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EC Tree
The taxonomic range for the selected organisms is: Pyrococcus furiosus The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
acs iii, acetyl-coa synthetase (adp-forming), adp-acs, acetate:coa ligase [adp-forming], tk0944/tk0943 protein,
more
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Acetyl-CoA synthetase
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Acetyl-CoA synthetase (ADP-forming)
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acetyl-coenzyme A synthetase (ADP-forming)
Q9Y8L1
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ADP-forming acetyl-CoA synthetase
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PF1540
gene name alpha subunit
PF1787
gene name, beta-subunit
Synthetase, acetyl coenzyme A (adenosine diphosphate-forming)
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ATP + acetate + CoA = ADP + phosphate + acetyl-CoA
ATP + acetate + CoA = ADP + phosphate + acetyl-CoA
reaction mechanism and structural modelling, formation of enzyme-bound acetyl phosphate and enzyme phosphorylation at His257alpha, overview
ATP + acetate + CoA = ADP + phosphate + acetyl-CoA
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
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Acid-thiol ligation
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acetate:CoA ligase (ADP-forming)
Also acts on propanoate and, very slowly, on butanoate.
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ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
Q9Y8L0, Q9Y8L1
major energy-conserving reaction during pyruvate and sugar conversion to acetate, catalyzing acetate formation and ATP synthesis
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r
ADP + phosphate + acetyl-CoA
?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
ADP + phosphate + butyryl-CoA
ATP + butyrate + CoA
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92% of the activity relative to acetyl-CoA
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?
ADP + phosphate + indoleacetyl-CoA
ATP + indoleacetate + CoA
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r, isoenzyme ACS II is active, ACS I not
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-
?
ADP + phosphate + phenylacetyl-CoA
ATP + phenylacetate + CoA
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r, isoenzyme ACS II is active, ACS I not
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-
?
ADP + phosphate + propionyl-CoA
ATP + propionate + CoA
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
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no activity with isoenzymes ACS I and ACS II
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-
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
ATP + isobutyrate + CoA
ADP + phosphate + isobutyryl-CoA
ATP + isopentanioate + CoA
ADP + phosphate + isovaleryl-CoA
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34% of the activity relative to acetate
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-
?
ATP + pentanoate + CoA
ADP + phosphate + valeryl-CoA
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36% of the activity relative to acetate
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?
GDP + phosphate + acetyl-CoA
GTP + acetate + CoA
IDP + phosphate + acetyl-CoA
ITP + acetate + CoA
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r, 250% of the activity relative to ADP
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?
additional information
?
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ADP + phosphate + acetyl-CoA
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?
ADP + phosphate + acetyl-CoA
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enzyme catalyzes acetate formation and ATP generation during fermentation of pyruvate to acetate
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?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
Q9Y8L0, Q9Y8L1
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r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
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r
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?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
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r
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?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
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r
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?
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
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isoenzymes ACS I and ACS II
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?
ADP + phosphate + propionyl-CoA
ATP + propionate + CoA
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r
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?
ADP + phosphate + propionyl-CoA
ATP + propionate + CoA
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110% of the activity relative to acetyl-CoA
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?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
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?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
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?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
the enzyme catalyzes the formation of acetate from acetyl-CoA and concomitant ATP synthesis by the mechanism of substrate level phosphorylation
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r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
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
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r
ATP + isobutyrate + CoA
ADP + phosphate + isobutyryl-CoA
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r
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?
ATP + isobutyrate + CoA
ADP + phosphate + isobutyryl-CoA
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isoenzymes ACS I and ACS II
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-
?
ATP + isobutyrate + CoA
ADP + phosphate + isobutyryl-CoA
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79% of the activity relative to acetate
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?
GDP + phosphate + acetyl-CoA
GTP + acetate + CoA
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?
GDP + phosphate + acetyl-CoA
GTP + acetate + CoA
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r, 220% of the activity relative to ADP
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?
additional information
?
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the enzyme performs catalytic arsenolysis of acetyl-CoA
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?
additional information
?
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the enzyme performs catalytic arsenolysis of acetyl-CoA
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?
