Information on EC 2.3.1.9 - acetyl-CoA C-acetyltransferase

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

EC NUMBER
COMMENTARY
2.3.1.9
-
RECOMMENDED NAME
GeneOntology No.
acetyl-CoA C-acetyltransferase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 acetyl-CoA = CoA + acetoacetyl-CoA
show the reaction diagram
bi bi ping pong mechanism
-
2 acetyl-CoA = CoA + acetoacetyl-CoA
show the reaction diagram
mechanism
-
2 acetyl-CoA = CoA + acetoacetyl-CoA
show the reaction diagram
mechanism
-
2 acetyl-CoA = CoA + acetoacetyl-CoA
show the reaction diagram
mechanism; ping-pong mechanism
-
2 acetyl-CoA = CoA + acetoacetyl-CoA
show the reaction diagram
ping-pong mechanism
-
2 acetyl-CoA = CoA + acetoacetyl-CoA
show the reaction diagram
proposed two-step ping pong mechanism
-
2 acetyl-CoA = CoA + acetoacetyl-CoA
show the reaction diagram
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
show the reaction diagram
Claisen condensation, mechanism
-
2 acetyl-CoA = CoA + acetoacetyl-CoA
show the reaction diagram
Claisen condensation, mechanism
2 acetyl-CoA = CoA + acetoacetyl-CoA
show the reaction diagram
Claisen condensation, mechanism
-
2 acetyl-CoA = CoA + acetoacetyl-CoA
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
Claisen condensation
-
-
Claisen condensation
-
Claisen condensation
-
-
condensation
-
-
-
-
thiolytic cleavage
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(R)- and (S)-3-hydroxybutanoate biosynthesis
-
-
2-methylbutanoate biosynthesis
-
-
3-hydroxypropanoate/4-hydroxybutanate cycle
-
-
acetoacetate degradation (to acetyl CoA)
-
-
acetyl-CoA fermentation to butanoate II
-
-
crotonate fermentation (to acetate and cyclohexane carboxylate)
-
-
ethylmalonyl-CoA pathway
-
-
glutaryl-CoA degradation
-
-
glycerol degradation to butanol
-
-
isoprene biosynthesis II (engineered)
-
-
isopropanol biosynthesis
-
-
ketogenesis
-
-
ketolysis
-
-
L-glutamate degradation V (via hydroxyglutarate)
-
-
L-isoleucine degradation I
-
-
L-lysine fermentation to acetate and butanoate
-
-
mevalonate pathway I
-
-
mevalonate pathway II (archaea)
-
-
mevalonate pathway III (archaea)
-
-
polyhydroxybutanoate biosynthesis
-
-
pyruvate fermentation to acetone
-
-
pyruvate fermentation to butanoate
-
-
pyruvate fermentation to butanol I
-
-
pyruvate fermentation to butanol II
-
-
pyruvate fermentation to hexanol
-
-
butanoate fermentation
-
-
CO2 fixation in Crenarchaeota
-
-
mevalonate metabolism
-
-
tryptophan metabolism
-
-
Fatty acid degradation
-
-
Synthesis and degradation of ketone bodies
-
-
Valine, leucine and isoleucine degradation
-
-
Lysine degradation
-
-
Benzoate degradation
-
-
Tryptophan metabolism
-
-
Pyruvate metabolism
-
-
Glyoxylate and dicarboxylate metabolism
-
-
Propanoate metabolism
-
-
Butanoate metabolism
-
-
Carbon fixation pathways in prokaryotes
-
-
Terpenoid backbone biosynthesis
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
Microbial metabolism in diverse environments
-
-
Biosynthesis of antibiotics
-
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:acetyl-CoA C-acetyltransferase
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2-methylacetoacetyl-CoA thiolase
-
-
-
-
3-oxothiolase
-
-
-
-
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 riparia, Vitis vinifera x Vitis vinifera
-
-
acetoacetyl-CoA thiolase T2
-
-
acetyl coenzyme A thiolase
-
-
-
-
acetyl-CoA acetyltransferase
-
-
-
-
acetyl-CoA acetyltransferase
-
acetyl-CoA:N-acetyltransferase
-
-
-
-
acetyltransferase, acetyl coenzyme A
-
-
-
-
ACTRANS
Vitis vinifera x Vitis riparia, Vitis vinifera x Vitis vinifera
-
-
beta-acetoacetyl coenzyme A thiolase
-
-
-
-
beta-ketothiolase
-
beta-ketothiolase
Pyrobaculum neutrophilum DSM 2338
-
-
beta-ketothiolase
-
-
cytosolic acetoacetyl-CoA thiolase
-
-
cytosolic acetoacetyl-CoA thiolase 1
-
cytosolic acetoacetyl-CoA thiolase 2
-
HFX_1022
I3R3D1 and I3R3D0
locus name, subunit PhaAbeta
HFX_1022
Haloferax mediterranei DSM 1411
I3R3D1 and I3R3D0
locus name, subunit PhaAbeta
-
HFX_1023
I3R3D1 and I3R3D0
locus name, subunit PhaAalpha
HFX_1023
Haloferax mediterranei DSM 1411
I3R3D1 and I3R3D0
locus name, subunit PhaAalpha
-
HFX_6003
I3RA72 and I3RA71
locus name, subunit BktBbeta
HFX_6003
Haloferax mediterranei DSM 1411
I3RA72 and I3RA71
locus name, subunit BktBbeta
-
HFX_6004
I3RA72 and I3RA71
locus name, subunit BktBalpha
HFX_6004
Haloferax mediterranei DSM 1411
I3RA72 and I3RA71
locus name, subunit BktBalpha
-
MmgA
-
gene name
Msed_0656
locus name
Msed_0656
locus name
-
thiolase II
-
-
-
-
thiolase II
-
Tneu_0249
locus name
Tneu_0249
Pyrobaculum neutrophilum DSM 2338
locus name
-
CAS REGISTRY NUMBER
COMMENTARY
9027-46-7
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cytosolic acetoacetyl-CoA thiolase 1
UniProt
Manually annotated by BRENDA team
cytosolic acetoacetyl-CoA thiolase 2
UniProt
Manually annotated by BRENDA team
