Information on EC 6.2.1.13 - Acetate-CoA ligase (ADP-forming)

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

EC NUMBER
COMMENTARY
6.2.1.13
-
RECOMMENDED NAME
GeneOntology No.
Acetate-CoA ligase (ADP-forming)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + acetate + CoA = ADP + phosphate + acetyl-CoA
show the reaction diagram
-
-
-
-
ATP + acetate + CoA = ADP + phosphate + acetyl-CoA
show the reaction diagram
reaction mechanism and structural modelling, formation of enzyme-bound acetyl phosphate and enzyme phosphorylation at His257alpha, overview, reaction mechanism: the formation of enzyme-bound acetyl phosphate and enzyme phosphorylation at His-257alpha, respectively, proceeds in analogy to succinyl-CoA synthetases. In contrast to succinyl-CoA synthetases, in acetyl-CoA synthetase the phosphoryl group is transferred from the His-257alpha to ADP via transient phosphorylation of a second conserved histidine residue in the beta-subunit, His-71alpha. It is proposed that acetyl-CoA synthetase reaction follows a four-step mechanism including transient phosphorylation of two active site histidine residues
E7FI45 and E7FHP1
ATP + acetate + CoA = ADP + phosphate + acetyl-CoA
show the reaction diagram
reaction mechanism: the formation of enzyme-bound acetyl phosphate and enzyme phosphorylation at His-257alpha, respectively, proceeds in analogy to succinyl-CoA synthetases. In contrast to succinyl-CoA synthetases, in acetyl-CoA synthetase the phosphoryl group is transferred from the His-257alpha to ADP via transient phosphorylation of a second conserved histidine residue in the beta-subunit, His-71alpha. It is proposed that acetyl-CoA synthetase reaction follows a four-step mechanism including transient phosphorylation of two active site histidine residues
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acid-thiol ligation
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
acetate formation from acetyl-CoA II
-
-
acetyl CoA biosynthesis
-
-
Glycolysis / Gluconeogenesis
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
Propanoate metabolism
-
-
pyruvate fermentation to acetate III
-
-
Pyruvate metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
Acetate:CoA ligase (ADP-forming)
Also acts on propanoate and, very slowly, on butanoate.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acetate:coenzyme A ligase (ADP-forming)
-
-
Acetyl-CoA synthetase (ADP-forming)
-
-
-
-
Acetyl-CoA synthetase (ADP-forming)
-
-
Acetyl-CoA synthetase (ADP-forming)
-
-
-
acetyl-coenzyme A synthetase
-
-
acetyl-coenzyme A synthetase (ADP-forming)
Q9Y8L1
-
ACS
-
-
-
-
ADP-ACS
Archaeoglobus fulgidus 7324
-
-
-
ADP-forming acetyl-CoA synthetase
-
-
ADP-forming acetyl-CoA synthetase
Archaeoglobus fulgidus 7324
-
-
-
ADP-forming acetyl-CoA synthetase
-
-
ADP-forming acetyl-CoA synthetase
-
-
ADP-forming acetyl-CoA synthetase isoenzyme I
-
-
ADP-forming acetyl-CoA synthetase isoenzyme I
-
-
-
PF1540
E7FI45 and E7FHP1
gene name alpha subunit
PF1787
E7FI45 and E7FHP1
gene name, beta-subunit
Synthetase, acetyl coenzyme A (adenosine diphosphate-forming)
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
62009-85-2
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Archaeoglobus fulgidus 7324
-
-
-
Manually annotated by BRENDA team
strain WB, clone 6, ATCC 30957
SwissProt
Manually annotated by BRENDA team
Giardia intestinalis WB
strain WB, clone 6, ATCC 30957
SwissProt
Manually annotated by BRENDA team
strain DSM 5350
-
-
Manually annotated by BRENDA team
strain DSM 3757
-
-
Manually annotated by BRENDA team
strain DSM 1137
-
-
Manually annotated by BRENDA team
enzyme form ACS1; enzyme form ACS2
-
-
Manually annotated by BRENDA team
strain DSM 4184
-
-
Manually annotated by BRENDA team
2 isoenzymes: ACS I and ACS II
-
-
Manually annotated by BRENDA team
ACD isoenzyme I, acdIa and acdIb genes encoding alpha- and beta-subunit of ACD
-
-
Manually annotated by BRENDA team
E7FI45 (alpha-subunit), E7FHP1 (beta-subunit)
E7FI45 and E7FHP1
-
Manually annotated by BRENDA team
subunit alpha; isoenzyme ACS I
Q9Y8L1
SwissProt
Manually annotated by BRENDA team
subunit beta; isoenzyme ACS I
Q9Y8L0
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
growth arrest is caused by elevated Acs, EC 6.2.1.1, activity, while overproduction of ADP-forming Ac-CoA synthesizing systems do not affect the growth behaviour of acetylation-deficient or acetylation-proficient strains
