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ADP + phosphate + acetyl-CoA
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
ADP + phosphate + butanoyl-CoA
ATP + butanoate + CoA
ADP + phosphate + butyryl-CoA
ATP + butyrate + CoA
ADP + phosphate + indoleacetyl-CoA
ATP + indoleacetate + CoA
-
Substrates: r, isoenzyme ACS II is active, ACS I not
Products: -
?
ADP + phosphate + isobutyryl-CoA
ATP + isobutyrate + CoA
ADP + phosphate + isovaleryl-CoA
ATP + isovalerate + CoA
Substrates: less than 1% activity compared to acetyl-CoA
Products: -
r
ADP + phosphate + phenylacetyl-CoA
ATP + phenylacetate + CoA
ADP + phosphate + propanoyl-CoA
ATP + propanoate + CoA
Substrates: 45% of the activity relative to acetyl-CoA
Products: -
?
ADP + phosphate + propionyl-CoA
ATP + propionate + CoA
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
ATP + 2-methylbutyrate + CoA
ADP + phosphate + 2-methylbutyryl-CoA
ATP + 3-methylthiopropionate + CoA
ADP + phosphate + 3-methylthiopropionyl-CoA
Substrates: -
Products: -
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
ATP + butyrate + CoA
ADP + phosphate + butyryl-CoA
ATP + heptanoate + CoA
ADP + phosphate + heptanoyl-CoA
Substrates: less than 4% activity compared to acetate
Products: -
r
ATP + hexanoate + CoA
ADP + phosphate + hexanoyl-CoA
Substrates: less than 4% activity compared to acetate
Products: -
r
ATP + imidazole-4-acetate + CoA
ADP + phosphate + imidazol-4-ylacetyl-CoA
-
Substrates: 17% activity compared to acetate
Products: -
?
ATP + isobutyrate + CoA
ADP + phosphate + isobutyryl-CoA
ATP + isopentanioate + CoA
ADP + phosphate + isovaleryl-CoA
-
Substrates: 34% of the activity relative to acetate
Products: -
?
ATP + isovalerate + CoA
ADP + phosphate + isovaleryl-CoA
ATP + n-butyrate + CoA
ADP + phosphate + n-butyryl-CoA
ATP + octanoate + CoA
ADP + phosphate + octanoyl-CoA
Substrates: less than 4% activity compared to acetate
Products: -
r
ATP + pentanoate + CoA
ADP + phosphate + valeryl-CoA
-
Substrates: 36% of the activity relative to acetate
Products: -
?
ATP + phenylacetate + CoA
ADP + phosphate + phenylacetyl-CoA
ATP + propionate + CoA
ADP + phosphate + propionyl-CoA
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
Substrates: less than 4% activity compared to acetate
Products: -
r
ATP + thioglycolate + CoA
ADP + phosphate + thioglycolyl-CoA
ATP + valerate + CoA
ADP + phosphate + valeryl-CoA
Substrates: less than 4% activity compared to acetate
Products: -
r
CDP + phosphate + acetyl-CoA
CTP + acetate + CoA
Substrates: 7% activity compared to ADP
Products: -
r
CTP + acetate + CoA
CDP + phosphate + acetyl-CoA
Substrates: 4.1% activity compared to ATP
Products: -
r
dADP + phosphate + acetyl-CoA
dATP + acetate + CoA
-
Substrates: 40% of the activity relative to ADP
Products: -
?
GDP + phosphate + acetyl-CoA
GTP + acetate + CoA
GTP + acetate + CoA
GDP + phosphate + acetyl-CoA
IDP + phosphate + acetyl-CoA
ITP + acetate + CoA
ITP + acetate + CoA
IDP + phosphate + acetyl-CoA
Substrates: 15% activity compared to ATP
Products: -
r
UDP + phosphate + acetyl-CoA
UTP + acetate + CoA
Substrates: 2.8% activity compared to ADP
Products: -
r
UTP + acetate + CoA
UDP + phosphate + acetyl-CoA
Substrates: 1.6% activity compared to ATP
Products: -
r
additional information
?
-
ADP + phosphate + acetyl-CoA
?
-
Substrates: enzyme catalyzes acetate formation and ATP generation during fermentation of pyruvate to acetate
Products: -
?
ADP + phosphate + acetyl-CoA
?
-
Substrates: energy-conserving pyruvate-to-acetate pathway
Products: -
?
ADP + phosphate + acetyl-CoA
?
-
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA
?
-
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA
?
-
Substrates: enzyme catalyzes acetate formation and ATP generation during fermentation of pyruvate to acetate
Products: -
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
-
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
-
Substrates: Archaeoglobus fulgidus strain 7324 converts starch to acetate via a modified Embden-Meyerhof pathway and acetyl-CoA synthetase (ADP-forming)
Products: -
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
-
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
-
Substrates: -
Products: -
r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
-
Substrates: -
Products: -
r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
-
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
Substrates: -
Products: -
r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
Substrates: -
Products: -
r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
Substrates: 100% activity
Products: -
r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
Substrates: the specific activity in the acetate-forming direction is approximately half that observed in the acetyl-CoA-forming direction
Products: -
r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
-
Substrates: reverse reaction not detected
Products: -
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
Substrates: no activity with butanoyl-CoA, propanoyl-CoA and pentanoyl-CoA
Products: -
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
Substrates: enzyme catalyzes acetate formation and ATP generation during fermentation of pyruvate to acetate
Products: -
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
Substrates: enzyme catalyzes acetate formation and ATP generation during fermentation of pyruvate to acetate
Products: -
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
-
Substrates: -
Products: -
r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
-
Substrates: downregulation of the enzyme is observed during periods of acetate consumption
Products: -
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
-
Substrates: -
Products: -
r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
-
Substrates: -
Products: -
ir, r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
-
Substrates: -
Products: -
ir, r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
-
Substrates: -
Products: -
r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
Q9Y8L0, Q9Y8L1
Substrates: -
Products: -
r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
-
Substrates: r
Products: -
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
-
Substrates: isoenzymes ACS I and ACS II
Products: -
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
Q9Y8L0, Q9Y8L1
Substrates: major energy-conserving reaction during pyruvate and sugar conversion to acetate, catalyzing acetate formation and ATP synthesis
Products: -
r
ADP + phosphate + butanoyl-CoA
ATP + butanoate + CoA
Substrates: 23% of the activity relative to acetyl-CoA
Products: -
?