cytosolic isozyme AACT2; ecotype Columbia, gene ACT2
UniProt
Manually annotated by BRENDA team
isozyme AACT1; ecotype Columbia, gene ACT1
UniProt
Manually annotated by BRENDA team
gene mmgA
-
-
Manually annotated by BRENDA team
2 forms: A and B
-
-
Manually annotated by BRENDA team
3 forms: I, A, B
-
-
Manually annotated by BRENDA team
ATCC 20336
-
-
Manually annotated by BRENDA team
L. G. Don, herbarium number LEF 920116
-
-
Manually annotated by BRENDA team
wild-type and constitutive mutant
-
-
Manually annotated by BRENDA team
strain ZP-6, haloarchaeon
-
-
Manually annotated by BRENDA team
Halobacterium sp. ZP-6
strain ZP-6, haloarchaeon
-
-
Manually annotated by BRENDA team
I3R3D1: catalytic subunit PhaAalpha, I3RA71: subunit PhaAbeta
I3R3D1 and I3R3D0
UniProt
Manually annotated by BRENDA team
I3RA72: catalytic subunit BktBalpha, I3RA71: subunit BktBbeta
I3RA72 and I3RA71
UniProt
Manually annotated by BRENDA team
Haloferax mediterranei DSM 1411
I3R3D1: catalytic subunit PhaAalpha, I3RA71: subunit PhaAbeta
I3R3D1 and I3R3D0
UniProt
Manually annotated by BRENDA team
Haloferax mediterranei DSM 1411
I3RA72: catalytic subunit BktBalpha, I3RA71: subunit BktBbeta
I3RA72 and I3RA71
UniProt
Manually annotated by BRENDA team
sunflower
-
-
Manually annotated by BRENDA team
patient with enzyme deficiency
-
-
Manually annotated by BRENDA team
; adzuki bean borer moth, female moths, gene Osat1
UniProt
Manually annotated by BRENDA team
Pyrobaculum neutrophilum DSM 2338
-
UniProt
Manually annotated by BRENDA team
2 forms: A and B
-
-
Manually annotated by BRENDA team
cicer, strain CC 1192
-
-
Manually annotated by BRENDA team
Vitis vinifera x Vitis riparia
-
-
-
Manually annotated by BRENDA team
Vitis vinifera x Vitis vinifera
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
enzyme deficiency is a rare metabolic disease of autosomal recessive inheritance characterized by intermittent ketoacidotic episodes with onset in the infant period and decline with age, overview
physiological function
Vitis vinifera x Vitis riparia, 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
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
Haloferax mediterranei DSM 1411
-
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
Pyrobaculum neutrophilum DSM 2338
-
the enzyme is involved in autotrophic carbon fixation
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 acetyl-CoA
acetoacetyl-CoA + CoA
show the reaction diagram
the thiolase is involved in the synthesis and catabolism of fatty acids
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
show the reaction diagram
I3R3D1 and I3R3D0, I3RA72 and I3RA71
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
show the reaction diagram
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
show the reaction diagram
Haloferax mediterranei DSM 1411
I3R3D1 and I3R3D0, I3RA72 and I3RA71
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
show the reaction diagram
Haloferax mediterranei DSM 1411
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
show the reaction diagram
-
cleavage of 2-methylacetoacetyl-CoA in the isoleucine catabolism
-
?
acetoacetyl-CoA + CoA
2 acetyl-CoA
show the reaction diagram
-
-
-
r
acetoacetyl-CoA + CoA
2 acetyl-CoA
show the reaction diagram
-
-
?
acetoacetyl-CoA + CoA
2 acetyl-CoA
show the reaction diagram
-
interconversion of 2 acetyl-CoA into acetoacetyl-CoA in the ketone body metabolism
-
r
acetoacetyl-CoA + CoA
2 acetyl-CoA
show the reaction diagram
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
show the reaction diagram
-
the enzyme shows preference for the thiolytic reaction direction
-
r
acetoacetyl-S-pantetheine + acetyldithio-CoA
acetyl-S-pantetheine + 3-ketobutyryldithio-CoA
show the reaction diagram
-
-
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
show the reaction diagram
-
-
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
show the reaction diagram
-
-
-
?
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
show the reaction diagram
-
-
-
?
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
show the reaction diagram
-
-
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
show the reaction diagram
-
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
show the reaction diagram
-
-
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
show the reaction diagram
-
enzyme deficiency affects isoleucine and ketone body metabolism
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
show the reaction diagram
involved in fatty acid synthesis
-
r
acetyl-CoA + acetyldithio-CoA
CoA + 3-ketobutyryldithio-CoA
show the reaction diagram
-
-
-
r
acetyl-CoA + propionyl-CoA
CoA + 3-oxopentanoyl-CoA
show the reaction diagram
I3R3D1 and I3R3D0, I3RA72 and I3RA71
-
-
?
acetyl-CoA + propionyl-CoA
CoA + 3-oxopentanoyl-CoA
show the reaction diagram
Haloferax mediterranei DSM 1411
I3R3D1 and I3R3D0, I3RA72 and I3RA71
-
-
?
