Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-methylacetoacetyl-CoA thiolase
-
-
-
-
3-ketoacyl-CoA (T1)-like thiolase
-
-
3-ketoacyl-coenzyme A thiolase
acetoacetyl-CoA acetyltransferase
acetoacetyl-CoA C-acetyltransferase
-
acetoacetyl-CoA thiolase T2
-
-
acetyl coenzyme A thiolase
-
-
-
-
acetyl-CoA acetyltransferase
acetyl-CoA C-acetyltransferase
acetyl-CoA:N-acetyltransferase
-
-
-
-
acetyltransferase, acetyl coenzyme A
-
-
-
-
beta-acetoacetyl coenzyme A thiolase
-
-
-
-
beta-ketoacyl-CoA thiolase
-
-
cytosolic acetoacetyl-CoA thiolase
-
-
cytosolic acetoacetyl-CoA thiolase 1
-
cytosolic acetoacetyl-CoA thiolase 2
-
3-ketoacyl-CoA thiolase

-
3-ketoacyl-CoA thiolase
-
3-ketoacyl-CoA thiolase
-
-
3-ketoacyl-coenzyme A thiolase

-
3-ketoacyl-coenzyme A thiolase
-
-
A1887

-
AACT

-
AACT1

-
ACAT

-
ACAT1

-
isoform
ACAT2

-
ACCT

-
-
acetoacetyl CoA thiolase

-
-
-
-
acetoacetyl CoA thiolase
-
acetoacetyl CoA thiolase
-
-
acetoacetyl-CoA acetyltransferase

-
-
acetoacetyl-CoA acetyltransferase
-
-
-
acetoacetyl-CoA thiolase

-
-
-
-
acetoacetyl-CoA thiolase
-
acetoacetyl-CoA thiolase
-
-
acetoacetyl-CoA thiolase
-
acetoacetyl-CoA thiolase
-
acetoacetyl-CoA thiolase
-
acetoacetyl-CoA thiolase
-
-
acetoacetyl-CoA thiolase
-
-
acetoacetyl-CoA thiolase
-
-
-
acetoacetyl-CoA thiolase
-
-
acetoacetyl-CoA thiolase
-
acetoacetyl-CoA thiolase
-
-
acetoacetyl-CoA thiolase
-
-
acetoacetyl-CoA thiolase
-
-
-
acetoacetyl-CoA thiolase
-
-
acetoacetyl-CoA thiolase
-
-
acetoacetyl-CoA thiolase
Vitis vinifera x Vitis vinifera
-
-
acetyl-CoA acetyltransferase

-
-
-
-
acetyl-CoA acetyltransferase
-
acetyl-CoA C-acetyltransferase

-
-
acetyl-CoA C-acetyltransferase
-
-
-
ACTRANS

-
-
ACTRANS
Vitis vinifera x Vitis vinifera
-
-
AFUB_000550

-
beta-ketothiolase

-
ERG10

-
-
Erg10A

-
HFX_1022

locus name, subunit PhaAbeta
HFX_1022
locus name, subunit PhaAbeta
-
HFX_1023

locus name, subunit PhaAalpha
HFX_1023
locus name, subunit PhaAalpha
-
HFX_6003

locus name, subunit BktBbeta
HFX_6003
locus name, subunit BktBbeta
-
HFX_6004

locus name, subunit BktBalpha
HFX_6004
locus name, subunit BktBalpha
-
KACT

-
Msed_0656

locus name
phaA

-
thiolase II

-
-
-
-
Tneu_0249

locus name
type II thiolase

-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 acetyl-CoA = CoA + acetoacetyl-CoA
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