physiological function
-
Archaeoglobus fulgidus strain 7324 converts starch to acetate via a modified Embden-Meyerhof pathway and acetyl-CoA synthetase (ADP-forming)
physiological function
Archaeoglobus fulgidus 7324
-
Archaeoglobus fulgidus strain 7324 converts starch to acetate via a modified Embden-Meyerhof pathway and acetyl-CoA synthetase (ADP-forming)
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
-
-
-
-
r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
-
-
-
-
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
-
-
-
ir, r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
-
-
-
-
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
-
-
-
-
r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
-
-
-
-
r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
-
-
-
r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
Q9Y1N2
-
-
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
Q9Y8L0, Q9Y8L1
-
-
r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
-
-
-
ir, r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
-
r
-
-
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
-
r
-
-
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
-
r
-
-
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
-
reverse reaction not detected
-
-
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
-
isoenzymes ACS I and ACS II
-
-
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
Q9Y1N2
no activity with butanoyl-CoA, propanoyl-CoA and pentanoyl-CoA
-
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
Q9Y1N2
enzyme catalyzes acetate formation and ATP generation during fermentation of pyruvate to acetate
-
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
Q9Y1N2
enzyme catalyzes acetate formation and ATP generation during fermentation of pyruvate to acetate
-
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
Q9Y8L0, Q9Y8L1
major energy-conserving reaction during pyruvate and sugar conversion to acetate, catalyzing acetate formation and ATP synthesis
-
r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
-
downregulation of the enzyme is observed during periods of acetate consumption
-
-
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
-
Archaeoglobus fulgidus strain 7324 converts starch to acetate via a modified Embden-Meyerhof pathway and acetyl-CoA synthetase (ADP-forming)
-
-
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
Giardia intestinalis WB
Q9Y1N2
enzyme catalyzes acetate formation and ATP generation during fermentation of pyruvate to acetate
-
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
-
-
-
-
r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
Archaeoglobus fulgidus 7324
-
-
-
-
?
ADP + phosphate + acetyl-CoA
?
show the reaction diagram
-
-
-
-
-
ADP + phosphate + acetyl-CoA
?
show the reaction diagram
-
-
-
-
-
ADP + phosphate + acetyl-CoA
?
show the reaction diagram
-
enzyme catalyzes acetate formation and ATP generation during fermentation of pyruvate to acetate
-
-
-
ADP + phosphate + acetyl-CoA
?
show the reaction diagram
-
enzyme catalyzes acetate formation and ATP generation during fermentation of pyruvate to acetate, energy-conserving pyruvate-to-acetate pathway
-
-
-
ADP + phosphate + butanoyl-CoA
ATP + butanoate + CoA
show the reaction diagram
Q9Y1N2
23% of the activity relative to acetyl-CoA
-
?
ADP + phosphate + butanoyl-CoA
ATP + butanoate + CoA
show the reaction diagram
Giardia intestinalis, Giardia intestinalis WB
Q9Y1N2
less efficiently than acetyl-CoA
-
?
ADP + phosphate + butyryl-CoA
ATP + butyrate + CoA
show the reaction diagram
-
no activity with n-butyryl-CoA
-
-
-
ADP + phosphate + butyryl-CoA
ATP + butyrate + CoA
show the reaction diagram
-
92% of the activity relative to acetyl-CoA
-
-
ADP + phosphate + indoleacetyl-CoA
ATP + indoleacetate + CoA
show the reaction diagram
-
r, isoenzyme ACS II is active, ACS I not
-
-
-
ADP + phosphate + isobutyryl-CoA
ATP + isobutyrate + CoA
show the reaction diagram
-
-
-
-
r
ADP + phosphate + phenylacetyl-CoA
ATP + phenylacetate + CoA
show the reaction diagram
-
-
-
-
r
ADP + phosphate + phenylacetyl-CoA
ATP + phenylacetate + CoA
show the reaction diagram
-
r, isoenzyme ACS II is active, ACS I not
-
-
-
ADP + phosphate + propanoyl-CoA
ATP + propanoate + CoA
show the reaction diagram
Q9Y1N2
45% of the activity relative to acetyl-CoA
-
?