ADP + phosphate + butanoyl-CoA
ATP + butanoate + CoA
Substrates: less efficiently than acetyl-CoA
Products: -
?
ADP + phosphate + butanoyl-CoA
ATP + butanoate + CoA
Substrates: less efficiently than acetyl-CoA
Products: -
?
ADP + phosphate + butyryl-CoA
ATP + butyrate + CoA
-
Substrates: no activity with n-butyryl-CoA
Products: -
?
ADP + phosphate + butyryl-CoA
ATP + butyrate + CoA
-
Substrates: 92% of the activity relative to acetyl-CoA
Products: -
?
ADP + phosphate + isobutyryl-CoA
ATP + isobutyrate + CoA
Substrates: less than 1% activity compared to acetyl-CoA
Products: -
r
ADP + phosphate + isobutyryl-CoA
ATP + isobutyrate + CoA
-
Substrates: -
Products: -
r
ADP + phosphate + phenylacetyl-CoA
ATP + phenylacetate + CoA
-
Substrates: -
Products: -
r
ADP + phosphate + phenylacetyl-CoA
ATP + phenylacetate + CoA
-
Substrates: r, isoenzyme ACS II is active, ACS I not
Products: -
?
ADP + phosphate + propionyl-CoA
ATP + propionate + CoA
Substrates: 16% activity compared to acetyl-CoA
Products: -
r
ADP + phosphate + propionyl-CoA
ATP + propionate + CoA
-
Substrates: 39% of the activity relative to acetyl-CoA
Products: -
?
ADP + phosphate + propionyl-CoA
ATP + propionate + CoA
-
Substrates: r
Products: -
?
ADP + phosphate + propionyl-CoA
ATP + propionate + CoA
-
Substrates: 110% of the activity relative to acetyl-CoA
Products: -
?
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
-
Substrates: 30% of the activity relative to acetyl-CoA
Products: -
?
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
-
Substrates: no activity with isoenzymes ACS I and ACS II
Products: -
?
ATP + 2-methylbutyrate + CoA
ADP + phosphate + 2-methylbutyryl-CoA
-
Substrates: 75% activity compared to acetate
Products: -
?
ATP + 2-methylbutyrate + CoA
ADP + phosphate + 2-methylbutyryl-CoA
Substrates: -
Products: -
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
-
Substrates: -
Products: -
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
-
Substrates: 100% activity
Products: -
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
-
Substrates: -
Products: -
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
Substrates: -
Products: -
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
Substrates: -
Products: -
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
Substrates: 100% activity
Products: -
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
Substrates: preferred direction of reaction
Products: -
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
-
Substrates: -
Products: -
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
-
Substrates: -
Products: -
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
-
Substrates: -
Products: -
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
-
Substrates: the enzyme is required for growth on ethanol. ACS activity is induced upon growth on ethanol, 2,3-butanediol, malonate and acetate
Products: -
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
-
Substrates: -
Products: -
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
-
Substrates: -
Products: -
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
Substrates: -
Products: -
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
Substrates: the enzyme catalyzes the formation of acetate from acetyl-CoA and concomitant ATP synthesis by the mechanism of substrate level phosphorylation
Products: -
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
Substrates: the phosphorolysis is catalyzed by the alpha-subunit alone, independent of the beta-subunit. Both the His257alpha and Glu218alpha are crucial for phosphorolysis. In case of Glu218alpha the charge is essential for activity and also the length of the side chain is important
Products: -
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
-
Substrates: -
Products: -
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
Substrates: -
Products: -
?
ATP + butyrate + CoA
ADP + phosphate + butyryl-CoA
-
Substrates: 98% activity compared to acetate
Products: -
?
ATP + butyrate + CoA
ADP + phosphate + butyryl-CoA
Substrates: 5.6% activity compared to acetate
Products: -
r
ATP + butyrate + CoA
ADP + phosphate + butyryl-CoA
-
Substrates: at 98% of the activity with acetate
Products: -
?
ATP + isobutyrate + CoA
ADP + phosphate + isobutyryl-CoA
-
Substrates: 46% activity compared to acetate
Products: -
?
ATP + isobutyrate + CoA
ADP + phosphate + isobutyryl-CoA
-
Substrates: 46% activity compared to acetate
Products: -
?
ATP + isobutyrate + CoA
ADP + phosphate + isobutyryl-CoA
Substrates: less than 4% activity compared to acetate
Products: -
r
ATP + isobutyrate + CoA
ADP + phosphate + isobutyryl-CoA
-
Substrates: at 38% of the activity with acetate
Products: -
?
ATP + isobutyrate + CoA
ADP + phosphate + isobutyryl-CoA
-
Substrates: r
Products: -
?
ATP + isobutyrate + CoA
ADP + phosphate + isobutyryl-CoA
-
Substrates: isoenzymes ACS I and ACS II
Products: -
?
ATP + isobutyrate + CoA
ADP + phosphate + isobutyryl-CoA
-
Substrates: 79% of the activity relative to acetate
Products: -
?
ATP + isobutyrate + CoA
ADP + phosphate + isobutyryl-CoA
Substrates: -
Products: -
?
ATP + isovalerate + CoA
ADP + phosphate + isovaleryl-CoA
-
Substrates: 65% activity compared to acetate
Products: -
?