mechanism
-
2 acetyl-CoA = CoA + acetoacetyl-CoA
mechanism
-
2 acetyl-CoA = CoA + acetoacetyl-CoA
mechanism
-
2 acetyl-CoA = CoA + acetoacetyl-CoA
ping-pong mechanism
-
2 acetyl-CoA = CoA + acetoacetyl-CoA
ping-pong mechanism
-
2 acetyl-CoA = CoA + acetoacetyl-CoA
bi bi 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
proposed two-step ping pong mechanism
-
2 acetyl-CoA = CoA + acetoacetyl-CoA
Claisen condensation, mechanism
-
2 acetyl-CoA = CoA + acetoacetyl-CoA
Claisen condensation, mechanism
2 acetyl-CoA = CoA + acetoacetyl-CoA
Claisen condensation, mechanism
2 acetyl-CoA = CoA + acetoacetyl-CoA
overall reaction
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 acetyl-CoA
acetoacetyl-CoA + CoA
2 acetyl-CoA
CoA + acetoacetyl-CoA
2-methylacetoacetyl-CoA + CoA
acetyl-CoA + propionyl-CoA
acetoacetyl-CoA + CoA
2 acetyl-CoA
acetoacetyl-S-pantetheine + acetyldithio-CoA
acetyl-S-pantetheine + 3-ketobutyryldithio-CoA
-
-
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
acetyl-CoA + acetyldithio-CoA
CoA + 3-ketobutyryldithio-CoA
-
-
-
r
acetyl-CoA + propionyl-CoA
CoA + 3-oxopentanoyl-CoA
CoA + acetoacetyl-10-bis-demethylpantetheine 11-pivaloate
acetyl-CoA + acetyl-10-bis-demethylpantetheine 11-pivaloate
-
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-S-(11-methoxymethyl)pantetheine
acetyl-CoA + acetyl-S-(11-methoxymethyl)pantetheine
-
-
-
-
?
CoA + acetoacetyl-S-(11-t-butyldimethylsilyl)pantetheine
acetyl-CoA + acetyl-S-(11-t-butyldimethylsilyl)pantetheine
-
-
-
?
CoA + acetoacetyl-S-(D-pantetheine) 11-pivalate
acetyl-CoA + acetyl-S-(D-pantetheine) 11-pivalate
-
-
-
?
CoA + acetoacetyl-S-(L-pantetheine) 11-pivalate
acetyl-CoA + acetyl-S-(L-pantetheine) 11-pivalate
-
-
-
?
CoA + acetoacetyl-S-homopantetheine 12-pivalate
acetyl-CoA + acetyl-S-homopantetheine 12-pivalate
-
-
-
?
CoA + acetoacetyl-S-pantetheine
acetyl-CoA + acetyl-S-pantetheine
-
-
-
?
additional information
?
-
2 acetyl-CoA

acetoacetyl-CoA + CoA
-
-
-
?
2 acetyl-CoA
acetoacetyl-CoA + CoA
the thiolase is involved in the synthesis and catabolism of fatty acids
-
-
?
2 acetyl-CoA

CoA + acetoacetyl-CoA
-
-
-
r
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
r
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
r
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
r
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
r
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
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 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
ir
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
r
2-methylacetoacetyl-CoA + CoA

acetyl-CoA + propionyl-CoA
-
-
-
-
?
2-methylacetoacetyl-CoA + CoA
acetyl-CoA + propionyl-CoA
-
cleavage of 2-methylacetoacetyl-CoA in the isoleucine catabolism
-
-
?
acetoacetyl-CoA + CoA

2 acetyl-CoA
-
the enzyme shows preference for the thiolytic reaction direction
-
-
r
acetoacetyl-CoA + CoA
2 acetyl-CoA
-
-
-
?
acetoacetyl-CoA + CoA
2 acetyl-CoA
coupled reaction assay in which the product of the thiolase reaction, acetyl-CoA, becomes the substrate for citrate synthase
-
-
r
acetoacetyl-CoA + CoA
2 acetyl-CoA
-
-
-
-
r
acetoacetyl-CoA + CoA
2 acetyl-CoA
-
interconversion of 2 acetyl-CoA into acetoacetyl-CoA in the ketone body metabolism
-
-
r
acetyl-CoA + acetyl-CoA

CoA + acetoacetyl-CoA
-
-
-
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
?
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
-
enzyme deficiency affects isoleucine and ketone body metabolism
-
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
involved in fatty acid synthesis
-
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
r
acetyl-CoA + propionyl-CoA