ADP + phosphate + propionyl-CoA
ATP + propionate + CoA
show the reaction diagram
-
r
-
-
ADP + phosphate + propionyl-CoA
ATP + propionate + CoA
show the reaction diagram
-
39% of the activity relative to acetyl-CoA
-
-
-
ADP + phosphate + propionyl-CoA
ATP + propionate + CoA
show the reaction diagram
-
110% of the activity relative to acetyl-CoA
-
-
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
show the reaction diagram
-
no activity with isoenzymes ACS I and ACS II
-
-
-
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
show the reaction diagram
-
30% of the activity relative to acetyl-CoA
-
-
-
ATP + 2-methylbutyrate + CoA
ADP + phosphate + 2-methylbutyryl-CoA
show the reaction diagram
-
75% activity compared to acetate
-
-
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
-
-
-
-
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
-
-
-
-
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
-
-
-
-
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
E7FI45 and E7FHP1
-
-
-
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
-
100% activity
-
-
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
-
the enzyme is required for growth on ethanol. ACS activity is induced upon growth on ethanol, 2,3-butanediol, malonate and acetate
-
-
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
E7FI45 and E7FHP1
the enzyme catalyzes the formation of acetate from acetyl-CoA and concomitant ATP synthesis by the mechanism of substrate level phosphorylation, 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
-
-
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
-
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
-
-
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
-
-
-
-
r
ATP + butyrate + CoA
ADP + phosphate + butyryl-CoA
show the reaction diagram
-
at 98% of the activity with acetate
-
-
?
ATP + butyrate + CoA
ADP + phosphate + butyryl-CoA
show the reaction diagram
-
98% activity compared to acetate
-
-
?
ATP + imidazole-4-acetate + CoA
ADP + phosphate + imidazole-4-acetyl-CoA
show the reaction diagram
-
17% activity compared to acetate
-
-
?
ATP + isobutyrate + CoA
ADP + phosphate + isobutyryl-CoA
show the reaction diagram
-
r, isoenzymes ACS I and ACS II
-
-
-
ATP + isobutyrate + CoA
ADP + phosphate + isobutyryl-CoA
show the reaction diagram
-
79% of the activity relative to acetate
-
-
-
ATP + isobutyrate + CoA
ADP + phosphate + isobutyryl-CoA
show the reaction diagram
-
at 38% of the activity with acetate
-
-
?
ATP + isobutyrate + CoA
ADP + phosphate + isobutyryl-CoA
show the reaction diagram
-
46% activity compared to acetate
-
-
?
ATP + isopentanioate + CoA
ADP + phosphate + isovaleryl-CoA
show the reaction diagram
-
34% of the activity relative to acetate
-
-
-
ATP + isovalerate + CoA
ADP + phosphate + isovaleryl-CoA
show the reaction diagram
-
at 25% of the activity with acetate
-
-
?
ATP + isovalerate + CoA
ADP + phosphate + isovaleryl-CoA
show the reaction diagram
-
65% activity compared to acetate
-
-
?
ATP + n-butyrate + CoA
ADP + phosphate + n-butyryl-CoA
show the reaction diagram
-
s.o., 3% of the activity relative to acetate
-
-
-
ATP + pentanoate + CoA
ADP + phosphate + valeryl-CoA
show the reaction diagram
-
36% of the activity relative to acetate
-
-
-
ATP + phenylacetate + CoA
ADP + phosphate + phenylacetyl-CoA
show the reaction diagram
-
10% activity compared to acetate
-
-
?
ATP + propionate + CoA
ADP + phosphate + propionyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + propionate + CoA
ADP + phosphate + propionyl-CoA
show the reaction diagram
-
at 47% of the activity relative to acetate
-
-
-
ATP + propionate + CoA
ADP + phosphate + propionyl-CoA
show the reaction diagram
-
at 108% of the activity with acetate
-
-
?
ATP + propionate + CoA
ADP + phosphate + propionyl-CoA
show the reaction diagram
-
100% activity compared to acetate
-
-
?
