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ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
ADP + phosphate + butyryl-CoA
ATP + butyrate + CoA
ADP + phosphate + indole-3-acetyl-CoA
ATP + indole-3-acetate + CoA
-
-
-
r
ADP + phosphate + phenylacetyl-CoA
ATP + phenylacetate + CoA
-
-
-
r
ADP + phosphate + propionyl-CoA
ATP + propionate + CoA
-
-
-
r
ATP + 2-(4-hydroxyphenyl)acetate + CoA
ADP + phosphate + 2-(4-hydroxyphenyl)acetyl-CoA
the enzyme accommodates a broad range of acids that correspond to those generated in the oxidative metabolism of Ala, Val, Leu, Ile, Met, Phe, and Cys
-
-
?
ATP + 2-(indol-3-yl)acetate + CoA
ADP + phosphate + 2-(indol-3-yl)acetyl-CoA
low activity. Low activity. The enzyme accommodates a broad range of acids that correspond to those generated in the oxidative metabolism of Ala, Val, Leu, Ile, Met, Phe, and Cys
-
-
?
ATP + 2-methylbutyrate + CoA
ADP + phosphate + 2-methylbutyryl-CoA
the enzyme accommodates a broad range of acids that correspond to those generated in the oxidative metabolism of Ala, Val, Leu, Ile, Met, Phe, and Cys
-
-
?
ATP + 3-methylthiopropionate + CoA
ADP + phosphate + 3-methylthiopropionyl-CoA
the enzyme accommodates a broad range of acids that correspond to those generated in the oxidative metabolism of Ala, Val, Leu, Ile, Met, Phe, and Cys
-
-
?
ATP + 4-aminobutyrate + CoA
ADP + phosphate + 4-aminobutyryl-CoA
low activity. The enzyme accommodates a broad range of acids that correspond to those generated in the oxidative metabolism of Ala, Val, Leu, Ile, Met, Phe, and Cys
-
-
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
ATP + butyrate + CoA
ADP + phosphate + butyryl-CoA
ATP + fumarate + CoA
ADP + phosphate + fumaryl-CoA
ATP + glycolate + CoA
ADP + phosphate + glycolyl-CoA
low activity. The enzyme accommodates a broad range of acids that correspond to those generated in the oxidative metabolism of Ala, Val, Leu, Ile, Met, Phe, and Cys
-
-
?
ATP + indole-3-acetate + CoA
ADP + phosphate + indole-3-acetyl-CoA
ATP + isobutyrate + CoA
ADP + phosphate + isobutyryl-CoA
ATP + isovalerate + CoA
ADP + phosphate + isovaleryl-CoA
ATP + lactate + CoA
ADP + phosphate + lactoyl-CoA
low activity. The enzyme accommodates a broad range of acids that correspond to those generated in the oxidative metabolism of Ala, Val, Leu, Ile, Met, Phe, and Cys
-
-
?
ATP + phenylacetate + CoA
ADP + phosphate + phenylacetyl-CoA
ATP + propionate + CoA
ADP + phosphate + propionyl-CoA
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
activity is 9% compared to activity with acetate
-
-
?
ATP + thioglycolate + CoA
ADP + phosphate + thioglycolyl-CoA
the enzyme accommodates a broad range of acids that correspond to those generated in the oxidative metabolism of Ala, Val, Leu, Ile, Met, Phe, and Cys
-
-
?
GDP + phosphate + acetyl-CoA
GTP + acetate + CoA
-
-
-
r
GTP + acetate + CoA
GDP + phosphate + acetyl-CoA
GTP + indole-3-acetate + CoA
GDP + phosphate + indole-3-acetyl-CoA
ATP (100%) is effectively replaced by GTP (70%)
-
-
?
GTP + phenylacetate + CoA
GDP + phosphate + phenylacetyl-CoA
ATP (100%) is effectively replaced by GTP (70%)
-
-
?
ITP + acetate + CoA
IDP + phosphate + acetyl-CoA
ITP gives 15% of the activity with ATP
-
-
r
additional information
?
-
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
-
-
-
r
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
the enzyme is specific for acetyl-CoA (100%) and butyryl-CoA (120%) but does not take phenylacetyl-CoA (0%). A significant rate of the reverse reaction direction, i.e., the ATP- and CoA-dependent conversion of acetate or butyrate to the corresponding CoA esters, can not be demonstrated
-
-
ir
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
the enzyme is specific for acetyl-CoA (100%) and butyryl-CoA (120%) but does not take phenylacetyl-CoA (0%). A significant rate of the reverse reaction direction, i.e., the ATP- and CoA-dependent conversion of acetate or butyrate to the corresponding CoA esters, can not be demonstrated
-
-
ir
ADP + phosphate + butyryl-CoA
ATP + butyrate + CoA
the enzyme is specific for acetyl-CoA (100%) and butyryl-CoA (120%) but does not take phenylacetyl-CoA (0%)
-
-
?