CoA + acetoacetyl-10-bis-demethylpantetheine 11-pivaloate
acetyl-CoA + acetyl-10-bis-demethylpantetheine 11-pivaloate
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?, r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?, ir
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?, r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?, r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?, r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?, r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
specific for acetoacetyl-CoA, no activity with ketodecanoyl-CoA, dithiothreitol and 2-mercaptoethanol
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
thiolase II from constitutive mutant is specific for acetoacetyl-CoA
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
thiolysis is preferred, highly specific for acetoacetyl-CoA
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
enzyme has both thiolase and acetyl-CoA:acyl carrier protein transacylase activity
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
enzyme has both thiolase and 3-hydroxy-3-methylglutaryl-CoA reductase activity
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
thiolysis is strongly preferred
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
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
show the reaction diagram
-
most active in thiolysis
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
peroxisomal thiolase most probably catalyzes the first reaction in peroxisomal cholesterol and dolichol synthesis
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
liver mitochondrial isoenzyme catalyzes the first step in biosynthesis of ketone bodies
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
enzyme of fatty acid oxidation cycle
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
cytosolic thiolase I is essential for the mevalonate pathway
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
involved in generation of acetoacetyl-CoA for poly-beta-hydroxybutyrate synthesis
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
Halobacterium sp. ZP-6
-
-
-
?, r
CoA + acetoacetyl-CoA
2 acetyl-CoA
show the reaction diagram
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
show the reaction diagram
the enzyme is involved in autotrophic carbon fixation
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
show the reaction diagram
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
show the reaction diagram
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
show the reaction diagram
Pyrobaculum neutrophilum DSM 2338
the enzyme is involved in autotrophic carbon fixation
-
?
CoA + acetoacetyl-S-(11-methoxymethyl)pantetheine
acetyl-CoA + acetyl-S-(11-methoxymethyl)pantetheine
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-S-(11-t-butyldimethylsilyl)pantetheine
acetyl-CoA + acetyl-S-(11-t-butyldimethylsilyl)pantetheine
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-S-(D-pantetheine) 11-pivalate
acetyl-CoA + acetyl-S-(D-pantetheine) 11-pivalate
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-S-(L-pantetheine) 11-pivalate
acetyl-CoA + acetyl-S-(L-pantetheine) 11-pivalate
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-S-homopantetheine 12-pivalate
acetyl-CoA + acetyl-S-homopantetheine 12-pivalate
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-S-pantetheine
acetyl-CoA + acetyl-S-pantetheine
show the reaction diagram
-
-
-
?
additional information
?
-
-
the enzyme plays a more important role in the activation of ketogenesis in Squalus acanthias than in mammals and birds
-
-
-
additional information
?
-
I3R3D1 and I3R3D0, I3RA72 and I3RA71
the catalytic triad of BktBalpha is likely to be Ser-His-His
-
-
-
additional information
?
-
I3R3D1 and I3R3D0, I3RA72 and I3RA71
the catalytic triad of PhaAalpha is likely to be Ser-His-His
-
-
-
additional information
?
-
Haloferax mediterranei DSM 1411
I3R3D1 and I3R3D0, I3RA72 and I3RA71
the catalytic triad of PhaAalpha is likely to be Ser-His-His
-
-
-
additional information
?
-
Haloferax mediterranei DSM 1411
I3R3D1 and I3R3D0, I3RA72 and I3RA71
the catalytic triad of BktBalpha is likely to be Ser-His-His
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 acetyl-CoA
acetoacetyl-CoA + CoA
show the reaction diagram
B7XEI5
the thiolase is involved in the synthesis and catabolism of fatty acids
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
show the reaction diagram
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
show the reaction diagram
Haloferax mediterranei DSM 1411
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
show the reaction diagram
-
cleavage of 2-methylacetoacetyl-CoA in the isoleucine catabolism
-
?
acetoacetyl-CoA + CoA
2 acetyl-CoA
show the reaction diagram
-
interconversion of 2 acetyl-CoA into acetoacetyl-CoA in the ketone body metabolism
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
show the reaction diagram
-
-
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
show the reaction diagram
-
enzyme deficiency affects isoleucine and ketone body metabolism
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
show the reaction diagram
Q9BWD1
involved in fatty acid synthesis
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
P07256
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
P07097
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
peroxisomal thiolase most probably catalyzes the first reaction in peroxisomal cholesterol and dolichol synthesis
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
liver mitochondrial isoenzyme catalyzes the first step in biosynthesis of ketone bodies
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
enzyme of fatty acid oxidation cycle
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
Q12598
cytosolic thiolase I is essential for the mevalonate pathway
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
-
involved in generation of acetoacetyl-CoA for poly-beta-hydroxybutyrate synthesis
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
show the reaction diagram
B1YB71
the enzyme is involved in autotrophic carbon fixation
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
show the reaction diagram
A4YEH9
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
show the reaction diagram
Halobacterium sp. ZP-6
-
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
show the reaction diagram
A4YEH9
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
show the reaction diagram
Pyrobaculum neutrophilum DSM 2338
B1YB71
the enzyme is involved in autotrophic carbon fixation
-
?
additional information
?
