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, Eukaryota, Bacteria

EC NUMBER
COMMENTARY
6.2.1.13
-
RECOMMENDED NAME
GeneOntology No.
Acetate-CoA ligase (ADP-forming)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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, -
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Acid-thiol ligation
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
acetate formation from acetyl-CoA II
-
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 ACCESSION NO.
COMMENTARY
LITERATURE
acetate:coenzyme A ligase (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
-
-
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
SEQUENCE CODE
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
SwissProt
Manually annotated by BRENDA team
subunit beta; isoenzyme ACS I
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
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
-, 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
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
-, Q9Y1N2
less efficiently than acetyl-CoA
-
?
ADP + phosphate + butanoyl-CoA
ATP + butanoate + CoA
show the reaction diagram
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 + 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
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
E7FI45 and E7FHP1, -
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 + butyrate + CoA
ADP + phosphate + butyryl-CoA
show the reaction diagram
-
at 98% of the activity with 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 + 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 + 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 + 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
-
-
?
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
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
-
-
-
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
-
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
-
-
-
-
?
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
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 ACCESSION NO.
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 ACCESSION NO.
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
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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Isobutyrate
-
10 mM, complete inhibition
NaCl
-
2-3 M, 40% loss of activity
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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
-
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
0.06
-
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
0.06
-
ADP
Q9Y8L0, Q9Y8L1
-
0.061
-
ADP
-
isoenzyme ACS II
0.0741
-
ADP
E7FI45 and E7FHP1, -
pH 6.5, 55C, mutant enzyme H257Dalpha
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
0.283
-
ADP
E7FI45 and E7FHP1, -
pH 6.5, 55C, mutant enzyme E217Dalpha
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
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
-
acetyl-CoA
0.021
-
CoA
Q9Y8L0, Q9Y8L1
-
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
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
1.35
-
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]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
-
E7FI45 and E7FHP1, -
assay at; assay at, both reaction directions
9
-
-
at 80C
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
30
-
isoenzyme ACS1
50
-
-
isoenzyme ACS2
50
-
-
assay at
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
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8.2
-
-, Q9Y1N2
estimation from sequence of cDNA
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Q9Y8L0, Q9Y8L1
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
78000
-
-, Q9Y1N2
estimation from sequence of cDNA
140000
-
-
gel filtration
145000
-
-
gel filtration
145000
-
Q9Y8L0, Q9Y8L1
gel filtration
150000
165000
-
native PAGE
150000
-
E7FI45 and E7FHP1, -
gel filtration
166000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
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
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 ACCESSION NO.
COMMENTARY
LITERATURE
phosphoprotein
E7FI45 and E7FHP1, -
His257alpha and His71beta are sites of transient phosphorylation
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
80
-
-
t1/2: 18 h for isoenzyme ACS I, 8 h for isoenzyme ACS II
80
-
-
120 min, no significant loss of activity
90
-
-
half-life: 105 min
100
-
-
half-life is 60 min, in presence of 1 M KCl no loss of activity after 2 h
100
-
-
half-life: 13 min. Completely stable for 120 min in presence of 1 M (NH4)2SO4
110
-
-
half-life is 30 min
additional information
-
Q9Y8L0, Q9Y8L1
80-110C, no lose activity upon incubation for 3h at 90C, lose about 60% after 2h at 100C
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
LITERATURE
stable to oxygen for 24 h
-
626
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
LITERATURE
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 ACCESSION NO.
LITERATURE
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
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
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