ATP + thioglycolate + CoA
ADP + phosphate + thioglycolyl-CoA
show the reaction diagram
-
110% activity compared to acetate
-
-
?
dADP + phosphate + acetyl-CoA
dATP + acetate + CoA
show the reaction diagram
-
40% of the activity relative to ADP
-
-
-
GDP + phosphate + acetyl-CoA
GTP + acetate + CoA
show the reaction diagram
-
-
-
-
-
GDP + phosphate + acetyl-CoA
GTP + acetate + CoA
show the reaction diagram
-
-
-
-
-
GDP + phosphate + acetyl-CoA
GTP + acetate + CoA
show the reaction diagram
-
r, 220% of the activity relative to ADP
-
-
GTP + acetate + CoA
GDP + phosphate + acetyl-CoA
show the reaction diagram
-
11% of the activity with ATP
-
-
?
IDP + phosphate + acetyl-CoA
ITP + acetate + CoA
show the reaction diagram
-
-
-
-
-
IDP + phosphate + acetyl-CoA
ITP + acetate + CoA
show the reaction diagram
-
r, 250% of the activity relative to ADP
-
-
additional information
?
-
-
ACS1, encoded by the gene facA, is induced by acetate and repressed by glucose at the transcriptional level, ACS2 may be a stress protein, expressed under carbon source starvation
-
-
-
additional information
?
-
E7FI45 and E7FHP1
the enzyme performs catalytic arsenolysis of acetyl-CoA
-
-
-
additional information
?
-
-
4-hydroxyphenylacetate, indol-3-acetate and succinate are not utilized as substrates
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
-
-
-
-
r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
-
-
-
ir
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
-
-
-
-
r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
-
-
-
-
r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
-
-
-
r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
-
-
-
ir
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
Q9Y1N2
enzyme catalyzes acetate formation and ATP generation during fermentation of pyruvate to acetate
-
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
Q9Y1N2
enzyme catalyzes acetate formation and ATP generation during fermentation of pyruvate to acetate
-
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
Q9Y8L0, Q9Y8L1
major energy-conserving reaction during pyruvate and sugar conversion to acetate, catalyzing acetate formation and ATP synthesis
-
r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
-
downregulation of the enzyme is observed during periods of acetate consumption
-
-
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
-
Archaeoglobus fulgidus strain 7324 converts starch to acetate via a modified Embden-Meyerhof pathway and acetyl-CoA synthetase (ADP-forming)
-
-
?
ADP + phosphate + acetyl-CoA
?
show the reaction diagram
-
-
-
-
-
ADP + phosphate + acetyl-CoA
?
show the reaction diagram
-
-
-
-
-
ADP + phosphate + acetyl-CoA
?
show the reaction diagram
-
enzyme catalyzes acetate formation and ATP generation during fermentation of pyruvate to acetate
-
-
-
ADP + phosphate + acetyl-CoA
?
show the reaction diagram
-
enzyme catalyzes acetate formation and ATP generation during fermentation of pyruvate to acetate, energy-conserving pyruvate-to-acetate pathway
-
-
-
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
Giardia intestinalis WB
Q9Y1N2
enzyme catalyzes acetate formation and ATP generation during fermentation of pyruvate to acetate
-
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
-
-
-
-
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
-
-
-
-
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
E7FI45 and E7FHP1
-
-
-
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
-
the enzyme is required for growth on ethanol. ACS activity is induced upon growth on ethanol, 2,3-butanediol, malonate and acetate
-
-
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
E7FI45 and E7FHP1
the enzyme catalyzes the formation of acetate from acetyl-CoA and concomitant ATP synthesis by the mechanism of substrate level phosphorylation
-
-
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
-
-
-
-
r
additional information
?