-
-
the enzyme plays a more important role in the activation of ketogenesis in Squalus acanthias than in mammals and birds
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
enzyme contains selenomethionine
-
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+
-
maximal activity at 5-10 mM, inhibition above
Mn2+
-
can replace Mg2+, 5 mM, 90% of activity with Mg2+, inhibition above
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11-Chloro-10-oxoundecanoic acid
-
acetyl-CoA or CoA protect
11-chloro-10-oxoundecanoyl-CoA
-
acetyl-CoA or CoA protect
-
2,3-pentadienoyl-S-pantetheine 11-pivalate
-
half-life for inactivation: 1.9 min
2-Butynoyl-CoA
-
0.1 mM, 74% inactivation after 10 min
2-Oxo-5-(1-hydroxy-2,4,6-heptatriynyl)-1,3-dioxolone-4-heptanoic acid
-
natural product isolated from actinomycete culture L-660,631, IC50: 0.00001 mM,
3-butynoyl-CoA
-
0.01 mM, 95% inactivation after 10 min, acetoacetyl-CoA or 0.8 mM CoA protect
3-hydroxybutyryl-CoA
-
-
3-Pentenoyl-S-pantetheine 11-pivalate
-
half-life for inactivation: 0.26 min
3-Pentynoyl-CoA
-
0.1 mM, complete inactivation after 10 min, acetoacetyl-CoA or 0.8 mM CoA protect
3-Pentynoylpantetheine
-
1 mM, complete inactivation after 10 min
4-Bromocrotonyl-CoA
-
0.1 mM, complete inactivation after 10 min, acetoacetyl-CoA protects
4-bromocrotonylpantetheine
-
1 mM, complete inactivation after 10 min
5,5'-dithiobis(2-nitrobenzoate)
-
0.4 mM, 87% inhibition
5-chloro-4-oxopentanoyl-CoA
-
acetyl-CoA or CoA protect
7-Chloro-6-oxoheptanoic acid
-
acetyl-CoA or CoA protect
7-chloro-6-oxoheptanoyl-CoA
-
acetyl-CoA or CoA protect
9-Chloro-8-oxononanoic acid
-
acetyl-CoA or CoA protect
9-chloro-8-oxononanoyl-CoA
-
acetyl-CoA or CoA protect
acetoacetyl-CoA
-
-
acetoacetyl-CoA
-
isoenzyme A: above 0.015 mM, isoenzyme B: above 0.01 mM
acetoacetyl-CoA
-
substrate inhibition above 0.105 mM
acetoacetyl-CoA
-
substrate inhibition beyond 0.0225 mM
acetyl-CoA
-
-
Acryl-S-pantetheine 11-pivalate
-
-
ATP
-
10 mM, 41% inhibition
bromoacetyl oxoester
-
acetyl-pantetheine 11-pivalate analog
-
Bromoacetyl thioester
-
acetyl-pantetheine 11-pivalate analog
Bromoacetylamide
-
acetyl-pantetheine 11-pivalate analog
Butyryl-CoA
-
1 mM, 42% inhibition
Ca2+
-
10 and 25 mM, 25 and 50% inhibition of thiolysis
citraconic anhydride
-
-
CoA
-
higher than 0.03 mM, inhibition in cleavage direction
CoA
-
competitive vs. acetoacetyl-CoA in thiolysis
CoA
-
both directions
CoA
-
inhibition in condensation direction
CoA
-
substrate inhibition above 0.05 mM, 50% inhibition of synthesis at 0.06 mM in bacteroids
CoA
feedback inhibition
dec-3-ynoic acid
-
irreversible inhibition
Dithionitrobenzoate
-
low but significant inhibition
iodoacetamide
-
0.4 mM, 36% inhibition
iodoacetamide
-
0.005 mM, inactivation half-life: 3 min
iodoacetamide
-
125fold molar excess, rapid inactivation
iodoacetamide
-
reacts with Cys89
iodoacetamide
-
0.3 mM, 93% inhibition after 30 min
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+
-
inhibits the rate of acetoacetyl-CoA thiolysis but not the rate of synthesis of acetoacetyl-CoA
Mg2+
-
60 mM, 45% inhibition of thiolysis, 69% inhibition of synthesis
Mg2+
-
2 and 5 mM, 20 and 40% inhibition of synthesis, respectively
N-ethylmaleimide
-
0.4 mM, 53% inhibition
N-ethylmaleimide
-
-
NADH
-
inhibition of thiolysis
NADH
-
inhibition of thiolysis
p-chloromercuribenzoate
-
0.4 mM, 95% inhibition
p-chloromercuribenzoate
-
-
Sodium borohydride
-
inactivation in the presence of either acetoacetyl-CoA or acetyl-CoA
Sodium borohydride
-
-
sulfhydryl reagents
-
-
thiolactomycin
-
0.36 mM, 50% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KCl
-
maximal activity at 4.5 M
lovostatin
-
1.9fold activity increase in rats treated with lovostatin
NaCl
-
maximal activity at 4.5 M
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.023
acetoacatyl-CoA
-
recombinant cytosolic thiolase I, thiolysis
-
0.025
acetoacatyl-CoA
-
peroxisomal thiolase I, thiolysis
-
0.21
acetoacetyl-10-bis-demethylpantetheine 11-pivalate
-
-
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
