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Information on EC 2.3.1.9 - acetyl-CoA C-acetyltransferase
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2.3.1.9 acetyl-CoA C-acetyltransferaseIUBMB Comments
The enzyme, found in both eukaryotes and prokaryotes, catalyses the Claisen condensation of an acetyl-CoA and an acyl-CoA (often another acetyl-CoA), leading to the formation of an acyl-CoA that is longer by two carbon atoms. The reaction starts with the acylation of a nucleophilic cysteine at the active site, usually by acetyl-CoA but potentially by a different acyl-CoA, with concomitant release of CoA. In the second step the acyl group is transferred to an acetyl-CoA molecule. cf. EC 2.3.1.16, acetyl-CoA C-acyltransferase.
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Word Map
- 2.3.1.9
- ketone
- mevalonate
- hmg-coa
- acetoacetate
-
beta-oxidation
- beta-ketothiolase
- 3-hydroxy-3-methylglutaryl-coa
- 3-hydroxybutyrate
-
acetoacetyl-coenzyme
- 2-methyl-3-hydroxybutyrate
-
tiglylglycine
-
aacts
-
ketogenesis
-
ketoacidotic
-
coa-transferase
- 2-methylacetoacetate
- 3-ketothiolase
-
thiolytic
- 3-oxoacyl-coas
- 3-hydroxyacyl-coa
- coash
-
lyso-paf
- 3-hydroxybutyryl-coa
-
ketone-body
- synthesis
- analysis
- biofuel production
The enzyme appears in viruses and cellular organisms
Reaction Schemes
2
=
+
Synonyms
2-methylacetoacetyl-CoA thiolase, 3-ketoacyl-CoA (T1)-like thiolase, 3-ketoacyl-CoA thiolase, 3-ketoacyl-coenzyme A thiolase, 3-oxothiolase, A1887, AACT, AACT1, AACT2, ACAT, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-methylacetoacetyl-CoA thiolase
-
-
-
-
3-ketoacyl-CoA thiolase
3-ketoacyl-coenzyme A thiolase
3-oxothiolase
-
-
-
-
A1887
AACT
AACT1
ACAT
ACAT1
ACAT2
ACCT
acetoacetyl CoA thiolase
acetoacetyl-CoA acetyltransferase
acetoacetyl-CoA thiolase
acetyl coenzyme A thiolase
-
-
-
-
acetyl-CoA acetyltransferase
acetyl-CoA C-acetyltransferase
acetyl-CoA:N-acetyltransferase
-
-
-
-
acetyltransferase, acetyl coenzyme A
-
-
-
-
ACTRANS
AFUB_000550
beta-acetoacetyl coenzyme A thiolase
-
-
-
-
beta-ketothiolase
ERG10
Erg10A
HFX_1022
HFX_1023
HFX_6003
HFX_6004
KACT
Msed_0656
phaA
thiolase II
Tneu_0249
type II thiolase
acetoacetyl CoA thiolase
-
-
-
-
acetoacetyl-CoA thiolase
-
-
-
-
acetyl-CoA acetyltransferase
-
-
-
-
thiolase II
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + [acetyl-CoA C-acetyltransferase]-L-cysteine = [acetyl-CoA C-acetyltransferase]-S-acetyl-L-cysteine + CoA
(1a)
-
-
-
[acetyl-CoA C-acetyltransferase]-S-acetyl-L-cysteine + acetyl-CoA = acetoacetyl-CoA + [acetyl-CoA C-acetyltransferase]-L-cysteine
(1b)
-
-
-
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
proposed two-step ping pong mechanism
-
2 acetyl-CoA = CoA + acetoacetyl-CoA
Claisen condensation, mechanism
2 acetyl-CoA = CoA + acetoacetyl-CoA
overall reaction
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
Claisen condensation
condensation
-
-
-
-
thiolytic cleavage
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
Benzoate degradation, Biosynthesis of secondary metabolites, Butanoate metabolism, Carbon fixation pathways in prokaryotes, Fatty acid degradation, Glyoxylate and dicarboxylate metabolism, Lysine degradation, Microbial metabolism in diverse environments, Pyruvate metabolism, Terpenoid backbone biosynthesis, Tryptophan metabolism, Valine, leucine and isoleucine degradation
MetaCyc
(R)- and (S)-3-hydroxybutanoate biosynthesis (engineered), 2-deoxy-D-ribose degradation II, 2-methylpropene degradation, 3-hydroxypropanoate/4-hydroxybutanate cycle, 4-oxopentanoate degradation, acetoacetate degradation (to acetyl CoA), acetyl-CoA fermentation to butanoate, crotonate fermentation (to acetate and cyclohexane carboxylate), ethylmalonyl-CoA pathway, glutaryl-CoA degradation, isoprene biosynthesis II (engineered), isopropanol biosynthesis (engineered), ketogenesis, ketolysis, L-glutamate degradation V (via hydroxyglutarate), L-lysine fermentation to acetate and butanoate, methyl tert-butyl ether degradation, mevalonate pathway I (eukaryotes and bacteria), mevalonate pathway II (haloarchaea), mevalonate pathway III (Thermoplasma), mevalonate pathway IV (archaea), oleate beta-oxidation, polyhydroxybutanoate biosynthesis, pyruvate fermentation to acetone, pyruvate fermentation to butanoate, pyruvate fermentation to butanol I, pyruvate fermentation to butanol II (engineered), pyruvate fermentation to hexanol (engineered), valproate beta-oxidation
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:acetyl-CoA C-acetyltransferase
The enzyme, found in both eukaryotes and prokaryotes, catalyses the Claisen condensation of an acetyl-CoA and an acyl-CoA (often another acetyl-CoA), leading to the formation of an acyl-CoA that is longer by two carbon atoms. The reaction starts with the acylation of a nucleophilic cysteine at the active site, usually by acetyl-CoA but potentially by a different acyl-CoA, with concomitant release of CoA. In the second step the acyl group is transferred to an acetyl-CoA molecule. cf. EC 2.3.1.16, acetyl-CoA C-acyltransferase.