-
-
ACS1, encoded by the gene facA, is induced by acetate and repressed by glucose at the transcriptional level, ACS2 may be a stress protein, expressed under carbon source starvation
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ADP
E7FI45 and E7FHP1
-
ATP
E7FI45 and E7FHP1
-
NADH
-
oxidation to NAD+ by assay system lactate dehydrogenase and pyruvate kinase
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
can replace Mg2+ in activition, with 15% of the efficiency
Ca2+
-
no effect
Ca2+
-
activates, 45% of the efficiency of Mg2+ and Mn2+
Co2+
-
44% of the activation relative to Mg2+; can replace Mg2+ in activation
Co2+
-
activates, 90% of the efficiency of Mg2+ and Mn2+
Mg2+
-
Km: 0.59; required
Mg2+
-
an Mg2+/ATP ratio of up to 10 is required for optimal activity, suggesting that Mg2+ not only complexes ADP but has an additional stimulating effect on enzyme function; Km: 0.2 mM; required
Mg2+
-
required, 30 mM for maximal catalytic activity
Mg2+
-
optimal MgCl2 concentration: 30 mM in absence of KCl, 20 mM in presence of 3 M KCl
Mg2+
-
activates
Mg2+
E7FI45 and E7FHP1
required
Mg2+
-
dependent on Mg2+, showing the highest activity at about 5 mM
Mn2+
-
can replace Mg2+ in activation
Mn2+
-
68% of the activation relative to Mg2+; can replace Mg2+ in activation
Mn2+
-
activates
additional information
-
contains neither iron nor other metals, such as copper, zinc, or magnesium
additional information
Q9Y1N2
requirement for a divalent cation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Isobutyrate
-
10 mM, complete inhibition
NaCl
-
2-3 M, 40% loss of activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.5
acetate
-
-
0.6
acetate
-
30C, isoenzyme ACS1
0.625
acetate
E7FI45 and E7FHP1
pH 6.5, 55C, recombinant wild-type enzyme; pH 6.5, 55C, wild-type enzyme
0.66
acetate
-
-
0.783
acetate
E7FI45 and E7FHP1
pH 6.5, 55C, mutant enzyme H257Dalpha
0.794
acetate
E7FI45 and E7FHP1
pH 6.5, 55C, mutant enzyme E217Dalpha
0.8
acetate
Q9Y8L0, Q9Y8L1
-
0.9
acetate
-
in 100 mM HEPES-KOH pH 7.5, 0.1 mM 5,5'-dithiobis(2-nitrobenzoic acid), 5 mM MgCl2, at 55C
1.02
acetate
-
pH 8.0, 37C, isoenzyme ACS2
1.1
acetate
-
isoenzyme ACS I
1.1
acetate
-
pH 7.5, 37C
5.3
acetate
-
pH 9.0, at 37C, oxic conditions
0.0039
acetyl-CoA
E7FI45 and E7FHP1
pH 6.5, 55C, wild-type enzyme
0.0062
acetyl-CoA
E7FI45 and E7FHP1
pH 6.5, 55C, mutant enzyme H257Dalpha
0.014
acetyl-CoA
E7FI45 and E7FHP1
pH 6.5, 55C, recombinant wild-type enzyme
0.017
acetyl-CoA
-
-
0.019
acetyl-CoA
Q9Y8L0, Q9Y8L1
-
0.023
acetyl-CoA
-
50C, pH not specified in the publication
0.025
acetyl-CoA
-
isoenzyme ACS I
0.026
acetyl-CoA
-
isoenzyme ACS II
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 55C
0.06
acetyl-CoA
Q9Y1N2
-
0.06
acetyl-CoA
Q9Y1N2
pH 7.5, at 30C
0.082
acetyl-CoA
E7FI45 and E7FHP1
pH 6.5, 55C, mutant enzyme E217Dalpha
0.12
acetyl-CoA
-
pH 6.5, 85C
0.45
acetyl-CoA
-
pH 7.5, 37C
0.015
ADP
-
50C, pH not specified in the publication
0.046
ADP
-
pH 7.5, 37C
0.05
ADP
-
-
0.061
ADP
-
isoenzyme ACS II
0.0741
ADP
E7FI45 and E7FHP1
pH 6.5, 55C, mutant enzyme H257Dalpha
0.08
ADP
-
-
0.091
ADP
-
in 100 mM HEPES-KOH pH 7.5, 0.1 mM 5,5'-dithiobis(2-nitrobenzoic acid), 5 mM MgCl2, at 55C
0.094
ADP
E7FI45 and E7FHP1
pH 6.5, 55C, wild-type enzyme
0.15
ADP
-
isoenzyme ACS I
0.2
ADP
Q9Y1N2
-
0.2
ADP
Q9Y1N2
pH 7.5, at 30C
0.23
ADP
-
-
0.283
ADP
E7FI45 and E7FHP1
pH 6.5, 55C, mutant enzyme E217Dalpha
0.07
ATP
-
-
0.09
ATP
Q9Y8L0, Q9Y8L1
-
0.221
ATP
E7FI45 and E7FHP1
pH 6.5, 55C, recombinant wild-type enzyme; pH 6.5, 55C, wild-type enzyme
0.3
ATP
-
pH 7.5, 37C
0.388
ATP
E7FI45 and E7FHP1
pH 6.5, 55C, mutant enzyme H257Dalpha
0.473
ATP
E7FI45 and E7FHP1