-
-
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
-
-
0.024
acetoacetyl-CoA
-
-
0.025
acetoacetyl-CoA
-
-
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, 37C
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, 85C
0.18
acetoacetyl-CoA
pH 7.5, 70C
0.12
acetoacetyl-S-(11-methoxymethyl)pantetheine
-
-
0.074
acetoacetyl-S-(11-t-butyldimethylsilyl)pantetheine
-
cosubstrate CoA
0.073
acetoacetyl-S-(D-pantetheine) 11-pivalate
-
-
0.25
acetoacetyl-S-homopantetheine 12-pivalate
-
-
0.46
acetoacetyl-S-pantetheine
-
-
0.0062
acetyl-CoA
-
isoenzyme A
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
0.104
acetyl-CoA
-
-
0.27
acetyl-CoA
-
-
0.27
acetyl-CoA
-
-
0.33
acetyl-CoA
-
-
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
0.0064
CoA
-
-
0.008
CoA
-
peroxisomal thiolase, thiolysis
0.0085
CoA
-
-
0.01
CoA
-
thiolysis
0.014
CoA
-
-
0.02
CoA
-
cytosolic thiolase, thiolysis
0.022
CoA
-
-
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
0.056
CoA
-
thiolysis
0.07
CoA
-
pH 6.0, 37C
0.154
CoA
-
isoenzyme B, thiolysis
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
14
3-ketobutyryldithio-CoA
Zoogloea ramigera
-
-
266
acetoacetyl-10-bis-demethylpantetheine 11-pivaloate
Zoogloea ramigera
-
-
-
0.0767
acetoacetyl-CoA
Streptomyces collinus
-
C92S mutant thiolase
36.2
acetoacetyl-CoA
Streptomyces collinus
-
native thiolase
40.1
acetoacetyl-CoA
Streptomyces collinus
-
recombinant thiolase
80
acetoacetyl-CoA
Bacillus subtilis
-
pH 6.0, 37C
410
acetoacetyl-CoA
Zoogloea ramigera
-
-
465
acetoacetyl-CoA
Zoogloea ramigera
-
-
620
acetoacetyl-CoA
Zoogloea ramigera
-
-
1000
acetoacetyl-CoA
Metallosphaera sedula
A4YEH9
pH 7.5, 70C
353
acetoacetyl-S-(11-methoxymethyl)pantetheine
Zoogloea ramigera
-
-
434
acetoacetyl-S-(11-t-butyldimethylsilyl)pantetheine
Zoogloea ramigera
-
-
469
acetoacetyl-S-(D-pantetheine) 11-pivalate
Zoogloea ramigera
-
-
256
acetoacetyl-S-(L-pantetheine) 11-pivalate
Zoogloea ramigera
-
-
177
acetoacetyl-S-homopantetheine 12-pivalate
Zoogloea ramigera
-
-
14
acetoacetyl-S-pantetheine
Zoogloea ramigera
-
-
174
acetoacetyl-S-pantetheine
Zoogloea ramigera
-
-
2.1
acetyl-CoA
Zoogloea ramigera
-
-
29.5
CoA
Gallus gallus
-
presence of Mg2+
900
thiolytic cleavage
Gallus gallus
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5600
acetoacetyl-CoA
Metallosphaera sedula
A4YEH9
pH 7.5, 70C
187
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.028
11-Chloro-10-oxoundecanoic acid
-
-
0.0025
11-chloro-10-oxoundecanoyl-CoA
-
-
-
1.54
2,3-pentadienoyl-S-pantetheine 11-pivalate
-
-
1.25
3-Pentenoyl-S-pantetheine 11-pivalate
-
-
0.025
3-Pentynoyl-CoA
-
-
0.013
4-Bromocrotonyl-CoA
-
-
0.015
5-chloro-4-oxopentanoyl-CoA
-
-
11.4
7-Chloro-6-oxoheptanoic acid
-
-
0.002
7-chloro-6-oxoheptanoyl-CoA
-
-
0.49
9-Chloro-8-oxononanoic acid
-
-
0.0014
9-chloro-8-oxononanoyl-CoA
-
-
0.0014
acetoacetyl-CoA
-
isoenzyme A
0.0016
acetoacetyl-CoA
-
isoenzyme A
0.006
CoA
-
enzyme from bacteroids
0.011
CoA
-
-
0.05
CoA
-
-
0.067
CoA
-
-
10
dec-3-ynoic acid
-
-
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,
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.05
-
-
0.16
-
acetoacetyl-CoA synthesis
13.2
purified native enzyme
15.78
purified recombinant enzyme
58.2
-
-
100 - 130
-
peroxisomal thiolase, thiolysis
412
-
thiolysis of acetoacetyl-CoA
506
-
thiolase II
additional information
-
assay method
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6
-
assay at
7
-
condensation
7.5
-
condensation
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
8.1 - 8.4
-
isoenzyme A and B, acetoacetyl-CoA synthesis
8.3
-
cytosolic and peroxisomal thiolase I
8.4
-
cleavage of acetoacetyl-CoA, 85% of maximal activity between pH 8.0 and pH 9.0
8.5
-
505 of maximal activity at pH 7.5 and pH 9.5, no activity below pH 6.5
8.5
-
thiolysis
9.5
-
thiolysis
10.5
-
synthesis
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 9
-
69% of maximal activity at pH 9.0
6 - 9
-
approx. 80% of maximal activity at pH 6.0, approx. 40% at pH 9.0
6.5 - 9.2
-
approx. 50% of maximal activity at pH 6.5 and pH 9.2, thiolysis