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CAS REGISTRY NUMBER
COMMENTARY
9027-46-7
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetoacetyl-S-pantetheine + acetyldithio-CoA
acetyl-S-pantetheine + 3-ketobutyryldithio-CoA
-
-
-
r
CoA + acetoacetyl-10-bis-demethylpantetheine 11-pivaloate
acetyl-CoA + acetyl-10-bis-demethylpantetheine 11-pivaloate
-
-
-
?
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
-
-
-
?
2 acetyl-CoA
acetoacetyl-CoA + CoA
the thiolase is involved in the synthesis and catabolism of fatty acids
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
r
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
the enzyme catalyzes a reaction in the mevalonate pathway
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
the enzyme catalyzes a reaction in the mevalonate pathway
-
-
?
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
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
-
interconversion of 2 acetyl-CoA into acetoacetyl-CoA in the ketone body metabolism
-
-
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 + propionyl-CoA
CoA + 3-oxopentanoyl-CoA
-
-
-
?
acetyl-CoA + propionyl-CoA
CoA + 3-oxopentanoyl-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
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
CoA substrate binding structure, overview
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
r
CoA + acetoacetyl-CoA
2 acetyl-CoA
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
CoA binding mode, overview
-
-
r
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
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
the enzyme is involved in autotrophic carbon fixation
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
the enzyme is involved in autotrophic carbon fixation
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
the enzyme of the biosynthetic pathway for polyhydroxyalkanoates
-
-
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
-
specific for acetoacetyl-CoA, no activity with ketodecanoyl-CoA, dithiothreitol and 2-mercaptoethanol
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
cytosolic thiolase I is essential for the mevalonate pathway
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
enzyme of fatty acid oxidation cycle
-
?
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
-
thiolase II from constitutive mutant is specific for acetoacetyl-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
-
enzyme has both thiolase and acetyl-CoA:acyl carrier protein transacylase activity
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
thiolysis is preferred, highly specific for acetoacetyl-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
?
-
Erg10A is a functional acetyl-CoA acetyltransferase catalyzing both synthetic and degradative reactions
-
-
-
additional information
?
-
-
Erg10A is a functional acetyl-CoA acetyltransferase catalyzing both synthetic and degradative reactions
-
-
-
additional information
?
-
Erg10A is a functional acetyl-CoA acetyltransferase catalyzing both synthetic and degradative reactions
-
-
-
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
?
-
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
the enzyme shows degradative thiolase activity by converting 3-ketoacyl-CoA to acyl-CoA
-
-
?
additional information
?
-
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
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
?
-
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
the enzyme shows degradative thiolase activity by converting 3-ketoacyl-CoA to acyl-CoA
-
-
?
additional information
?
-
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
the enzyme shows degradative thiolase activity by converting 3-oxoacyl-CoA to acyl-CoA
-
-
?
additional information
?
-
I3R3D1; I3R3D0
the catalytic triad of BktBalpha is likely to be Ser-His-His
-
-
?
additional information
?
-
I3RA72; I3RA71
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
?
-
I3R3D1; I3R3D0
the catalytic triad of PhaAalpha is likely to be Ser-His-His
-
-
?
additional information
?
-
I3RA72; I3RA71
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
?
-
I3R3D1; I3R3D0
the catalytic triad of PhaAalpha is likely to be Ser-His-His
-
-
?
additional information
?