CoA + 3-oxopentanoyl-CoA
-
-
-
?
acetyl-CoA + propionyl-CoA
CoA + 3-oxopentanoyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA

2 acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
CoA binding mode, overview
-
-
r
CoA + acetoacetyl-CoA
2 acetyl-CoA
CoA substrate binding structure, overview
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
CoA substrate binding structure, overview
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
2 acetyl-CoA
CoA binding mode, overview
-
-
r
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
the enzyme is involved in autotrophic carbon fixation
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
the enzyme is involved in autotrophic carbon fixation
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
-
-
-
r
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
the enzyme of the biosynthetic pathway for polyhydroxyalkanoates
-
-
r
CoA + acetoacetyl-CoA

acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
rate of synthesis is 0.31 and 0.08 the rate of thiolysis for isoenzyme A and B, respectively
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
specific for acetoacetyl-CoA, no activity with ketodecanoyl-CoA, dithiothreitol and 2-mercaptoethanol
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
cytosolic thiolase I is essential for the mevalonate pathway
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?, r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?, r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?, r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
enzyme of fatty acid oxidation cycle
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
enzyme has both thiolase and 3-hydroxy-3-methylglutaryl-CoA reductase activity
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?, r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
thiolase II from constitutive mutant is specific for acetoacetyl-CoA
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?, r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?, r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?, ir
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
thiolysis is strongly preferred
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
peroxisomal thiolase most probably catalyzes the first reaction in peroxisomal cholesterol and dolichol synthesis
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
liver mitochondrial isoenzyme catalyzes the first step in biosynthesis of ketone bodies
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
enzyme has both thiolase and acetyl-CoA:acyl carrier protein transacylase activity
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
thiolysis is preferred, highly specific for acetoacetyl-CoA
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
?, r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
most active in thiolysis
-
r
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
involved in generation of acetoacetyl-CoA for poly-beta-hydroxybutyrate synthesis
-
?
additional information

?
-
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
?
-
the enzyme shows degradative thiolase activity by converting 3-ketoacyl-CoA to acyl-CoA
-
-
?
additional information
?
-
the bound CoA substrate is located within the deep cleft formed by subdomains I, II, and III. The thiol group of CoA is located in the vicinity of the catalytic site for the degradation reaction, whereas,the adenosine nucleotide moiety is exposed on the surface. Unlike enzyme ReH16_A1887, that shows substantial structural changeupon the binding of CoA, the CoA-bound form of enzyme ReH16_B0759 exhibits quite similar structure to the apoform of the protein except for residual movement of Arg220. Moreover, the CoA binding mode of enzyme ReH16_B0759 is quite different from that of enzyme ReH16_A1887
-
-
?
additional information
?
-
the enzyme shows degradative thiolase activity by converting 3-ketoacyl-CoA to acyl-CoA
-
-
?
additional information
?
-
the enzyme shows degradative thiolase activity by converting 3-oxoacyl-CoA to acyl-CoA
-
-
?
additional information
?
-
the catalytic triad of BktBalpha is likely to be Ser-His-His
-
-
?
additional information
?
-
the catalytic triad of BktBalpha is likely to be Ser-His-His
-
-
?
additional information
?
-
-
the catalytic triad of BktBalpha is likely to be Ser-His-His
-
-
?
additional information
?
-
the catalytic triad of PhaAalpha is likely to be Ser-His-His
-
-
?
additional information
?
-
the catalytic triad of PhaAalpha is likely to be Ser-His-His
-
-
?
additional information
?
-
-
the catalytic triad of PhaAalpha is likely to be Ser-His-His
-
-
?
additional information
?
-
the catalytic triad of PhaAalpha is likely to be Ser-His-His
-
-
?
additional information
?
-
the catalytic triad of PhaAalpha is likely to be Ser-His-His
-
-
?
additional information
?
-
the catalytic triad of BktBalpha is likely to be Ser-His-His
-
-
?
additional information
?
-
the catalytic triad of BktBalpha is likely to be Ser-His-His
-
-
?
additional information
?
-
-
no activity is observed with acetyl-CoA
-
-
?
additional information
?
-
-
the enzyme plays a more important role in the activation of ketogenesis in Squalus acanthias than in mammals and birds
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 acetyl-CoA
acetoacetyl-CoA + CoA
the thiolase is involved in the synthesis and catabolism of fatty acids
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
2-methylacetoacetyl-CoA + CoA
acetyl-CoA + propionyl-CoA
-
cleavage of 2-methylacetoacetyl-CoA in the isoleucine catabolism
-
-
?
acetoacetyl-CoA + CoA
2 acetyl-CoA
-
interconversion of 2 acetyl-CoA into acetoacetyl-CoA in the ketone body metabolism
-
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
CoA + acetoacetyl-CoA
2 acetyl-CoA
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
additional information
?
-
2 acetyl-CoA