7 - 9
significant decrease in activiy below pH 7.0 or above pH 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
assay at
37
-
acetoacetyl-CoA synthesis and thiolysis
37
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
isoform AACT! is highly expressed in root tips, young leaf, top stem and anther
Manually annotated by BRENDA team
-
mitochondrial acetoacetyl CoA thiolase is decreased by 80% in ulcerative colitis compared with control. Mitochondrial thiolase activity in ulcerative colitis does not correlate with clinical, endoscopic or histological indices of disease severity. Mitochondrial thiolase activity is reduced in the normal right colon mucosa of patients with left-sided ulcerative colitis
Manually annotated by BRENDA team
isoform AACT! is highly expressed in root tips, young leaf, top stem and anther
Manually annotated by BRENDA team
; low ACT1 expression
Manually annotated by BRENDA team
isoform AACT! is highly expressed in root tips, young leaf, top stem and anther
Manually annotated by BRENDA team
isoform AACT! is highly expressed in root tips, young leaf, top stem and anther
Manually annotated by BRENDA team
isoform AACT! is primarily expressed in the vascular system
Manually annotated by BRENDA team
-
acetoacetyl-CoA thiolase activity in isolated liver mitochondria is markedly increased in the ketotic dogfish compared to the recently captured fish
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
additional information
mRNA is ubiquitously expressed in 6 adult tissues including pheromone gland; Osat1 is expressed in all adult tissues
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
N-terminal sequence targets thiolase I to the peroxisome
Manually annotated by BRENDA team
-
cytosolic thiolase I
Manually annotated by BRENDA team
-
peroxisomal thiolase I
Manually annotated by BRENDA team
isozyme AACT1, its peroxisomal localisation depends on the presence of a C-terminal peroxisomal targeting sequence, PTS1, motif, Ser-Ala-Leu
Manually annotated by BRENDA team
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)
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Escherichia coli (strain K12)
Mycobacterium avium (strain 104)
Peptoclostridium difficile (strain 630)
Peptoclostridium difficile (strain 630)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80000
-
gel filtration
487703
84000
-
about, recombinant His-tagged enzyme, gel filtration
702812
147600
-
isoenzyme B, sedimentation analysis
487677
150000
-
isoenzyme A, gel filtration
487677
151000
-
gel filtration, isoenzyme A and B
487676
152000
-
isoenzyme B, gel filtration
487677
152000
-
analytical ultracentrifugation
487698
154600
-
isoenzyme A, sedimentation analysis
487677
155000
-
gel filtration
487672
155000
-
isoenzyme I, gel filtration
487677
156000
-
sucrose density gradient sedimentation
487690
160000
-
peroxisomal thiolase, gel filtration
487699
162000
-
-
487680
164000
-
gel filtration
486430
166000
-
gel filtration
487690
169000
-
sedimentation equilibrium
487669, 487671
170000
-
gel filtration
487673
180000
-
gel filtration
487687
180000
-
gel filtration
487695
185000
-
native thiolase, gel filtration
486875
187000
-
recombinant thiolase, gel filtration
486875
188000
-
gel filtration
487669
190000
-
gel filtration
487668
193000
-
native PAGE
487687
240000
-
peroxisomal thiolase I, gel filtration
487694
250000
-
cytosolic thiolase I, gel filtration
487694
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 63000, SDS-PAGE
?
-
x * 45000, SDS-PAGE
?
-
x * 86496, deduced from nucleotide sequence; x * 88712, MALDI-mass spectrometry
?
x * 41200, calculated, x * 40000, SDS-PAGE; x * 42100
?
x * 47000, recombinant enzyme, SDS-PAGE
?
x * 43445, calculated, x * 43000, SDS-PAGE
?
I3R3D1 and I3R3D0, I3RA72 and I3RA71
composed of two different types of subunits: catalytic subunit PhaAalpha, and subunit PhaABbeta
?
x * 42444, calculated from sequence
?
Haloferax mediterranei DSM 1411
-
composed of two different types of subunits: catalytic subunit PhaAalpha, and subunit PhaABbeta
-
?