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ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
Q9Y8L0, Q9Y8L1
major energy-conserving reaction during pyruvate and sugar conversion to acetate, catalyzing acetate formation and ATP synthesis
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r
ADP + phosphate + acetyl-CoA
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
ADP + phosphate + acetyl-CoA
?
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?
ADP + phosphate + acetyl-CoA
?
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enzyme catalyzes acetate formation and ATP generation during fermentation of pyruvate to acetate
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?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
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?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
the enzyme catalyzes the formation of acetate from acetyl-CoA and concomitant ATP synthesis by the mechanism of substrate level phosphorylation
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r
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additional information
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contains neither iron nor other metals, such as copper, zinc, or magnesium
Co2+
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can replace Mg2+ in activation
Co2+
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44% of the activation relative to Mg2+
Mg2+
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required
Mg2+
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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
Mn2+
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can replace Mg2+ in activation
Mn2+
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68% of the activation relative to Mg2+
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0.8
acetate
Q9Y8L0, Q9Y8L1
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0.019
acetyl-CoA
Q9Y8L0, Q9Y8L1
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0.021
CoA
Q9Y8L0, Q9Y8L1
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0.1
phosphate
Q9Y8L0, Q9Y8L1
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0.0039 - 0.082
acetyl-CoA
0.43
GTP
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isoenzyme ACS I
0.457
Isobutyrate
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isoenzyme ACS I
0.012 - 0.029
isobutyryl-CoA
0.004
phenylacetyl-CoA
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isoenzyme ACS II
additional information
additional information
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0.5
acetate
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0.625
acetate
pH 6.5, 55°C, recombinant wild-type enzyme
0.625
acetate
pH 6.5, 55°C, wild-type enzyme
0.783
acetate
pH 6.5, 55°C, mutant enzyme H257Dalpha
0.794
acetate
pH 6.5, 55°C, mutant enzyme E217Dalpha
1.1
acetate
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isoenzyme ACS I
0.0039
acetyl-CoA
pH 6.5, 55°C, wild-type enzyme
0.0062
acetyl-CoA
pH 6.5, 55°C, mutant enzyme H257Dalpha
0.014
acetyl-CoA
pH 6.5, 55°C, recombinant wild-type enzyme
0.025
acetyl-CoA
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isoenzyme ACS I
0.026
acetyl-CoA
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isoenzyme ACS II
0.082
acetyl-CoA
pH 6.5, 55°C, mutant enzyme E217Dalpha
0.05
ADP
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0.061
ADP
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isoenzyme ACS II
0.0741
ADP
pH 6.5, 55°C, mutant enzyme H257Dalpha
0.094
ADP
pH 6.5, 55°C, wild-type enzyme
0.15
ADP
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isoenzyme ACS I
0.283
ADP
pH 6.5, 55°C, mutant enzyme E217Dalpha
0.07
ATP
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0.221
ATP
pH 6.5, 55°C, recombinant wild-type enzyme
0.221
ATP
pH 6.5, 55°C, wild-type enzyme
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
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isoenzyme ACS I
0.0139
CoA
pH 6.5, 55°C, wild-type enzyme
0.018
CoA
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isoenzyme ACS I
0.041
CoA
pH 6.5, 55°C, mutant enzyme E217Dalpha
0.0771
CoA
pH 6.5, 55°C, mutant enzyme H257Dalpha
0.132
GDP
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isoenzyme ACS I
0.236
GDP
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isoenzyme ACS II
0.012
isobutyryl-CoA
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isoenzyme ACS II
0.029
isobutyryl-CoA
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isoenzyme ACS I
0.2
phosphate
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0.272
phosphate
pH 6.5, 55°C, recombinant wild-type enzyme
0.272
phosphate
pH 6.5, 55°C, wild-type enzyme
0.396
phosphate
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isoenzyme ACS I
0.58
phosphate
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isoenzyme ACS II
0.714
phosphate
pH 6.5, 55°C, mutant enzyme E217Dalpha
0.919
phosphate
pH 6.5, 55°C, mutant enzyme H257Dalpha
additional information
additional information