ATP + isovalerate + CoA
ADP + phosphate + isovaleryl-CoA
Substrates: less than 4% activity compared to acetate
Products: -
r
ATP + isovalerate + CoA
ADP + phosphate + isovaleryl-CoA
-
Substrates: at 25% of the activity with acetate
Products: -
?
ATP + isovalerate + CoA
ADP + phosphate + isovaleryl-CoA
Substrates: -
Products: -
?
ATP + n-butyrate + CoA
ADP + phosphate + n-butyryl-CoA
-
Substrates: s.o.
Products: -
?
ATP + n-butyrate + CoA
ADP + phosphate + n-butyryl-CoA
-
Substrates: 3% of the activity relative to acetate
Products: -
?
ATP + phenylacetate + CoA
ADP + phosphate + phenylacetyl-CoA
-
Substrates: 10% activity compared to acetate
Products: -
?
ATP + phenylacetate + CoA
ADP + phosphate + phenylacetyl-CoA
Substrates: less than 4% activity compared to acetate
Products: -
r
ATP + phenylacetate + CoA
ADP + phosphate + phenylacetyl-CoA
Substrates: -
Products: -
?
ATP + propionate + CoA
ADP + phosphate + propionyl-CoA
-
Substrates: 100% activity compared to acetate
Products: -
?
ATP + propionate + CoA
ADP + phosphate + propionyl-CoA
-
Substrates: 100% activity compared to acetate
Products: -
?
ATP + propionate + CoA
ADP + phosphate + propionyl-CoA
-
Substrates: at 47% of the activity relative to acetate
Products: -
?
ATP + propionate + CoA
ADP + phosphate + propionyl-CoA
Substrates: 72% activity compared to acetate
Products: -
r
ATP + propionate + CoA
ADP + phosphate + propionyl-CoA
-
Substrates: at 108% of the activity with acetate
Products: -
?
ATP + propionate + CoA
ADP + phosphate + propionyl-CoA
-
Substrates: -
Products: -
?
ATP + thioglycolate + CoA
ADP + phosphate + thioglycolyl-CoA
-
Substrates: 110% activity compared to acetate
Products: -
?
ATP + thioglycolate + CoA
ADP + phosphate + thioglycolyl-CoA
Substrates: -
Products: -
?
GDP + phosphate + acetyl-CoA
GTP + acetate + CoA
-
Substrates: -
Products: -
?
GDP + phosphate + acetyl-CoA
GTP + acetate + CoA
Substrates: 106% activity compared to ADP
Products: -
r
GDP + phosphate + acetyl-CoA
GTP + acetate + CoA
-
Substrates: -
Products: -
?
GDP + phosphate + acetyl-CoA
GTP + acetate + CoA
-
Substrates: r, 220% of the activity relative to ADP
Products: -
?
GTP + acetate + CoA
GDP + phosphate + acetyl-CoA
Substrates: 57% activity compared to ATP
Products: -
r
GTP + acetate + CoA
GDP + phosphate + acetyl-CoA
-
Substrates: 11% of the activity with ATP
Products: -
?
IDP + phosphate + acetyl-CoA
ITP + acetate + CoA
-
Substrates: -
Products: -
?
IDP + phosphate + acetyl-CoA
ITP + acetate + CoA
Substrates: 28% activity compared to ADP
Products: -
r
IDP + phosphate + acetyl-CoA
ITP + acetate + CoA
-
Substrates: r, 250% of the activity relative to ADP
Products: -
?
additional information
?
-
-
Substrates: 4-hydroxyphenylacetate, indol-3-acetate and succinate are not utilized as substrates
Products: -
?
additional information
?
-
-
Substrates: 4-hydroxyphenylacetate, indol-3-acetate and succinate are not utilized as substrates
Products: -
?
additional information
?
-
Substrates: ADP-forming acetyl-CoA synthetase (ACD) catalyzes the interconversion of acetyl-CoA and acetate
Products: -
?
additional information
?
-
Substrates: ADP-forming acetyl-CoA synthetase (ACD) catalyzes the interconversion of acetyl-CoA and acetate
Products: -
?
additional information
?
-
Substrates: metabolites of both reaction directions are determined by gas chromatography
Products: -
?
additional information
?
-
-
Substrates: metabolites of both reaction directions are determined by gas chromatography
Products: -
?
additional information
?
-
Substrates: no activity with diphosphate, AMP, TDP, TTP, butyryl-CoA, succinyl-CoA, or phenylacetyl-CoA
Products: -
?
additional information
?
-
-
Substrates: no activity with diphosphate, AMP, TDP, TTP, butyryl-CoA, succinyl-CoA, or phenylacetyl-CoA
Products: -
?
additional information
?
-
-
Substrates: ACS1, encoded by the gene facA, is induced by acetate and repressed by glucose at the transcriptional level
Products: -
?
additional information
?
-
-
Substrates: ACS2 may be a stress protein, expressed under carbon source starvation
Products: -
?
additional information
?
-
-
Substrates: the enzyme performs catalytic arsenolysis of acetyl-CoA
Products: -
?
additional information
?
-
Substrates: the enzyme performs catalytic arsenolysis of acetyl-CoA
Products: -
?
additional information
?
-
Substrates: almost no activity with formate, 5-aminovalerate, 4-guanidinobutyrate, 2-(imidazol-4-yl)acetate, malonate, and succinate
Products: -
?
additional information
?
-
-
Substrates: almost no activity with formate, 5-aminovalerate, 4-guanidinobutyrate, 2-(imidazol-4-yl)acetate, malonate, and succinate
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ADP + phosphate + acetyl-CoA
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
additional information
?
-
ADP + phosphate + acetyl-CoA
?
-
Substrates: enzyme catalyzes acetate formation and ATP generation during fermentation of pyruvate to acetate
Products: -
?
ADP + phosphate + acetyl-CoA
?
-
Substrates: energy-conserving pyruvate-to-acetate pathway
Products: -
?
ADP + phosphate + acetyl-CoA
?