-
I3RA72; I3RA71
the catalytic triad of PhaAalpha is likely to be Ser-His-His
-
-
?
additional information
?
-
I3R3D1; I3R3D0
the catalytic triad of BktBalpha is likely to be Ser-His-His
-
-
?
additional information
?
-
I3RA72; I3RA71
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
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 acetyl-CoA
acetoacetyl-CoA + CoA
the thiolase is involved in the synthesis and catabolism of fatty acids
-
-
?
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
2 acetyl-CoA
CoA + acetoacetyl-CoA
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
r
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
the enzyme is responsible for supplying the precursors for biosynthesis of poly(3-hydroxybutyrate-co-3-hydroxyvalerate)
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
the enzyme catalyzes a reaction in the mevalonate pathway
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
the enzyme catalyzes a reaction in the mevalonate pathway
-
-
?
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
CoA + acetoacetyl-CoA
2 acetyl-CoA
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
r
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
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
the enzyme is involved in autotrophic carbon fixation
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
the enzyme is involved in autotrophic carbon fixation
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
the enzyme of the biosynthetic pathway for polyhydroxyalkanoates
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
cytosolic thiolase I is essential for the mevalonate pathway
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
enzyme of fatty acid oxidation cycle
-
?
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
-
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
?
-
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
the enzyme shows degradative thiolase activity by converting 3-ketoacyl-CoA to acyl-CoA
-
-
?
additional information
?
-
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
the enzyme shows degradative thiolase activity by converting 3-ketoacyl-CoA to acyl-CoA
-
-
?
additional information
?
-
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
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
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
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+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,3-pentadienoyl-S-pantetheine 11-pivalate
-
half-life for inactivation: 1.9 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
4-bromocrotonyl-CoA
-
0.1 mM, complete inactivation after 10 min, acetoacetyl-CoA protects
acetoacetyl CoA
-
thiolysis reaction shows a substrate inhibition at high concentrations; when one of the substrates (acetoacetyl CoA or CoA) is varied, while the concentrations of the second substrates (CoA or acetoacetyl CoA respectively) remain constant
CoA
-
substrate inhibition above 0.05 mM, 50% inhibition of synthesis at 0.06 mM in bacteroids
CoA
-
thiolysis reaction shows a substrate inhibition at high concentrations; when one of the substrates (acetoacetyl CoA or CoA) is varied, while the concentrations of the second substrates (CoA or acetoacetyl CoA respectively) remain constant
iodoacetamide
-
0.5 mM, 96% inhibition, acetoacetyl-CoA partly protects
iodoacetamide
-
2 mM, complete inactivation after approx. 60 min, 0.3 mM acetoacetyl-CoA or 1.6 mM acetyl-CoA protect
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
Sodium borohydride
-
inactivation in the presence of either acetoacetyl-CoA or acetyl-CoA
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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,
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.8
8.1
8.3
8.4
-
cleavage of acetoacetyl-CoA, 85% of maximal activity between pH 8.0 and pH 9.0
8.5
8.5
-
505 of maximal activity at pH 7.5 and pH 9.5, no activity below pH 6.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
cytosolic isozyme AACT2; ecotype Columbia, gene ACT2
UniProt
brenda
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
gene H16_A1887; gene H16_A1887
UniProt
brenda
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
gene H16_B0759; gene H16_B0759
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
higher expression levels in the liver, kidney, adrenal gland and ovary
brenda
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
higher expression levels in the liver, kidney, adrenal gland and ovary
brenda
-
expression of AACT in primordia (2.4fold) 33 and 15 d mycelia (2.3 fold) is significantly higher than in 9 d mycelia
brenda
higher expression levels in the liver, kidney, adrenal gland and ovary
brenda
-
expression of AACT in primordia (2.4fold) 33 and 15 d mycelia (2.3 fold) is significantly higher than in 9 d mycelia
brenda
isoform AACT! is primarily expressed in the vascular system
brenda
additional information
isoform AACT! is highly expressed in root tips, young leaf, top stem and anther
brenda
no significant difference in expression among roots, stems and leaves
brenda
higher expression levels in the liver, kidney, adrenal gland and ovary. mRNA levels in the liver rapidly increase after hatching, with a maximum on d 5 posthatching, after which they gradually decreased to adult levels
brenda
-
acetoacetyl-CoA thiolase activity in isolated liver mitochondria is markedly increased in the ketotic dogfish compared to the recently captured fish
brenda
isoform AACT! is highly expressed in root tips, young leaf, top stem and anther
brenda
no significant difference in expression among roots, stems and leaves
brenda
isoform AACT! is highly expressed in root tips, young leaf, top stem and anther
brenda