pH 6.5, 55C, 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 55C
1
ATP
-
pH 9.0, at 37C, oxic conditions
0.0139
CoA
E7FI45 and E7FHP1
pH 6.5, 55C, wild-type enzyme
0.018
CoA
-
isoenzyme ACS I
0.02
CoA
-
-
0.02
CoA
-
acetyl-CoA
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 55C
0.03
CoA
-
-
0.041
CoA
E7FI45 and E7FHP1
pH 6.5, 55C, mutant enzyme E217Dalpha
0.0771
CoA
E7FI45 and E7FHP1
pH 6.5, 55C, mutant enzyme H257Dalpha
0.08
CoA
-
pH 7.5, 37C
0.41
CoA
-
pH 9.0, at 37C, oxic conditions
1.09
dADP
-
-
0.132
GDP
-
isoenzyme ACS I
0.236
GDP
-
isoenzyme ACS II
0.43
GTP
-
isoenzyme ACS I
0.457
Isobutyrate
-
isoenzyme ACS I
0.012
isobutyryl-CoA
-
isoenzyme ACS II
0.029
isobutyryl-CoA
-
isoenzyme ACS I
0.004
phenylacetyl-CoA
-
isoenzyme ACS II
0.11
phenylacetyl-CoA
-
pH 6.5, 85C
0.1
phosphate
Q9Y8L0, Q9Y8L1
-
0.2
phosphate
-
-
0.272
phosphate
E7FI45 and E7FHP1
pH 6.5, 55C, recombinant wild-type enzyme; pH 6.5, 55C, wild-type enzyme
0.3
phosphate
-
50C, pH not specified in the publication
0.396
phosphate
-
isoenzyme ACS I
0.58
phosphate
-
isoenzyme ACS II
0.6
phosphate
-
-
0.714
phosphate
E7FI45 and E7FHP1
pH 6.5, 55C, mutant enzyme E217Dalpha
0.919
phosphate
E7FI45 and E7FHP1
pH 6.5, 55C, mutant enzyme H257Dalpha
1
phosphate
-
in 100 mM HEPES-KOH pH 7.5, 0.1 mM 5,5'-dithiobis(2-nitrobenzoic acid), 5 mM MgCl2, at 55C
1.35
phosphate
Q9Y1N2
-
1.35
phosphate
Q9Y1N2
pH 7.5, at 30C
1.59
phosphate
-
-
2
phosphate
-
pH 7.5, 37C
5.2
Propionate
-
pH 8.0, 37C, isoenzyme ACS2
8.55
Propionate
-
30C, isoenzyme ACS1
0.04
isobutyryl-CoA
-
pH 6.5, 85C
additional information
additional information
E7FI45 and E7FHP1
kinetics of wild-type and mutant enzymes
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
67
acetate
-
isoenzyme ACS II
42
acetyl-CoA
-
isoenzyme ACS II
157
acetyl-CoA
-
isoenzyme ACS I
115
ADP
-
isoenzyme ACS II
203
ADP
-
isoenzyme ACS I
68
ATP
-
isoenzyme ACS II
82
ATP
-
isoenzyme ACS I
65
CoA
-
isoenzyme ACS I
70
CoA
-
isoenzyme ACS II
73
CoA
-
isoenzyme ACS I
21
GDP
-
isoenzyme ACS II
411
GDP
-
isoenzyme ACS I
27
GTP
-
isoenzyme ACS II
66
indoleacetate
-
isoenzyme ACS II
22
Isobutyrate
-
isoenzyme ACS II
55
Isobutyrate
-
isoenzyme ACS I
8
isobutyryl-CoA
-
isoenzyme ACS II
121
isobutyryl-CoA
-
GTP, isoenzyme ACS I
89
phenylacetate
-
isoenzyme ACS II
138
phenylacetyl-CoA
-
isoenzyme ACS II
117
phosphate
-
isoenzyme ACS II
182
phosphate
-
isoenzyme ACS I
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.03
-
pH 9.0, at 37C, oxic conditions, during stationary phase on glucose
0.03
-
50C, pH not specified in the publication, enzyme from starch-grown cells
0.04
-
pH 9.0, at 37C, oxic conditions, during exponential growth phase on glucose
0.1
-
pH 9.0, at 37C, oxic conditions, during exponential growth phase on glucose
0.3
-
50C, pH not specified in the publication, enzyme from lactate-grown cells
0.45
-
pH 9.0, at 37C, oxic conditions, purified enzyme
30
-
isoenzyme ACS II
64.6
-
isoenzyme ACS I
additional information
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
E7FI45 and E7FHP1
assay at; assay at, both reaction directions
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 7.5
-
pH 5.5: about 40% of maximal activity, pH 7.5: about 20% of maximal activity
6 - 11
-
6: about 60% of maximal activity, 11: about 40% of maximal activity, isoenzyme ACS I
6 - 8
-
about 50% of maximal activity at pH 6 and 8
6.5 - 8.5
-
pH 6.5: about 60% of maximal activity, pH 8.5: about 60% of maximal activity
7 - 11
-
7: about 60% of maximal activity, 11: about 65% of maximal activity, isoenzyme ACS II
7.3 - 7.8
-
the pH optimum is at pH 7.5, with remaining activities of about 40% at pH 7.3 and 59% at pH 7.8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 30