-
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA
?
-
Substrates: -
Products: -
?
ADP + phosphate + acetyl-CoA
?
-
Substrates: enzyme catalyzes acetate formation and ATP generation during fermentation of pyruvate to acetate
Products: -
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
-
Substrates: Archaeoglobus fulgidus strain 7324 converts starch to acetate via a modified Embden-Meyerhof pathway and acetyl-CoA synthetase (ADP-forming)
Products: -
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
-
Substrates: -
Products: -
r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
-
Substrates: -
Products: -
r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
Substrates: -
Products: -
r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
Substrates: -
Products: -
r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
Substrates: the specific activity in the acetate-forming direction is approximately half that observed in the acetyl-CoA-forming direction
Products: -
r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
Substrates: enzyme catalyzes acetate formation and ATP generation during fermentation of pyruvate to acetate
Products: -
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
Substrates: enzyme catalyzes acetate formation and ATP generation during fermentation of pyruvate to acetate
Products: -
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
-
Substrates: -
Products: -
r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
-
Substrates: downregulation of the enzyme is observed during periods of acetate consumption
Products: -
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
-
Substrates: -
Products: -
r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
-
Substrates: -
Products: -
ir
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
-
Substrates: -
Products: -
ir
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
-
Substrates: -
Products: -
r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
Q9Y8L0, Q9Y8L1
Substrates: major energy-conserving reaction during pyruvate and sugar conversion to acetate, catalyzing acetate formation and ATP synthesis
Products: -
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
-
Substrates: -
Products: -
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
-
Substrates: -
Products: -
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
Substrates: -
Products: -
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
Substrates: -
Products: -
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
Substrates: preferred direction of reaction
Products: -
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
-
Substrates: -
Products: -
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
-
Substrates: the enzyme is required for growth on ethanol. ACS activity is induced upon growth on ethanol, 2,3-butanediol, malonate and acetate
Products: -
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
Substrates: -
Products: -
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
Substrates: the enzyme catalyzes the formation of acetate from acetyl-CoA and concomitant ATP synthesis by the mechanism of substrate level phosphorylation
Products: -
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
-
Substrates: -
Products: -
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
Substrates: -
Products: -
?
additional information
?
-
Substrates: ADP-forming acetyl-CoA synthetase (ACD) catalyzes the interconversion of acetyl-CoA and acetate
Products: -
?
additional information
?
-
Substrates: ADP-forming acetyl-CoA synthetase (ACD) catalyzes the interconversion of acetyl-CoA and acetate
Products: -
?
additional information
?
-
-
Substrates: ACS1, encoded by the gene facA, is induced by acetate and repressed by glucose at the transcriptional level
Products: -
?
additional information
?
-
-
Substrates: ACS2 may be a stress protein, expressed under carbon source starvation
Products: -
?
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.
0.132 - 0.457
Isobutyrate
0.012 - 0.04
isobutyryl-CoA
0.329
phenylacetate
at pH 6.5 and 55°C
0.004 - 0.11
phenylacetyl-CoA
0.032
propionyl-CoA
at pH 7.3 and 37°C
0.322
thioglycolate
at pH 6.5 and 55°C
additional information
additional information
-
0.31
acetate
mutant enzyme H533D, pH and temperature not specified in the publication
0.4
acetate
mutant enzyme H533E, pH and temperature not specified in the publication
0.55
acetate
mutant enzyme H533Q, pH and temperature not specified in the publication
0.6
acetate
-
30°C, isoenzyme ACS1
0.625
acetate
pH 6.5, 55°C, recombinant wild-type enzyme
0.625
acetate
pH 6.5, 55°C, wild-type enzyme
0.68
acetate
mutant enzyme H533A, pH and temperature not specified in the publication
0.76
acetate
mutant enzyme H533N, pH and temperature not specified in the publication
0.783
acetate
pH 6.5, 55°C, mutant enzyme H257Dalpha
0.794
acetate
pH 6.5, 55°C, mutant enzyme E217Dalpha
0.8
acetate
Q9Y8L0, Q9Y8L1
-
0.8
acetate
pH 6.0, 37°C, recombinant enzyme
0.8
acetate
at pH 7.0 and 37°C
0.84