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kinetics of wild-type and mutant enzymes
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additional information
additional information
kinetics of wild-type and mutant enzymes
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67
acetate
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isoenzyme ACS II
27
GTP
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isoenzyme ACS II
66
indoleacetate
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isoenzyme ACS II
89
phenylacetate
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isoenzyme ACS II
138
phenylacetyl-CoA
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isoenzyme ACS II
42
acetyl-CoA
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isoenzyme ACS II
157
acetyl-CoA
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isoenzyme ACS I
115
ADP
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isoenzyme ACS II
203
ADP
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isoenzyme ACS I
68
ATP
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isoenzyme ACS II
65
CoA
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isoenzyme ACS I
70
CoA
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isoenzyme ACS II
21
GDP
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isoenzyme ACS II
411
GDP
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isoenzyme ACS I
22
Isobutyrate
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isoenzyme ACS II
55
Isobutyrate
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isoenzyme ACS I
8
isobutyryl-CoA
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isoenzyme ACS II
121
isobutyryl-CoA
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GTP, isoenzyme ACS I
117
phosphate
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isoenzyme ACS II
182
phosphate
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isoenzyme ACS I
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additional information
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6.5
assay at
6.5
assay at, both reaction directions
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6 - 11
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6: about 60% of maximal activity, 11: about 40% of maximal activity, isoenzyme ACS I
6 - 8
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about 50% of maximal activity at pH 6 and 8
7 - 11
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7: about 60% of maximal activity, 11: about 65% of maximal activity, isoenzyme ACS II
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80
assay at, catalytic arsenolysis of acetyl-CoA
55
assay at
55
assay at, both reaction directions
90
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25
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isoenzymes ACS I and ACS II are inactive at
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Q9Y8L0, Q9Y8L1
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brenda
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brenda
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Q9Y8L0, Q9Y8L1
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brenda
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150000 - 165000
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native PAGE
23000
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2 * 45000 (alpha) + 2 * 23000 (beta), SDS-PAGE
25878
2 * 49965 (alpha) + 2 * 25878 (beta), calculated from sequence
27000
2 * 47000, alpha-subunit, + 2 * 27000, beta-subunit, SDS-PAGE
45000
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2 * 45000 (alpha) + 2 * 23000 (beta), SDS-PAGE
49965
2 * 49965 (alpha) + 2 * 25878 (beta), calculated from sequence
145000
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gel filtration
145000
Q9Y8L0, Q9Y8L1
gel filtration
25000
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2 * 47000 (alpha) + 2 * 25000 (beta), SDS-PAGE
25000
Q9Y8L0, Q9Y8L1
alpha2,beta2, 2 * 47000 (alpha) + 2 * 25000 (beta), SDS-PAGE
47000
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2 * 47000 (alpha) + 2 * 25000 (beta), SDS-PAGE
47000
Q9Y8L0, Q9Y8L1
alpha2,beta2, 2 * 47000 (alpha) + 2 * 25000 (beta), SDS-PAGE
47000
2 * 47000, alpha-subunit, + 2 * 27000, beta-subunit, SDS-PAGE
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heterotetramer
Q9Y8L0, Q9Y8L1
alpha2,beta2, 2 * 47000 (alpha) + 2 * 25000 (beta), SDS-PAGE
heterotetramer
2 * 49965 (alpha) + 2 * 25878 (beta), calculated from sequence
tetramer
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2 * 47000 (alpha) + 2 * 25000 (beta), SDS-PAGE
tetramer
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2 * 45000 (alpha) + 2 * 23000 (beta), SDS-PAGE
tetramer
2 * 47000, alpha-subunit, + 2 * 27000, beta-subunit, SDS-PAGE
additional information
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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
additional information
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
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phosphoprotein