-
isoenzyme ACS1
50
-
isoenzyme ACS2
55
E7FI45 and E7FHP1
assay at; assay at, both reaction directions
80
E7FI45 and E7FHP1
assay at, catalytic arsenolysis of acetyl-CoA
87
Q9Y8L0, Q9Y8L1
-
90
-
above, at pH 8.0
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 40
-
20C: about 75% of maximal activity, 40C: about 45% of maximal activity, isoenzyme ACS1
25 - 55
-
25C: about 45% of maximal activity, 55C: about 40% of maximal activity, isoenzyme ACS2
25
-
isoenzymes ACS I and ACS II are inactive at
30 - 50
-
30C: about 50% of maximal activity, 50C: about 80% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.2
Q9Y1N2
estimation from sequence of cDNA
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
specific activity is 10fold higher in starch-grown cells than in lactate-grown cells
Manually annotated by BRENDA team
Archaeoglobus fulgidus 7324
-
specific activity is 10fold higher in starch-grown cells than in lactate-grown cells
-
Manually annotated by BRENDA team
-
specific activity is 10fold higher in starch-grown cells than in lactate-grown cells
Manually annotated by BRENDA team
Archaeoglobus fulgidus 7324
-
specific activity is 10fold higher in starch-grown cells than in lactate-grown cells
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Q9Y8L0, Q9Y8L1
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
78000
Q9Y1N2
estimation from sequence of cDNA
651402
140000
-
gel filtration
626
145000
-
gel filtration
625
145000
Q9Y8L0, Q9Y8L1
gel filtration
651644
150000 - 165000
-
native PAGE
625
150000
E7FI45 and E7FHP1
gel filtration
693061
166000
-
gel filtration
660834
300000
-
native enzyme, gel filtration
727557
317000
-
recombinant enzyme, gel filtration
727557
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 70000, isoenzyme ACS1, SDS-PAGE, x * 77000, isoenzyme ACS2, SDS-PAGE
dimer
-
2 * 87000, SDS-PAGE
heterotetramer
Q9Y8L0, Q9Y8L1
alpha2,beta2, 2 * 47000 (alpha) + 2 * 25000 (beta), SDS-PAGE
heterotetramer
E7FI45 and E7FHP1
2 * 49965 (alpha) + 2 * 25878 (beta), calculated from sequence
homotetramer
-
4 * 75000, native enzyme, SDS-PAGE, 4 * 77000, recombinant enzyme, SDS-PAGE
homotetramer
-
4 * 75000, native enzyme, SDS-PAGE, 4 * 77000, recombinant enzyme, SDS-PAGE
-
tetramer
-
2 * 47000 (alpha) + 2 * 25000 (beta), SDS-PAGE
tetramer
-
2 * 45000 (alpha) + 2 * 23000 (beta), SDS-PAGE
tetramer
E7FI45 and E7FHP1
2 * 47000, alpha-subunit, + 2 * 27000, beta-subunit, SDS-PAGE
monomer
Giardia intestinalis WB
-
-
-
additional information
E7FI45 and E7FHP1
a heterotetrameric ACD with alpha2beta structure, structural model, ACD shows a spatial arrangement of the subunits different from Escherichia coli succinyl-CoA synthetase, SCS, but maintaining a similar catalytic site, structural consequences of the domain shuffling in ACD, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
E7FI45 and E7FHP1
His257alpha and His71beta are sites of transient phosphorylation
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, sitting-drop vapour-diffusion method, crystals belong to monoclinic space group C2, with unit-cell parameters a = 131.3, b = 186.1, c = 121.5, beta = 122.6, and diffract at 2.0 A resolution
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
-
t1/2: 18 h for isoenzyme ACS I, 8 h for isoenzyme ACS II
626
80
-
120 min, no significant loss of activity
660834
90
-
half-life: 105 min
660834
100
-
half-life is 60 min, in presence of 1 M KCl no loss of activity after 2 h
625
100
-
half-life: 13 min. Completely stable for 120 min in presence of 1 M (NH4)2SO4
660834
110
-
half-life is 30 min
625
additional information
Q9Y8L0, Q9Y8L1
80-110C, no lose activity upon incubation for 3h at 90C, lose about 60% after 2h at 100C