CoA + acetoacetyl-CoA
-
-
-
r
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
r
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
r
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
?
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
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
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
ir
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
?
2 acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
-
?
acetyl-CoA + acetyl-CoA

CoA + acetoacetyl-CoA
-
-
-
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
-
enzyme deficiency affects isoleucine and ketone body metabolism
-
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
involved in fatty acid synthesis
-
-
r
acetyl-CoA + acetyl-CoA
CoA + acetoacetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA

2 acetyl-CoA
-
-
-
r
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
2 acetyl-CoA
-
-
-
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
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
cytosolic thiolase I is essential for the mevalonate pathway
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
enzyme of fatty acid oxidation cycle
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
peroxisomal thiolase most probably catalyzes the first reaction in peroxisomal cholesterol and dolichol synthesis
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
liver mitochondrial isoenzyme catalyzes the first step in biosynthesis of ketone bodies
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
-
?
CoA + acetoacetyl-CoA
acetyl-CoA + acetyl-CoA
-
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 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
?
-
-
no activity is observed with acetyl-CoA
-
-
?
additional information
?
-
-
the enzyme plays a more important role in the activation of ketogenesis in Squalus acanthias than in mammals and birds
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
11-Chloro-10-oxoundecanoic acid
-
acetyl-CoA or CoA protect
11-chloro-10-oxoundecanoyl-CoA
-
acetyl-CoA or CoA protect
2,3-pentadienoyl-S-pantetheine 11-pivalate
-
half-life for inactivation: 1.9 min
2-butynoyl-CoA
-
0.1 mM, 74% inactivation after 10 min
2-Oxo-5-(1-hydroxy-2,4,6-heptatriynyl)-1,3-dioxolone-4-heptanoic acid
-
natural product isolated from actinomycete culture L-660,631, IC50: 0.00001 mM,
3-butynoyl-CoA
-
0.01 mM, 95% inactivation after 10 min, acetoacetyl-CoA or 0.8 mM CoA protect
3-Pentenoyl-S-pantetheine 11-pivalate
-
half-life for inactivation: 0.26 min
3-pentynoyl-CoA
-
0.1 mM, complete inactivation after 10 min, acetoacetyl-CoA or 0.8 mM CoA protect
3-Pentynoylpantetheine
-
1 mM, complete inactivation after 10 min
4-bromocrotonyl-CoA
-
0.1 mM, complete inactivation after 10 min, acetoacetyl-CoA protects
4-bromocrotonylpantetheine
-
1 mM, complete inactivation after 10 min
5,5'-dithiobis(2-nitrobenzoate)
-
0.4 mM, 87% inhibition
5-chloro-4-oxopentanoyl-CoA
-
acetyl-CoA or CoA protect
7-Chloro-6-oxoheptanoic acid
-
acetyl-CoA or CoA protect
7-chloro-6-oxoheptanoyl-CoA
-
acetyl-CoA or CoA protect
9-Chloro-8-oxononanoic acid
-
acetyl-CoA or CoA protect
9-chloro-8-oxononanoyl-CoA
-
acetyl-CoA or CoA protect
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
Acryl-S-pantetheine 11-pivalate
-
-
ATP
-
10 mM, 41% inhibition
Bromoacetyl thioester
-
acetyl-pantetheine 11-pivalate analog
Bromoacetylamide
-
acetyl-pantetheine 11-pivalate analog
butyryl-CoA
-
1 mM, 42% inhibition
Ca2+
-
10 and 25 mM, 25 and 50% inhibition of thiolysis
dec-3-ynoic acid
-
irreversible inhibition
Dithionitrobenzoate
-
low but significant inhibition
thiolactomycin
-
0.36 mM, 50% inhibition
acetoacetyl-CoA