His257alpha and His71beta are sites of transient phosphorylation
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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
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D212betaE
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
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
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
1-10% of wild-type activity
H257alphaD
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
mutant shows no activity in either direction
H71betaA
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
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100
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half-life is 60 min, in presence of 1 M KCl no loss of activity after 2 h
110
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half-life is 30 min
80
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t1/2: 18 h for isoenzyme ACS I, 8 h for isoenzyme ACS II
additional information
Q9Y8L0
80-110ºC, no lose activity upon incubation for 3h at 90ºC, lose about 60% after 2h at 100ºC
additional information
Q9Y8L1
80-110ºC, no lose activity upon incubation for 3h at 90ºC, lose about 60% after 2h at 100ºC
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salts stabilize against heat inactivation. In presence of 1 M KCl the enzyme does not lose activity after 2 h incubation
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sensitivity towards heat inactivation is increased with storage at -20°C
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stable to oxygen for 24 h
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626
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-20°C, 1-2 mg/ml enzyme, in 20 mM Tris/HCl, pH 8.0, 2 mM MgCl2, 150 mM NaCl, stable for several weeks
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about 10fold, 15 min at 80ºC and subsequent anion-exchange chromatography
Q9Y8L0, Q9Y8L1
isoenzymes ACS I and ACS II
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recombinant wild-type and mutant enzyme subunits from Escherichia coli strain BL21(DE3) by heat precipitation at 90°C 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
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overexpression in Escherichia coli
Q9Y8L0, Q9Y8L1
acdIa and acdIb genes encoding alpha- and beta-subunit of ACD, expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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equal amounts of Escherichia coli extracts containing alpha and beta subunits separately expressed mixed and incubated on ice
Q9Y8L0, Q9Y8L1
equal amounts of Escherichia coli extracts containing alpha and beta subunits separately expressed, mixed and incubated on ice
Q9Y8L0, Q9Y8L1
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Schfer, T.; Schnheit, P.
Pyruvate metabolism of the hyperthermophilic archaebaterium Pyrococcus furiosus. Acetate formation from acetyl-CoA and ATP synthesis are catalyzed by an acetyl-CoA synthetase (ADP forming)
Arch. Microbiol.
155
366-377
1991
Pyrococcus furiosus
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brenda
Glasemacher, J.; Bock, A.K.; Schmid, R.; Schnheit, P.
Purification and properties of acetyl-CoA synthetase (ADP-forming), an archaeal enzyme of acetate formation and ATP synthesis, from the hyperthermophile Pyrococcus furiosus
Eur. J. Biochem.
244
561-567
1997
Pyrococcus furiosus
brenda
Mai, X.; Adams, M.W.W.
Purification and characterization of two reversible and ADP-dependent acetyl coenzyme A synthetases from the hyperthermophilic archaeon Pyrococcus furiosus
J. Bacteriol.
178
5897-5903
1996
Pyrococcus furiosus
brenda
Musfeldt, M.; Selig, M.; Schonheit, P.
Acetyl coenzyme A synthetase (ADP forming) from the hyperthermophilic Archaeon pyrococcus furiosus: identification, cloning, separate expression of the encoding genes, acdAI and acdBI, in Escherichia coli, and in vitro reconstitution of the active heterotetrameric enzyme from its recombinant subunits
J. Bacteriol.
181
5885-5888
1999
Giardia intestinalis (Q9Y1N2), Pyrococcus furiosus (Q9Y8L0), Pyrococcus furiosus (Q9Y8L1)
brenda
Lehtioe, L.; Fabrichniy, I.; Hansen, T.; Schoenheit, P.; Goldman, A.
Unusual twinning in an acetyl coenzyme A synthetase (ADP-forming) from Pyrococcus furiosus
Acta Crystallogr. Sect. D
D61
350-354
2005
Pyrococcus furiosus
brenda
Braesen, C.; Schmidt, M.; Groetzinger, J.; Schoenheit, P.
Reaction mechanism and structural model of ADP-forming acetyl-CoA synthetase from the hyperthermophilic archaeon Pyrococcus furiosus: evidence for a second active site histidine residue
J. Biol. Chem.
283
15409-15418
2008
Pyrococcus furiosus, Pyrococcus furiosus (E7FI45 and E7FHP1)
brenda
Schfer, T.; Schnheit, P.
Maltose fermentation to acetate, CO2 and H2 in the anaerobic hyperthermophilic archaeon Pyrococcus furiosus evidence for the operation of a novel sugar fermentation pathway
Arch. Microbiol.
158
188-202
1992
Pyrococcus furiosus
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brenda