acetate
mutant enzyme H533K, pH and temperature not specified in the publication
0.9
acetate
-
in 100 mM HEPES-KOH pH 7.5, 0.1 mM 5,5'-dithiobis(2-nitrobenzoic acid), 5 mM MgCl2, at 55°C
1.02
acetate
-
pH 8.0, 37°C, isoenzyme ACS2
1.1
acetate
-
isoenzyme ACS I
1.1
acetate
-
pH 7.5, 37°C
1.3
acetate
at pH 6.0 and 37°C
1.5
acetate
at pH 6.5 and 55°C
1.7
acetate
mutant enzyme H533R, pH and temperature not specified in the publication
5.3
acetate
-
pH 9.0, at 37ºC, oxic conditions
14
acetate
wild type enzyme, pH and temperature not specified in the publication
14
acetate
at pH 7.3 and 37°C
0.0039
acetyl-CoA
pH 6.5, 55°C, wild-type enzyme
0.0062
acetyl-CoA
pH 6.5, 55°C, mutant enzyme H257Dalpha
0.01
acetyl-CoA
mutant enzyme H533A, pH and temperature not specified in the publication
0.012
acetyl-CoA
mutant enzyme H533E, pH and temperature not specified in the publication
0.014
acetyl-CoA
pH 6.5, 55°C, recombinant wild-type enzyme
0.015
acetyl-CoA
mutant enzyme H533N, pH and temperature not specified in the publication
0.016
acetyl-CoA
mutant enzyme H533R, pH and temperature not specified in the publication
0.019
acetyl-CoA
Q9Y8L0, Q9Y8L1
-
0.019
acetyl-CoA
mutant enzyme H533Q, pH and temperature not specified in the publication
0.023
acetyl-CoA
-
50°C, pH not specified in the publication
0.025
acetyl-CoA
-
isoenzyme ACS I
0.026
acetyl-CoA
-
isoenzyme ACS II
0.027
acetyl-CoA
mutant enzyme H533D, pH and temperature not specified in the publication
0.03
acetyl-CoA
mutant enzyme H533K, pH and temperature not specified in the publication
0.037
acetyl-CoA
-
in 100 mM HEPES-KOH pH 7.5, 0.1 mM 5,5'-dithiobis(2-nitrobenzoic acid), 5 mM MgCl2, at 55°C
0.04
acetyl-CoA
at pH 7.3 and 37°C
0.043
acetyl-CoA
wild type enzyme, pH and temperature not specified in the publication
0.06
acetyl-CoA
pH 7.5, at 30ºC
0.082
acetyl-CoA
pH 6.5, 55°C, mutant enzyme E217Dalpha
0.12
acetyl-CoA
-
pH 6.5, 85°C
0.13
acetyl-CoA
at pH 7.0 and 37°C
0.14
acetyl-CoA
pH 7.0, 37°C, recombinant enzyme
0.14
acetyl-CoA
at pH 6.0 and 37°C
0.45
acetyl-CoA
-
pH 7.5, 37°C
0.015
ADP
-
50°C, pH not specified in the publication
0.046
ADP
-
pH 7.5, 37°C
0.061
ADP
-
isoenzyme ACS II
0.0741
ADP
pH 6.5, 55°C, mutant enzyme H257Dalpha
0.091
ADP
-
in 100 mM HEPES-KOH pH 7.5, 0.1 mM 5,5'-dithiobis(2-nitrobenzoic acid), 5 mM MgCl2, at 55°C
0.094
ADP
pH 6.5, 55°C, wild-type enzyme
0.15
ADP
-
isoenzyme ACS I
0.283
ADP
pH 6.5, 55°C, mutant enzyme E217Dalpha
0.41
ADP
mutant enzyme H533A, pH and temperature not specified in the publication
0.57
ADP
mutant enzyme H533N, pH and temperature not specified in the publication
0.6
ADP
mutant enzyme H533D, pH and temperature not specified in the publication
0.64
ADP
mutant enzyme H533R, pH and temperature not specified in the publication
0.71
ADP
with propionyl-CoA as cosubstrate, at pH 7.3 and 37°C
0.9
ADP
at pH 7.0 and 37°C
0.97
ADP
mutant enzyme H533K, pH and temperature not specified in the publication
1.19
ADP
mutant enzyme H533E, pH and temperature not specified in the publication
1.28
ADP
mutant enzyme H533Q, pH and temperature not specified in the publication
1.56
ADP
wild type enzyme, pH and temperature not specified in the publication
1.6
ADP
with acetyl-CoA as cosubstrate, at pH 7.3 and 37°C
1.9
ADP
pH 7.0, 37°C, recombinant enzyme
1.9
ADP
at pH 6.0 and 37°C
0.0556
ATP
at pH 6.5 and 55°C
0.221
ATP
pH 6.5, 55°C, recombinant wild-type enzyme
0.221
ATP
pH 6.5, 55°C, wild-type enzyme
0.3
ATP
pH 6.0, 37°C, recombinant enzyme
0.3
ATP
at pH 7.0 and 37°C
0.388
ATP
pH 6.5, 55°C, mutant enzyme H257Dalpha
0.473
ATP
pH 6.5, 55°C, mutant enzyme E217Dalpha
0.477
ATP
-
isoenzyme ACS I
0.57
ATP
-
in 100 mM HEPES-KOH pH 7.5, 0.1 mM 5,5'-dithiobis(2-nitrobenzoic acid), 5 mM MgCl2, at 55°C
0.6
ATP
at pH 6.0 and 37°C
1
ATP
-
pH 9.0, at 37ºC, oxic conditions
1.2
ATP
mutant enzyme H533D, pH and temperature not specified in the publication
1.7
ATP
mutant enzyme H533K, pH and temperature not specified in the publication
2.2
ATP
mutant enzyme H533A, pH and temperature not specified in the publication
2.5
ATP
mutant enzyme H533Q, pH and temperature not specified in the publication
2.5
ATP
mutant enzyme H533R, pH and temperature not specified in the publication
3.9
ATP
mutant enzyme H533E, pH and temperature not specified in the publication
7.2
ATP
with propionate as cosubstrate, at pH 7.3 and 37°C
7.7
ATP
mutant enzyme H533N, pH and temperature not specified in the publication
12
ATP
wild type enzyme, pH and temperature not specified in the publication
12
ATP
with acetate as cosubstrate, at pH 7.3 and 37°C
0.0056
CoA
at pH 6.5 and 55°C
0.011
CoA
mutant enzyme H533D, pH and temperature not specified in the publication
0.011
CoA
mutant enzyme H533Q, pH and temperature not specified in the publication
0.0139
CoA
pH 6.5, 55°C, wild-type enzyme
0.018
CoA
-
isoenzyme ACS I
0.021
CoA
Q9Y8L0, Q9Y8L1
-
0.024
CoA
-
in 100 mM HEPES-KOH pH 7.5, 0.1 mM 5,5'-dithiobis(2-nitrobenzoic acid), 5 mM MgCl2, at 55°C
0.041
CoA
pH 6.5, 55°C, mutant enzyme E217Dalpha
0.07
CoA