-
-
acetoacetyl-CoA
-
substrate inhibition above 0.105 mM
acetoacetyl-CoA
-
substrate inhibition beyond 0.0225 mM
acetoacetyl-CoA
-
isoenzyme A: above 0.015 mM, isoenzyme B: above 0.01 mM
CoA

-
both directions
CoA
-
inhibition in condensation direction
CoA
-
higher than 0.03 mM, inhibition in cleavage direction
CoA
-
competitive vs. acetoacetyl-CoA in thiolysis
CoA
-
substrate inhibition above 0.05 mM, 50% inhibition of synthesis at 0.06 mM in bacteroids
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
-
0.3 mM, 93% inhibition after 30 min
iodoacetamide
-
2 mM, complete inactivation after approx. 60 min, 0.3 mM acetoacetyl-CoA or 1.6 mM acetyl-CoA protect
iodoacetamide
-
0.005 mM, inactivation half-life: 3 min
iodoacetamide
-
0.4 mM, 36% inhibition
iodoacetamide
-
125fold molar excess, rapid inactivation
iodoacetamide
-
reacts with Cys89
Mg2+

inhibitory at concentrations higher than 5 mM
Mg2+
-
60 mM, 45% inhibition of thiolysis, 69% inhibition of synthesis
Mg2+
-
inhibits the rate of acetoacetyl-CoA thiolysis but not the rate of synthesis of acetoacetyl-CoA
Mg2+
-
2 and 5 mM, 20 and 40% inhibition of synthesis, respectively
N-ethylmaleimide

-
-
N-ethylmaleimide
-
0.4 mM, 53% inhibition
NADH

-
inhibition of thiolysis
NADH
-
inhibition of thiolysis
p-chloromercuribenzoate

-
-
p-chloromercuribenzoate
-
0.4 mM, 95% inhibition
Sodium borohydride

-
-
Sodium borohydride
-
inactivation in the presence of either acetoacetyl-CoA or acetyl-CoA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.21
acetoacetyl-10-bis-demethylpantetheine 11-pivalate
-
-
0.0038 - 0.18
acetoacetyl-CoA
0.12
acetoacetyl-S-(11-methoxymethyl)pantetheine
-
-
0.074
acetoacetyl-S-(11-t-butyldimethylsilyl)pantetheine
-
cosubstrate CoA
0.073
acetoacetyl-S-(D-pantetheine) 11-pivalate
-
-
0.25
acetoacetyl-S-homopantetheine 12-pivalate
-
-
0.46
acetoacetyl-S-pantetheine
-
-
additional information
additional information
Michaelis-Menten kinetics
-
0.0038
acetoacetyl-CoA