no significant difference in expression among roots, stems and leaves
brenda
additional information
ACT2 is expressed at relatively high level in all plant tissues
brenda
additional information
ACT2 is expressed at relatively high level in all plant tissues
brenda
additional information
the expression of ACT1 is restricted to roots and inflorescences and its transcript is present at very low levels
brenda
additional information
the expression of ACT1 is restricted to roots and inflorescences and its transcript is present at very low levels
brenda
additional information
immunoreactive protein is detected in all the tissues
brenda
additional information
-
immunoreactive protein is detected in all the tissues
brenda
additional information
Osat1 is expressed in all adult tissues
brenda
additional information
mRNA is ubiquitously expressed in 6 adult tissues including pheromone gland
brenda
additional information
-
mRNA is ubiquitously expressed in 6 adult tissues including pheromone gland
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
enzyme mainly distributes in the endoplasmic reticulum, vacuoles originated from endoplasmic reticulum and cytosol aound vacuoles originated from endoplasmic reticulum
brenda
enzyme mainly distributes in the endoplasmic reticulum, vacuoles originated from endoplasmic reticulum and cytosol aound vacuoles originated from endoplasmic reticulum
brenda
additional information
N-terminal sequence targets thiolase I to the peroxisome
brenda
isozyme AACT1, its peroxisomal localisation depends on the presence of a C-terminal peroxisomal targeting sequence, PTS1, motif, Ser-Ala-Leu
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
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
malfunction
-
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
Pyricularia oryzae Ku80
-
mutants with deletion of isoform Acat1 exhibit defect in virulence only, while mutants of isoform Acat2 are characterized by reduction in growth and virulence
-
metabolism
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
metabolism
the enzyme shows degradative thiolase activity catalyzing the fourth step of beta-oxidation degradative pathways by converting 3-oxoacyl-CoA to acyl-CoA
metabolism
-
the enzyme of the biosynthetic pathway for polyhydroxyalkanoates
metabolism
the enzyme catalyzes a reaction in the mevalonate pathway. Mevalonate is a building block of archaeal lipids. Three enzymes are involved in its biosynthesis: acetoacetyl-CoA thiolase (thiolase), 3-hydroxy-3-methylglutaryl (HMG)-CoA synthase (HMGCS), and HMG-CoA reductase. The thiolase reaction is highly endergonic. In the thiolase/HMGCS complex, the endergonic thiolase reaction is directly coupled to the exergonic 3-hydroxy-3-methylglutaryl (HMG)-CoA synthase reaction. A third protein spatially connects both enzymes. The two enzymes share the same substrate-binding site. Genomic information indicates that the presence of a thiolase/HMGCS complex is common in most of archaea and many bacteria
metabolism
-
the enzyme catalyzes a reaction in the mevalonate pathway. Mevalonate is a building block of archaeal lipids. Three enzymes are involved in its biosynthesis: acetoacetyl-CoA thiolase (thiolase), 3-hydroxy-3-methylglutaryl (HMG)-CoA synthase (HMGCS), and HMG-CoA reductase. The thiolase reaction is highly endergonic. In the thiolase/HMGCS complex, the endergonic thiolase reaction is directly coupled to the exergonic 3-hydroxy-3-methylglutaryl (HMG)-CoA synthase reaction. A third protein spatially connects both enzymes. The two enzymes share the same substrate-binding site. Genomic information indicates that the presence of a thiolase/HMGCS complex is common in most of archaea and many bacteria
-
metabolism
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
the enzyme shows degradative thiolase activity catalyzing the fourth step of beta-oxidation degradative pathways by converting 3-ketoacyl-CoA to acyl-CoA
-
metabolism
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
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
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
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
plants lacking isoform AACT1 function are completely viable and show no apparent growth phenotypes
physiological function
the enzyme is involved in autotrophic carbon fixation
physiological function
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
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 fatty acid metabolism, for energy or physical requirements to adapt to the host
physiological function
Erg10A is essential for the survival of Neosartoya fumigata. The reduced expression of Erg10A leads to severe morphological defects and increased susceptibility to oxidative and cell wall stresses
physiological function
expression in Saccharomyces cerevisiae complements a yeast Erg10knockout mutant
physiological function
Pyricularia oryzae Ku80
-
the activity of isoform Acat1 promotes virulence in the rice blast fungus
-
physiological function
-
Erg10A is essential for the survival of Neosartoya fumigata. The reduced expression of Erg10A leads to severe morphological defects and increased susceptibility to oxidative and cell wall stresses
-
physiological function
-
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
-
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 autotrophic carbon fixation
-
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
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
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
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
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
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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PDB
SCOP
CATH
UNIPROT
ORGANISM