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Enzyme Nomenclature
Information on EC 2.3.1.9 - acetyl-CoA C-acetyltransferase
for references in articles please use BRENDA:EC2.3.1.9
Word Map on EC 2.3.1.9
- 2.3.1.9
- ketone
- mevalonate
- acetoacetate
- hmg-coa
-
beta-oxidation
- 3-hydroxybutyrate
- 2-methyl-3-hydroxybutyrate
- 3-hydroxy-3-methylglutaryl-coa
-
acetoacetyl-coenzyme
-
tiglylglycine
-
ketoacidotic
-
ketogenesis
- beta-ketothiolase
-
coa-transferase
- 3-hydroxyacyl-coa
- 3-ketothiolase
- 3-oxoacyl-coas
-
thiolytic
- acylcarnitine
- coash
-
aacts
-
ketogenic
- 2-methylacetoacetate
-
ketone-body
-
lyso-paf
- 3-hydroxybutyryl-coa
- synthesis
- biofuel production
- analysis
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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EC NUMBER 
COMMENTARY 
2.3.1.9
-
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RECOMMENDED NAME
GeneOntology No.
acetyl-CoA C-acetyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 acetyl-CoA = CoA + acetoacetyl-CoA
mechanism; 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
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
Claisen condensation
condensation
-
-
-
-
thiolytic cleavage
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:acetyl-CoA C-acetyltransferase
-
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CAS REGISTRY NUMBER
COMMENTARY
9027-46-7
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
I3R3D1: catalytic subunit PhaAalpha, I3RA71: subunit PhaAbeta
I3R3D1 and I3R3D0
UniProt
I3RA72: catalytic subunit BktBalpha, I3RA71: subunit BktBbeta
I3RA72 and I3RA71
UniProt
I3R3D1: catalytic subunit PhaAalpha, I3RA71: subunit PhaAbeta
I3R3D1 and I3R3D0
UniProt
I3RA72: catalytic subunit BktBalpha, I3RA71: subunit BktBbeta
I3RA72 and I3RA71
UniProt
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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
-
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-oxoacyl-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
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; 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
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
I3R3D1 and I3R3D0, I3RA72 and I3RA71
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
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; 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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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
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
-
r
2 acetyl-CoA
CoA + acetoacetyl-CoA
I3R3D1 and I3R3D0, I3RA72 and I3RA71
-
-
-
?
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
-
-
-
?
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-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
I3R3D1 and I3R3D0, I3RA72 and I3RA71
-
-
-
?
acetyl-CoA + propionyl-CoA
CoA + 3-oxopentanoyl-CoA
I3R3D1 and I3R3D0, I3RA72 and I3RA71
-
-
-
?
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
-
-
-
-
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
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
?
-
-
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
?
-
-
the catalytic triad of BktBalpha is likely to be Ser-His-His
-
-
-
additional information
?
-
I3R3D1 and I3R3D0
the catalytic triad of BktBalpha is likely to be Ser-His-His
-
-
-
additional information
?
-
I3RA72 and I3RA71
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
?
-
I3R3D1 and I3R3D0
the catalytic triad of PhaAalpha is likely to be Ser-His-His
-
-
-
additional information
?
-
I3RA72 and I3RA71
the catalytic triad of PhaAalpha is likely to be Ser-His-His
-
-
-
additional information
?
-
I3R3D1 and I3R3D0
the catalytic triad of PhaAalpha is likely to be Ser-His-His
-
-
-
additional information
?
-
I3RA72 and I3RA71
the catalytic triad of PhaAalpha is likely to be Ser-His-His
-
-
-
additional information
?
-
I3R3D1 and I3R3D0
the catalytic triad of BktBalpha is likely to be Ser-His-His
-
-
-
additional information
?
-
I3RA72 and 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 SUBSTRATES
NATURAL PRODUCTS
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
B7XEI5
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
Q0KAI3
-
-
-
r
2 acetyl-CoA
CoA + acetoacetyl-CoA
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
-
r
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)
-
-
?
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
CoA + acetoacetyl-CoA
2 acetyl-CoA
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
Q0K368
-
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
Q0KAI3
-
-
-
r
CoA + acetoacetyl-CoA
2 acetyl-CoA
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
-
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
Q12598
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
?
-
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
?