mutant enzyme H533A, pH and temperature not specified in the publication
0.0771
CoA
pH 6.5, 55°C, mutant enzyme H257Dalpha
0.08
CoA
mutant enzyme H533N, pH and temperature not specified in the publication
0.1
CoA
mutant enzyme H533R, pH and temperature not specified in the publication
0.13
CoA
mutant enzyme H533K, pH and temperature not specified in the publication
0.2
CoA
pH 6.0, 37°C, recombinant enzyme
0.2
CoA
at pH 7.0 and 37°C
0.2
CoA
wild type enzyme, pH and temperature not specified in the publication
0.2
CoA
with acetate as cosubstrate, at pH 7.3 and 37°C
0.26
CoA
mutant enzyme H533E, pH and temperature not specified in the publication
0.4
CoA
at pH 6.0 and 37°C
0.41
CoA
-
pH 9.0, at 37ºC, oxic conditions
1.6
CoA
with propionate as cosubstrate, at pH 7.3 and 37°C
0.132
GDP
-
isoenzyme ACS I
0.236
GDP
-
isoenzyme ACS II
1.9
GDP
with acetyl-CoA as cosubstrate, at pH 7.3 and 37°C
0.43
GTP
-
isoenzyme ACS I
10
GTP
with acetate as cosubstrate, at pH 7.3 and 37°C
0.132
Isobutyrate
at pH 6.5 and 55°C
0.457
Isobutyrate
-
isoenzyme ACS I
0.012
isobutyryl-CoA
-
isoenzyme ACS II
0.029
isobutyryl-CoA
-
isoenzyme ACS I
0.04
isobutyryl-CoA
-
pH 6.5, 85°C
0.004
phenylacetyl-CoA
-
isoenzyme ACS II
0.11
phenylacetyl-CoA
-
pH 6.5, 85°C
0.1
phosphate
Q9Y8L0, Q9Y8L1
-
0.15
phosphate
mutant enzyme H533R, pH and temperature not specified in the publication
0.18
phosphate
mutant enzyme H533E, pH and temperature not specified in the publication
0.25
phosphate
mutant enzyme H533D, pH and temperature not specified in the publication
0.272
phosphate
pH 6.5, 55°C, recombinant wild-type enzyme
0.272
phosphate
pH 6.5, 55°C, wild-type enzyme
0.3
phosphate
-
50°C, pH not specified in the publication
0.396
phosphate
-
isoenzyme ACS I
0.58
phosphate
-
isoenzyme ACS II
0.714
phosphate
pH 6.5, 55°C, mutant enzyme E217Dalpha
0.75
phosphate
mutant enzyme H533A, pH and temperature not specified in the publication
0.86
phosphate
mutant enzyme H533Q, pH and temperature not specified in the publication
0.919
phosphate
pH 6.5, 55°C, mutant enzyme H257Dalpha
0.94
phosphate
mutant enzyme H533N, pH and temperature not specified in the publication
1
phosphate
-
in 100 mM HEPES-KOH pH 7.5, 0.1 mM 5,5'-dithiobis(2-nitrobenzoic acid), 5 mM MgCl2, at 55°C
1.35
phosphate
pH 7.5, at 30ºC
1.5
phosphate
with propionyl-CoA as cosubstrate, at pH 7.3 and 37°C
1.77
phosphate
wild type enzyme, pH and temperature not specified in the publication
1.8
phosphate
at pH 7.0 and 37°C
1.8
phosphate
with acetyl-CoA as cosubstrate, at pH 7.3 and 37°C
2
phosphate
-
pH 7.5, 37°C
2.7
phosphate
pH 7.0, 37°C, recombinant enzyme
2.7
phosphate
at pH 6.0 and 37°C
3.25
phosphate
mutant enzyme H533K, pH and temperature not specified in the publication
5.2
propionate
-
pH 8.0, 37°C, isoenzyme ACS2
8.55
propionate
-
30°C, isoenzyme ACS1
29
propionate
at pH 7.3 and 37°C
additional information
additional information
-
kinetics of wild-type and mutant enzymes
-
additional information
additional information
kinetics of wild-type and mutant enzymes
-
additional information
additional information
Michaelis-Menten kinetics, the amoebal ACS displays hyperbolic kinetics for its substrates acetyl-CoA, Pi and ADP and its products acetate, ATP and CoA
-
additional information
additional information
-
Michaelis-Menten kinetics, the amoebal ACS displays hyperbolic kinetics for its substrates acetyl-CoA, Pi and ADP and its products acetate, ATP and CoA
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
66
indoleacetate
-
isoenzyme ACS II
138
phenylacetyl-CoA
-
isoenzyme ACS II
190
propionate
at pH 7.3 and 37°C
21
propionyl-CoA
at pH 7.3 and 37°C
26.1
thioglycolate
at pH 6.5 and 55°C
0.18
acetate
mutant enzyme H533D, pH and temperature not specified in the publication
0.26
acetate
mutant enzyme H533E, pH and temperature not specified in the publication
1.2
acetate
mutant enzyme H533Q, pH and temperature not specified in the publication
1.5
acetate
mutant enzyme H533N, pH and temperature not specified in the publication
3.3
acetate
mutant enzyme H533A, pH and temperature not specified in the publication
3.4
acetate
mutant enzyme H533K, pH and temperature not specified in the publication
5.6
acetate
mutant enzyme H533R, pH and temperature not specified in the publication
35
acetate
at pH 6.0 and 37°C
46
acetate
pH 6.0, 37°C, recombinant enzyme
46
acetate
at pH 7.0 and 37°C
49.3
acetate
at pH 6.5 and 55°C
67
acetate
-
isoenzyme ACS II
233
acetate
wild type enzyme, pH and temperature not specified in the publication
240
acetate
at pH 7.3 and 37°C
0.12
acetyl-CoA
mutant enzyme H533E, pH and temperature not specified in the publication
1.4
acetyl-CoA
mutant enzyme H533N, pH and temperature not specified in the publication
1.6
acetyl-CoA
mutant enzyme H533D, pH and temperature not specified in the publication
1.7
acetyl-CoA
mutant enzyme H533Q, pH and temperature not specified in the publication
2.4
acetyl-CoA
mutant enzyme H533K, pH and temperature not specified in the publication
2.7
acetyl-CoA