-
native thiolase
0.004
acetoacetyl-CoA
-
isoenzyme B, thiolysis
0.005
acetoacetyl-CoA
-
wild-type enzyme
0.005
acetoacetyl-CoA
-
E252del mutant 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
-
wild-type enzyme
0.01
acetoacetyl-CoA
-
isoenzyme A, thiolysis
0.01
acetoacetyl-CoA
-
mutant enzyme E252del
0.011
acetoacetyl-CoA
-
-
0.016
acetoacetyl-CoA
-
cytosolic thiolase, thiolysis
0.0176
acetoacetyl-CoA
pH 7.8, 30ưC
0.019
acetoacetyl-CoA
-
-
0.02067
acetoacetyl-CoA
at pH 8.9 and 25ưC
0.023
acetoacetyl-CoA
-
recombinant cytosolic thiolase I, thiolysis
0.024
acetoacetyl-CoA
-
-
0.025
acetoacetyl-CoA
-
-
0.025
acetoacetyl-CoA
-
peroxisomal thiolase I, thiolysis
0.027
acetoacetyl-CoA
-
pH 8.0, 65ưC
0.032
acetoacetyl-CoA
-
-
0.032
acetoacetyl-CoA
-
isoenzyme B, thiolysis
0.035
acetoacetyl-CoA
-
peroxisomal thiolase, synthesis
0.0385
acetoacetyl-CoA
-
-
0.042
acetoacetyl-CoA
-
cytosolic thiolase I, thiolysis
0.042
acetoacetyl-CoA
-
thiolysis
0.043
acetoacetyl-CoA
pH 8.1, 30ưC
0.05
acetoacetyl-CoA
-
pH 6.0, 37ưC
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, 85ưC
0.158
acetoacetyl-CoA
pH 8.3, 30ưC, recombinant enzyme
0.18
acetoacetyl-CoA
pH 7.5, 70ưC
0.0062
acetyl-CoA

-
isoenzyme A
0.0258
acetyl-CoA
at pH 8.9 and 25ưC
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
0.091
acetyl-CoA
-
isoenzyme B, synthesis
0.1386
acetyl-CoA
pH 7.8, 30ưC
0.232
acetyl-CoA
pH 8.1, 30ưC
0.25
acetyl-CoA
-
pH 8.0, 65ưC
0.38
acetyl-CoA
-
enzyme from bacteroids
0.47
acetyl-CoA
-
synthesis
0.6
acetyl-CoA
-
synthesis
0.69
acetyl-CoA
-
recombinant cytosolic thiolase I, thiolysis
0.74
acetyl-CoA
-
recombinant peroxisomal thiolase I, thiolysis
0.77
acetyl-CoA
-
cytosolic thiolase I, thiolysis
1.05
acetyl-CoA
-
peroxisomal thiolase I, thiolysis
1.06
acetyl-CoA
-
synthesis
0.0048
CoA

-
-
0.008
CoA
-
peroxisomal thiolase, thiolysis
0.008
CoA
pH 7.8, 30ưC
0.011
CoA
-
pH 8.0, 65ưC
0.02
CoA
-
cytosolic thiolase, thiolysis
0.025
CoA
-
isoenzyme A, thiolysis
0.026
CoA
pH 8.1, 30ưC
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
-
mutant enzyme E252del
0.05
CoA
-
E252del mutant enzyme
0.07
CoA
-
pH 6.0, 37ưC
0.154
CoA
-
isoenzyme B, thiolysis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
brenda
-
brenda
-
-
brenda
-
brenda
male flower and leaf, second highest expression level
brenda
-
-
brenda
highest expression level
brenda
-
-
brenda
-
brenda
higher expression levels in the liver, kidney, adrenal gland and ovary
brenda
-
brenda
-
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
highest expression in roots and petals
brenda
-
brenda
-
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
-
brenda
etiolated
brenda
-
brenda
-
brenda
isoform AACT! is primarily expressed in the vascular system
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
brenda
-
brenda
-
brenda
low ACT1 expression
brenda
-
brenda
isoform AACT! is highly expressed in root tips, young leaf, top stem and anther
brenda
-
brenda
no significant difference in expression among roots, stems and leaves
brenda
and male flower, second highest expression level
brenda
-
-
brenda
-
-
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
-
brenda
-
-
brenda
-
acetoacetyl-CoA thiolase activity in isolated liver mitochondria is markedly increased in the ketotic dogfish compared to the recently captured fish
brenda
-
brenda
low ACT1 expression
brenda
isoform AACT! is highly expressed in root tips, young leaf, top stem and anther
brenda
highest expression in roots and petals
brenda
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
-
brenda
-
-
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
expression is found in all tissues
brenda
additional information
-
expression is found in all tissues
brenda
additional information
Osat1 is expressed in all adult 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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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-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
-
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
-
physiological function

Vitis vinifera x Vitis vinifera
-
involved in terpenoid metabolism
physiological function
-
involved in terpenoid metabolism
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
-
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.