-
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
Q0K368
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
Q0KAI3
the enzyme shows degradative thiolase activity by converting 3-ketoacyl-CoA to acyl-CoA
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additional information
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Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
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the enzyme shows degradative thiolase activity by converting 3-oxoacyl-CoA to acyl-CoA
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additional information
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no activity is observed with acetyl-CoA
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additional information
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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-
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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+
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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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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,3-pentadienoyl-S-pantetheine 11-pivalate
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half-life for inactivation: 1.9 min
2-Oxo-5-(1-hydroxy-2,4,6-heptatriynyl)-1,3-dioxolone-4-heptanoic acid
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natural product isolated from actinomycete culture L-660,631, IC50: 0.00001 mM,
3-butynoyl-CoA
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0.01 mM, 95% inactivation after 10 min, acetoacetyl-CoA or 0.8 mM CoA protect
3-Pentenoyl-S-pantetheine 11-pivalate
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half-life for inactivation: 0.26 min
3-Pentynoyl-CoA
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0.1 mM, complete inactivation after 10 min, acetoacetyl-CoA or 0.8 mM CoA protect
4-Bromocrotonyl-CoA
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0.1 mM, complete inactivation after 10 min, acetoacetyl-CoA protects
CoA
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substrate inhibition above 0.05 mM, 50% inhibition of synthesis at 0.06 mM in bacteroids
iodoacetamide
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0.5 mM, 96% inhibition, acetoacetyl-CoA partly protects
iodoacetamide
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2 mM, complete inactivation after approx. 60 min, 0.3 mM acetoacetyl-CoA or 1.6 mM acetyl-CoA protect
Mg2+
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60 mM, 45% inhibition of thiolysis, 69% inhibition of synthesis
Mg2+
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inhibits the rate of acetoacetyl-CoA thiolysis but not the rate of synthesis of acetoacetyl-CoA
Sodium borohydride
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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
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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
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cleavage of acetoacetyl-CoA, 85% of maximal activity between pH 8.0 and pH 9.0
8.5
8.5
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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
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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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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
isoform AACT! is highly expressed in root tips, young leaf, top stem and anther
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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
isoform AACT! is primarily expressed in the vascular system
additional information
isoform AACT! is highly expressed in root tips, young leaf, top stem and anther
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acetoacetyl-CoA thiolase activity in isolated liver mitochondria is markedly increased in the ketotic dogfish compared to the recently captured fish
isoform AACT! is highly expressed in root tips, young leaf, top stem and anther
isoform AACT! is highly expressed in root tips, young leaf, top stem and anther
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
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
additional information
mRNA is ubiquitously expressed in 6 adult tissues including pheromone gland; Osat1 is expressed in all adult tissues
additional information
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mRNA is ubiquitously expressed in 6 adult tissues including pheromone gland; Osat1 is expressed in all adult tissues
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
N-terminal sequence targets thiolase I to the peroxisome
isozyme AACT1, its peroxisomal localisation depends on the presence of a C-terminal peroxisomal targeting sequence, PTS1, motif, Ser-Ala-Leu
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Clostridium acetobutylicum (strain EA 2018)
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
41000
42000
43000
44000
80000
152000
155000
180000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
homodimer
tetramer
additional information
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x * 86496, deduced from nucleotide sequence; x * 88712, MALDI-mass spectrometry
?
I3R3D1 and I3R3D0, I3RA72 and I3RA71
composed of two different types of subunits: catalytic subunit PhaAalpha, and subunit PhaABbeta
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composed of two different types of subunits: catalytic subunit PhaAalpha, and subunit PhaABbeta
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homodimer
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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
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
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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
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tetramer
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4 * 45000-47000, native thiolase, SDS-PAGE; 4 * 46000-48000, recombinant thiolase, SDS-PAGE
additional information
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composed of two different types of subunits: catalytic subunit BktBalpha, and BktBbeta
additional information
I3R3D1 and I3R3D0
composed of two different types of subunits: catalytic subunit BktBalpha, and BktBbeta
additional information
I3RA72 and I3RA71
composed of two different types of subunits: catalytic subunit BktBalpha, and BktBbeta
additional information
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composed of two different types of subunits: catalytic subunit BktBalpha, and BktBbeta
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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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
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hanging drop vapor diffusion method at 4°C. Unliganded and liganded (with CoA and with K+) structures of the human mitochondrial recombinant tetrameric thiolase
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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
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hangig-drop vapor diffusion at 21°C, crystal structure at 2.0 A resolution
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wild-type thiolase and acetylated thiolase complexed with CoA, C89A mutant thiolase complexed with acetyl-CoA and acetoacetyl-CoA, Q64A mutant thiolase
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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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
60
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
labile enzyme, partially stabilized by 1-2 mM dithiothreitol and 20% ethylene glycol
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more than 10% sucrose, 2-mercaptoethanol or dithiothreitol are necessary to maintain activity
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urea: 2.5 M, 17 h, 50% loss of activity, 5 M, 45 min, 50% loss of activity, 7 M, 1 min, 50% loss of activity
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10°C, less than 0.2 mg/ml protein, 50 mM Tris, pH 7.2, 0.5 mM dithiothreitol, 8 d, 60-70% loss of activity
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-20°C, 20 mM Tris-HCl, pH 7.8, 0.5 mM 1 mM, EDTA, 15 d, loss of more than 50% activity