mutant enzyme H533A, pH and temperature not specified in the publication
18
acetyl-CoA
mutant enzyme H533R, pH and temperature not specified in the publication
34
acetyl-CoA
pH 7.0, 37°C, recombinant enzyme
34
acetyl-CoA
at pH 6.0 and 37°C
42
acetyl-CoA
-
isoenzyme ACS II
55
acetyl-CoA
at pH 7.0 and 37°C
110
acetyl-CoA
at pH 7.3 and 37°C
111
acetyl-CoA
wild type enzyme, pH and temperature not specified in the publication
157
acetyl-CoA
-
isoenzyme ACS I
0.27
ADP
mutant enzyme H533E, pH and temperature not specified in the publication
1.4
ADP
mutant enzyme H533N, pH and temperature not specified in the publication
1.7
ADP
mutant enzyme H533D, pH and temperature not specified in the publication
2.5
ADP
mutant enzyme H533Q, pH and temperature not specified in the publication
2.8
ADP
mutant enzyme H533A, pH and temperature not specified in the publication
3.3
ADP
mutant enzyme H533K, pH and temperature not specified in the publication
20
ADP
mutant enzyme H533R, pH and temperature not specified in the publication
24
ADP
with propionyl-CoA as cosubstrate, at pH 7.3 and 37°C
34
ADP
pH 7.0, 37°C, recombinant enzyme
115
ADP
-
isoenzyme ACS II
138
ADP
wild type enzyme, pH and temperature not specified in the publication
140
ADP
with acetyl-CoA as cosubstrate, at pH 7.3 and 37°C
203
ADP
-
isoenzyme ACS I
0.25
ATP
mutant enzyme H533D, pH and temperature not specified in the publication
0.28
ATP
mutant enzyme H533E, pH and temperature not specified in the publication
1.4
ATP
mutant enzyme H533Q, pH and temperature not specified in the publication
2
ATP
mutant enzyme H533N, pH and temperature not specified in the publication
3.3
ATP
mutant enzyme H533A, pH and temperature not specified in the publication
3.7
ATP
mutant enzyme H533K, pH and temperature not specified in the publication
6.6
ATP
mutant enzyme H533R, pH and temperature not specified in the publication
46
ATP
pH 6.0, 37°C, recombinant enzyme
53.7
ATP
at pH 6.5 and 55°C
68
ATP
-
isoenzyme ACS II
240
ATP
with propionate as cosubstrate, at pH 7.3 and 37°C
320
ATP
wild type enzyme, pH and temperature not specified in the publication
320
ATP
with acetate as cosubstrate, at pH 7.3 and 37°C
0.25
CoA
mutant enzyme H533D, pH and temperature not specified in the publication
0.27
CoA
mutant enzyme H533E, pH and temperature not specified in the publication
1.3
CoA
mutant enzyme H533Q, pH and temperature not specified in the publication
2
CoA
mutant enzyme H533N, pH and temperature not specified in the publication
4.1
CoA
mutant enzyme H533K, pH and temperature not specified in the publication
4.2
CoA
mutant enzyme H533A, pH and temperature not specified in the publication
7
CoA
mutant enzyme H533R, pH and temperature not specified in the publication
46
CoA
pH 6.0, 37°C, recombinant enzyme
53.1
CoA
at pH 6.5 and 55°C
70
CoA
-
isoenzyme ACS II
220
CoA
with acetate as cosubstrate, at pH 7.3 and 37°C
260
CoA
with propionate as cosubstrate, at pH 7.3 and 37°C
328
CoA
wild type enzyme, pH and temperature not specified in the publication
21
GDP
-
isoenzyme ACS II
170
GDP
with acetyl-CoA as cosubstrate, at pH 7.3 and 37°C
411
GDP
-
isoenzyme ACS I
27
GTP
-
isoenzyme ACS II
180
GTP
with acetate as cosubstrate, at pH 7.3 and 37°C
22
Isobutyrate
-
isoenzyme ACS II
50.9
Isobutyrate
at pH 6.5 and 55°C
55
Isobutyrate
-
isoenzyme ACS I
8
isobutyryl-CoA
-
isoenzyme ACS II
121
isobutyryl-CoA
-
GTP, isoenzyme ACS I
40.6
phenylacetate
at pH 6.5 and 55°C
89
phenylacetate
-
isoenzyme ACS II
0.22
phosphate
mutant enzyme H533E, pH and temperature not specified in the publication
1.5
phosphate
mutant enzyme H533N, pH and temperature not specified in the publication
1.7
phosphate
mutant enzyme H533D, pH and temperature not specified in the publication
1.8
phosphate
mutant enzyme H533Q, pH and temperature not specified in the publication
2.3
phosphate
mutant enzyme H533A, pH and temperature not specified in the publication
3.1
phosphate
mutant enzyme H533K, pH and temperature not specified in the publication
14
phosphate
mutant enzyme H533R, pH and temperature not specified in the publication
18
phosphate
with propionyl-CoA as cosubstrate, at pH 7.3 and 37°C
34
phosphate
pH 7.0, 37°C, recombinant enzyme
115
phosphate
wild type enzyme, pH and temperature not specified in the publication
117
phosphate
-
isoenzyme ACS II
120
phosphate
with acetyl-CoA as cosubstrate, at pH 7.3 and 37°C
182
phosphate
-
isoenzyme ACS I
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
90
GDP
with acetyl-CoA as cosubstrate, at pH 7.3 and 37°C
18
GTP
with acetate as cosubstrate, at pH 7.3 and 37°C
385
Isobutyrate
at pH 6.5 and 55°C
123
phenylacetate
at pH 6.5 and 55°C
6.3
propionate
at pH 7.3 and 37°C
650
propionyl-CoA
at pH 7.3 and 37°C
81
thioglycolate
at pH 6.5 and 55°C
0.59
acetate
mutant enzyme H533D, pH and temperature not specified in the publication
0.67
acetate
mutant enzyme H533E, pH and temperature not specified in the publication
1.9
acetate
mutant enzyme H533N, pH and temperature not specified in the publication
2.2
acetate
