
-
hanging drop vapor diffusion method at 4°C. Unliganded and liganded (with CoA and with K+) structures of the human mitochondrial recombinant tetrameric thiolase
-
only successful in the presence of CoA
microbatch method, using either 20% (w/v) PEG 3350, 0.15 M calcium chloride dehydrate, or 45% (w/v) PEG 200, 0.1 M MES monohydrate pH 6.0, 0.07 M calcium chloride dehydrate or 0.2 M sodium acetate trihydrate, 0.1 M sodium cacodylate trihydrate pH 6.5, 30% (w/v) PEG 8000, 5% (v/v) n-octyl-beta-D-glucoside
-
hangig-drop vapor diffusion at 21°C, 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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0
-
1 h, complete loss of activity
37
-
wild-type T2 protein is stable even after chasing for 48 h at 37°C. 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 37°C