Pyrobaculum neutrophilum DSM 2338
-
x * 42444, calculated from sequence
-
dimer
-
2 * 43000, CTAB-PAGE; 2 * 60000, SDS-PAGE
dimer
-
2 * 42000, recombinant His-tagged enzyme, SDS-PAGE
dimer
Halobacterium sp. ZP-6
-
2 * 43000, CTAB-PAGE; 2 * 60000, SDS-PAGE
-
hexamer
-
6 * 41000, SDS-PAGE
tetramer
-
4 * 41000, SDS-PAGE
tetramer
-
4 * 45000-47000, native thiolase, SDS-PAGE; 4 * 46000-48000, recombinant thiolase, SDS-PAGE
tetramer
-
4 * 44000, SDS-PAGE
tetramer
-
4 * 41000, SDS-PAGE
tetramer
-
4 * 38000-40000, SDS-PAGE
tetramer
-
4 * 40000, enzyme A and B, SDS-PAGE
tetramer
-
4 * 39000, SDS-PAGE
tetramer
; 4 * 40598, deduced from nucleotide sequence
tetramer
-
4 * 44000, SDS-PAGE
tetramer
-
4 * 44000, SDS-PAGE
tetramer
-
4 * 42000, SDS-PAGE
tetramer
-
4 * 44000, SDS-PAGE
tetramer
-
4 * 40495, electrospray ionization mass spectroscopy
tetramer
-
4 * 42000, peroxisomal thiolase, SDS-PAGE
tetramer
four identical subunits
hexamer
-
6 * 41000, cytosolic and peroxisomal thiolase I, SDS-PAGE
additional information
I3R3D1 and I3R3D0, I3RA72 and I3RA71
composed of two different types of subunits: catalytic subunit BktBalpha, and BktBbeta
additional information
Haloferax mediterranei DSM 1411
-
composed of two different types of subunits: catalytic subunit BktBalpha, and BktBbeta
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method at 4C. Unliganded and liganded (with CoA and with K+) structures of the human mitochondrial recombinant tetrameric thiolase
-
only successful in the presence of CoA
hangig-drop vapor diffusion at 21C, crystal structure at 2.0 A resolution
-
wild-type thiolase and acetylated thiolase complexed with CoA, C89A mutant thiolase complexed with acetyl-CoA and acetoacetyl-CoA, Q64A mutant thiolase
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0
-
1 h, complete loss of activity
487703
37
-
wild-type T2 protein is stable even after chasing for 48 h at 37C. The amount of E252del mutant protein at 48 h incubation with cycloheximide is estimated to be 50% of that observed at 0 h. E252del mutant T2 is unstable compared to the wild-type protein at 37C
676035
40
stable up to
719606
60
-
15 min, loss of 47% activity
486875
60
10 min, 50% residual activity
719606
63
-
5 min, stable
487691
70
-
10 h, 4 M KCl, 20% loss of activity
487703
85
-
10 h, 4 M KCl, 35% loss of activity
487703
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dithiothreitol stabilizes
-
glycerol stabilizes
-
unstable in dilute solution, less than 0.5 mg/ml protein
-
more than 10% sucrose, 2-mercaptoethanol or dithiothreitol are necessary to maintain activity
-
labile enzyme, partially stabilized by 1-2 mM dithiothreitol and 20% ethylene glycol
-
urea: 2.5 M, 17 h, 50% loss of activity, 5 M, 45 min, 50% loss of activity, 7 M, 1 min, 50% loss of activity
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
sensitive to borohydride reduction
-
487690
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10C, less than 0.2 mg/ml protein, 50 mM Tris, pH 7.2, 0.5 mM dithiothreitol, 8 d, 60-70% loss of activity
-
-20C, in dilute solution, less than 0.5 mg/ml protein, 24 h, complete loss of activity
-
4C, 1 mM dithiothreitol, 10% v/v glycerol, N2 atmosphere, 1 month, less than 10% loss of activity
-
0C, 0.05 M Tris-HCl, pH 7.8, 2 mM dithiothreitol, 1 mM EDTA, 20% glycerol, 6 weeks, 50% loss of activity
-
-90C, 12 months
-
25C, 1 week, 4.5 M KCl, no loss of activity
-
25C, 72 h, 200 mM KCl, 90% loss of activity
-
-20C, 20 mM Tris-HCl, pH 7.8, 0.5 mM 1 mM, EDTA, 15 d, loss of more than 50% activity
-
-20C, 20 mM Tris-HCl, pH 7.8, 0.5 mM dithiothreitol, 1 mM, EDTA, 15 d, loss of 20% activity
-
-20C, 20 mM Tris-HCl, pH 7.8, 0.5 mM dithiothreitol, 1 mM, EDTA, 20% glycerol, 60 d, loss of less than 20% activity
-
-20C, 50 mM Tris-HCl, pH 8.0, 0.5 mM dithiothreitol, glycerol
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
ammonium sulfate, calcium phosphate gel, ethanol, partial purification
-
isoenzymes A and B, ammonium sulfate, cellulose phosphate column, crystallization
-
ammonium sulfate, hydroxylapatite, phosphocellulose
-
cytosolic thiolase I
-
DEAE-Sepharose, butyl-Toyopearl, Cellulofine
-
Q-Sepharose, S-Sepharose, Superose 6, partially purifed
-
ammonium sulfate, Sephacryl S-200, superose 6, Mono Q
-
ammonium sulfate, DEAE-Sephacel, Blue Sepharose, AX 300 column
-
CM-Sephadex; single-step purification
-
DEAE-cellulose, ammonium sulfate, gel filtration, DEAE-cellulose, Matrex gel green A
-
recombinant protein
recombinant His-tagged thiolase, Ni-affinity column
-
ammonium sulfate, Sephadex G-150, DEAE-Sephadex, QAE-Sephadex; constitutive mutant, thiolase II, heat treatment, phosphocellulose
-
cytosolic enzyme
-
liver enzyme, ammonium sulfate, calcium phosphate gel, phosphocellulose column, DEAE-cellulose, hydroxylapatite, Sephadex G-200
-
poly ethylene glycol 6000, DEAE-cellulose 52, benzyl-Sepharose, hydroxylapatite
-
hydroxyapatite, Superdex, Fractogel
-
recombinant His-tagged AACT 88fold to homogeneity by nickel affinity chromatography from Escherichia coli TOP10 cells
recombinant enzyme
-
2 forms: A and B
-
peroxisomal thiolase, DEAE-cellulose, phosphocellulose column, Blue-Sepharose
-
pH 5.5, DEAE-cellulose, calcium phosphate column, celulose phosphate column
-
ammonium sulfate, Econo-Q, Superose 6, Mono Q, HA-Ultrogel, Mono Q
-
Q-Sepharose, ammonium sulfate, Sephacryl S-200, Mono Q, FPLC S-300
-