mutant enzyme H533Q, pH and temperature not specified in the publication
3.3
acetate
mutant enzyme H533R, pH and temperature not specified in the publication
4.1
acetate
mutant enzyme H533K, pH and temperature not specified in the publication
4.8
acetate
mutant enzyme H533A, pH and temperature not specified in the publication
16
acetate
wild type enzyme, pH and temperature not specified in the publication
16
acetate
at pH 7.3 and 37°C
26
acetate
at pH 6.0 and 37°C
32.8
acetate
at pH 6.5 and 55°C
58
acetate
at pH 7.0 and 37°C
58
acetate
pH 6.0, 37°C, recombinant enzyme
0.06
acetyl-CoA
mutant enzyme H533D, pH and temperature not specified in the publication
0.09
acetyl-CoA
mutant enzyme H533Q, pH and temperature not specified in the publication
10
acetyl-CoA
mutant enzyme H533E, pH and temperature not specified in the publication
79
acetyl-CoA
mutant enzyme H533K, pH and temperature not specified in the publication
92
acetyl-CoA
mutant enzyme H533N, pH and temperature not specified in the publication
239
acetyl-CoA
at pH 6.0 and 37°C
239
acetyl-CoA
pH 7.0, 37°C, recombinant enzyme
266
acetyl-CoA
mutant enzyme H533A, pH and temperature not specified in the publication
458
acetyl-CoA
at pH 7.0 and 37°C
1115
acetyl-CoA
mutant enzyme H533R, pH and temperature not specified in the publication
2600
acetyl-CoA
wild type enzyme, pH and temperature not specified in the publication
2600
acetyl-CoA
at pH 7.3 and 37°C
0.2
ADP
mutant enzyme H533E, pH and temperature not specified in the publication
1.9
ADP
mutant enzyme H533Q, pH and temperature not specified in the publication
2.5
ADP
mutant enzyme H533N, pH and temperature not specified in the publication
2.9
ADP
mutant enzyme H533D, pH and temperature not specified in the publication
3.4
ADP
mutant enzyme H533K, pH and temperature not specified in the publication
6.9
ADP
mutant enzyme H533A, pH and temperature not specified in the publication
17
ADP
at pH 6.0 and 37°C
17
ADP
pH 7.0, 37°C, recombinant enzyme
32
ADP
mutant enzyme H533R, pH and temperature not specified in the publication
34
ADP
with propionyl-CoA as cosubstrate, at pH 7.3 and 37°C
76
ADP
at pH 7.0 and 37°C
89
ADP
wild type enzyme, pH and temperature not specified in the publication
89
ADP
with acetyl-CoA as cosubstrate, at pH 7.3 and 37°C
0.07
ATP
mutant enzyme H533E, pH and temperature not specified in the publication
0.21
ATP
mutant enzyme H533D, pH and temperature not specified in the publication
0.26
ATP
mutant enzyme H533N, pH and temperature not specified in the publication
1.6
ATP
mutant enzyme H533A, pH and temperature not specified in the publication
2.4
ATP
mutant enzyme H533K, pH and temperature not specified in the publication
2.7
ATP
mutant enzyme H533R, pH and temperature not specified in the publication
27
ATP
wild type enzyme, pH and temperature not specified in the publication
27
ATP
with acetate as cosubstrate, at pH 7.3 and 37°C
33
ATP
with propionate as cosubstrate, at pH 7.3 and 37°C
59
ATP
at pH 6.0 and 37°C
116
ATP
mutant enzyme H533Q, pH and temperature not specified in the publication
144
ATP
at pH 7.0 and 37°C
144
ATP
pH 6.0, 37°C, recombinant enzyme
965
ATP
at pH 6.5 and 55°C
0.57
CoA
mutant enzyme H533Q, pH and temperature not specified in the publication
1.1
CoA
mutant enzyme H533E, pH and temperature not specified in the publication
23
CoA
mutant enzyme H533D, pH and temperature not specified in the publication
26
CoA
mutant enzyme H533N, pH and temperature not specified in the publication
60
CoA
mutant enzyme H533A, pH and temperature not specified in the publication
70
CoA
mutant enzyme H533R, pH and temperature not specified in the publication
90
CoA
at pH 6.0 and 37°C
160
CoA
with propionate as cosubstrate, at pH 7.3 and 37°C
213
CoA
at pH 7.0 and 37°C
213
CoA
pH 6.0, 37°C, recombinant enzyme
287
CoA
mutant enzyme H533K, pH and temperature not specified in the publication
1100
CoA
wild type enzyme, pH and temperature not specified in the publication
1100
CoA
with acetate as cosubstrate, at pH 7.3 and 37°C
9490
CoA
at pH 6.5 and 55°C
0.97
phosphate
mutant enzyme H533K, pH and temperature not specified in the publication
1.3
phosphate
mutant enzyme H533E, pH and temperature not specified in the publication
1.7
phosphate
mutant enzyme H533N, pH and temperature not specified in the publication
2.1
phosphate
mutant enzyme H533Q, pH and temperature not specified in the publication
3.1
phosphate
mutant enzyme H533A, pH and temperature not specified in the publication
7.3
phosphate
mutant enzyme H533D, pH and temperature not specified in the publication
12
phosphate
at pH 6.0 and 37°C
12
phosphate
pH 7.0, 37°C, recombinant enzyme
12
phosphate
with propionyl-CoA as cosubstrate, at pH 7.3 and 37°C
32
phosphate
at pH 7.0 and 37°C
65
phosphate
wild type enzyme, pH and temperature not specified in the publication
65
phosphate
with acetyl-CoA as cosubstrate, at pH 7.3 and 37°C
95
phosphate
mutant enzyme H533R, pH and temperature not specified in the publication
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