651644
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
requires high salt concentrations for long-term stability
-
stability for more than 48 requires high salt concentrations, i.e., 1-2 M of KCl or NaCl
-
salts stabilize against heat inactivation. In presence of 1 M KCl the enzyme does not lose activity after 2 h incubation
-
sensitivity towards heat inactivation is increased with storage at -20C
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
stable to oxygen for 24 h
-
626
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 1-2 mg/ml enzyme, in 20 mM Tris/HCl, pH 8.0, 2 mM MgCl2, 150 mM NaCl, stable for several weeks
-
on ice stable for 2 d
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA affinity chromatography, phenyl Sepharose column chromatography, Q-Sepharose column chromatography, and Superdex 200 gel filtration
-
ion-exchange chromatography
Q9Y1N2
gel filtration on a Superdex TM200 column
-
partial, isoenzyme ACS1; partial, isoenzyme ACS2
-
about 10fold, 15 min at 80C and subsequent anion-exchange chromatography
Q9Y8L0, Q9Y8L1
isoenzymes ACS I and ACS II
-
recombinant wild-type and mutant enzyme subunits from Escherichia coli strain BL21(DE3) by heat precipitation at 90C for 30 min, followed by reconstitution of holoenzyme through hydrophobic interaction chromatography ultrafiltration, and gel filtration, the chromatographic steps are then repeated; wild-type end mutant enzymes
E7FI45 and E7FHP1
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
acdIa and acdIb genes encoding alpha- and beta-subunit of ACD, expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
E7FI45 and E7FHP1
overexpression in Escherichia coli
Q9Y8L0, Q9Y8L1
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is induced 10fold during growth on D-glucose
-
the enzyme is induced 10fold during growth on D-glucose
-
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D212betaE
E7FI45 and E7FHP1
site-directed mutagenesis, comparison of the wild-type CD spectrum with the mutant CD spectrum, structure and reaction kinetics, overview. The mutant shows 2-4% of the wild-type activity, phosphorylation of the mutant is reduced
E218alphaD
E7FI45 and E7FHP1
site-directed mutagenesis, comparison of the wild-type CD spectrum with the mutant CD spectrum, structure and reaction kinetics, overview. The mutant shows 1-10% of the wild-type activity, phopshorylation of the mutant is reduced
E218alphaQ
E7FI45 and E7FHP1
site-directed mutagenesis, comparison of the wild-type CD spectrum with the mutant CD spectrum, structure and reaction kinetics, overview. Inactive mutant, phopshorylation of the mutant is reduced
E218Dalpha
E7FI45 and E7FHP1
1-10% of wild-type activity
H257alphaD
E7FI45 and E7FHP1
site-directed mutagenesis, comparison of the wild-type CD spectrum with the mutant CD spectrum, structure and reaction kinetics, overview. Inactive mutant, which is not phosphorylated at both the alpha- and beta-subunit
H257Dalpha
E7FI45 and E7FHP1
mutant shows no activity in either direction
H71betaA
E7FI45 and E7FHP1
site-directed mutagenesis, comparison of the wild-type CD spectrum with the mutant CD spectrum, structure and reaction kinetics, overview. Inactive mutant, which is impaired in phosphorylation of the beta subunit
G266S
-
the Acs mutant does not cause growth arrest in contrast to the wild-type enzyme
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
equal amounts of Escherichia coli extracts containing alpha and beta subunits separately expressed mixed and incubated on ice; equal amounts of Escherichia coli extracts containing alpha and beta subunits separately expressed, mixed and incubated on ice
Q9Y8L0, Q9Y8L1