ammonium sulfate, acetone, acid treatment, CM-Sephadex, Sepharose 6B
-
ammonium sulfate, DEAE-Sepharose, hydroxyapatite, phosphocellulose, Blue Sepharose
-
protamine sulfate, DEAE-cellulose, phosphocellulose, Sephadex G-200
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene ACT1, DNA and amino acid sequence determination and analysis, expression, expression analysis, phylogenetic analysis, overexpression in transgenic Arabidopsis thaliana plants using transfection with Agrobacterium tumefaciens; gene ACT2, DNA and amino acid sequence determination and analysis, expression analysis, phylogenetic analysis, overexpression in transgenic Arabidopsis thaliana plants using transfection with Agrobacterium tumefaciens
gene mmgA, encoded in the mmg operon, DNA and amino acid sequence determination and analysis, overexpression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
expression of cytosolic and peroxisomal thiolase I in Saccharomyces cerevisiae
-
expression in Escherichia coli
expression in Escherichia coli
-
AACT, DNA and amino acid sequence determination and analysis, sequence comparison with Arabidopsis thaliana, expression of the active His-tagged enzyme in Escherichia coli TOP10 cells
recombinantly expressed in Escherichia coli
expression in Sf9 cell; gene OSAT1, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of the His-tagged enzyme in Spodoptera frugiperda Sf9 cells using a baculovirus expression system, expression in the cytosol, rather than nucleus and mitochondria
overexpressed as soluble N-terminal His10-tagged protein in Escherichia coli
expression in Escherichia coli
-
expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is highly increased in roots and leaves under cold and salinity stress
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E252del
-
25% of wild-type activity at 37C, 40% of wild-type activity at 30C. Mutant is unstable compared to the wild-type protein at 37C. KM-value for acetoacetyl-CoA is 2fold higher than wild-type value. Km-value for CoA is 1.8fold lower than wild-type value; no residual activity under any condition; relative protein amount and enzyme activity of 30% and 25% respectively, in comparison to the wild-type at 37C. 2fold Km-elevation for substrates coenzyme A and acetoacetyl-CoA compared to wild-type values. Vmax is comparable to wild-type value
N158D
-
inactive mutant protein; no residual activity under any condition
N158S
-
inactive mutant protein; no residual activity under any condition
N282H
-
inactive mutant protein; no residual activity under any condition
N353K
-
cDNAs yield neither residual T2 protein nor enzyme activity; no residual activity under any condition
Q272X
-
no residual activity under any condition
Q73P
-
cDNAs yield neither residual T2 protein nor enzyme activity; no residual activity under any condition
R208Q
-
inactive mutant protein; no residual activity under any condition
Y219H
-
inactive mutant protein; no residual activity under any condition
C92S
-
kcat decreases to 0.2% of that for the recombinant thiolase
C378G
-
mutation eliminates the ability of thiolase to catalyze proton abstraction from C2 of acetyl-CoA
C89A
-
no thiolytic activity towards acetoacetyl-CoA
Q64A
-
30% lower kcat than that of the wild-type
additional information
I3R3D1 and I3R3D0, I3RA72 and I3RA71
the deletion mutant strain expressing the enzyme with an S83A, H281Q, or H331Q mutation in BktBalpha does not accumulate polyhydroxyalkanoate at all, whereas strains expressing the enzyme with a C365A or C365S mutation in subunit BktBalpha have no significant effect on poly(3-hydroxybutyrate-co-3-hydroxyvalerate) accumulation; the introduction of the S84A, H282Q, or H332Q mutation into subunit PhaAalpha results in inactive enzyme, while the C366A or C366S mutation does not obviously affect PhaA activity
additional information
Haloferax mediterranei DSM 1411
-
the deletion mutant strain expressing the enzyme with an S83A, H281Q, or H331Q mutation in BktBalpha does not accumulate polyhydroxyalkanoate at all, whereas strains expressing the enzyme with a C365A or C365S mutation in subunit BktBalpha have no significant effect on poly(3-hydroxybutyrate-co-3-hydroxyvalerate) accumulation; the introduction of the S84A, H282Q, or H332Q mutation into subunit PhaAalpha results in inactive enzyme, while the C366A or C366S mutation does not obviously affect PhaA activity
-
M193T
-
naturally occuring mutation leading to enzyme deficiency and to the ketoacidotic episode phenotype, but with differing clinical severity, overview
additional information
-
naturally occurring mutations analyzed
additional information
-
a single-base substitution (c.1124A>G) activates a 5-base upstream cryptic splice donor site within exon 11 in the human mitochondrial acetoacetyl-CoA thiolase gene
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
I3R3D1 and I3R3D0, I3RA72 and I3RA71
the enzyme has biotechnological potential in haloarchaea for production of poly(3-hydroxybutyrate-co-3-hydroxyvalerate) with controllable 3-oxopentano content, from unrelated cheap carbon sources
synthesis
Haloferax mediterranei DSM 1411
-
the enzyme has biotechnological potential in haloarchaea for production of poly(3-hydroxybutyrate-co-3-hydroxyvalerate) with controllable 3-oxopentano content, from unrelated cheap carbon sources
-
analysis
assay based on the specific absorbance at 303 nm of the Mg2+-enolate complex of acetoacetyl-Coa