ADP + phosphate + butyryl-CoA
ATP + butyrate + CoA
the enzyme is specific for acetyl-CoA (100%) and butyryl-CoA (120%) but does not take phenylacetyl-CoA (0%)
-
-
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
activity is 13% compared to activity with phenylacetate. At 1 mM acetyl-CoA, the enzyme activity is less than 2% of the rate obtained with phenylacetyl-CoA
-
-
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
GTP is as effective as ATP as a substrate
-
-
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
-
-
-
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
-
-
-
r
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
the enzyme accommodates a broad range of acids that correspond to those generated in the oxidative metabolism of Ala, Val, Leu, Ile, Met, Phe, and Cys
-
-
?
ATP + butyrate + CoA
ADP + phosphate + butyryl-CoA
activity is 36% compared to activity with phenylacetate
-
-
?
ATP + butyrate + CoA
ADP + phosphate + butyryl-CoA
activity is 84% compared to activity with acetate
-
-
r
ATP + fumarate + CoA
ADP + phosphate + fumaryl-CoA
activity is 10% compared to activity with acetate
-
-
?
ATP + fumarate + CoA
ADP + phosphate + fumaryl-CoA
activity is 29% compared to activity with phenylacetate
-
-
?
ATP + indole-3-acetate + CoA
ADP + phosphate + indole-3-acetyl-CoA
activity is 4% compared to activity with acetate
-
-
?
ATP + indole-3-acetate + CoA
ADP + phosphate + indole-3-acetyl-CoA
the enzyme shows the highest activity with the aryl acids, indoleacetate (100%) and phenylacetate (65%), as compared to acetate (10-13%)
-
-
r
ATP + isobutyrate + CoA
ADP + phosphate + isobutyryl-CoA
activity is 31% compared to activity with phenylacetate
-
-
?
ATP + isobutyrate + CoA
ADP + phosphate + isobutyryl-CoA
activity is 56% compared to activity with acetate
-
-
?
ATP + isobutyrate + CoA
ADP + phosphate + isobutyryl-CoA
the enzyme accommodates a broad range of acids that correspond to those generated in the oxidative metabolism of Ala, Val, Leu, Ile, Met, Phe, and Cys
-
-
?
ATP + isovalerate + CoA
ADP + phosphate + isovaleryl-CoA
activity is 10% compared to activity with acetate
-
-
?
ATP + isovalerate + CoA
ADP + phosphate + isovaleryl-CoA
activity is 18% compared to activity with phenylacetate
-
-
?
ATP + isovalerate + CoA
ADP + phosphate + isovaleryl-CoA
the enzyme accommodates a broad range of acids that correspond to those generated in the oxidative metabolism of Ala, Val, Leu, Ile, Met, Phe, and Cys
-
-
?
ATP + phenylacetate + CoA
ADP + phosphate + phenylacetyl-CoA
activity is 10% compared to activity with acetate
-
-
?
ATP + phenylacetate + CoA
ADP + phosphate + phenylacetyl-CoA
the enzyme shows the highest activity with the aryl acids, indoleacetate (100%) and phenylacetate (65%), as compared to acetate (10-13%). ATP (100%) is effectively replaced by GTP (70%)
-
-
r
ATP + phenylacetate + CoA
ADP + phosphate + phenylacetyl-CoA
the enzyme accommodates a broad range of acids that correspond to those generated in the oxidative metabolism of Ala, Val, Leu, Ile, Met, Phe, and Cys
-
-
?
ATP + propionate + CoA
ADP + phosphate + propionyl-CoA
activity is 42% compared to activity with phenylacetate
-
-
?
ATP + propionate + CoA
ADP + phosphate + propionyl-CoA
propionate is as effective as acetate as substrate
-
-
r
ATP + propionate + CoA
ADP + phosphate + propionyl-CoA
-
-
-
r
GTP + acetate + CoA
GDP + phosphate + acetyl-CoA
GTP is as effective as ATP as a substrate
-
-
r
GTP + acetate + CoA
GDP + phosphate + acetyl-CoA
-
-
-
r
GTP + acetate + CoA
GDP + phosphate + acetyl-CoA
GTP gives 57% of the activity with ATP
-
-
r
additional information
?
-
to transmit an activated phosphoryl moiety from the acetyl-CoA binding site (within the alpha subunit) to the NDP-binding site (within the beta subunit), a distance of 51 A has to be bridged, binding mode of the Ac moiety within acetyl-CoA, and binding mode of Ado nucleotides within site II located in the beta subunit
-
-
?
additional information
?
-
the enzyme can utilize both ADP/ATP and GDP/GTP in the respective directions of the reaction. Less than 4% of maximal activity is observed with isobutyrate, valerate, isovalerate, hexanoate, heptanoate, octanoate, succinate, or phenylacetate as the acyl substrate. Activity observed with ATP (representing 100% activity) is nearly double that with GTP (57%) and substantially higher than the activities observed with ITP (15%), CTP (4.1%), or UTP (1.6%), no activity is observed with TTP or diphosphate. Enzymatic activity in the acetate-forming direction is determined by measuring the release of CoA with a sulfhydryl group (CoASH) from acyl-CoA by using Ellman's thiol reagent (DTNB). Production of NTB2- by CoASH cleavage of DTNB is measured spectrophotometrically at 412 nm. Activity in the acetate-forming direction is confirmed using the hexokinase/glucose-6-phosphate dehydrogenase-coupled assay. This assay couples ATP formation to the reduction of NADP+ to NADPH, which is measured spectrophotometrically at 340 nm
-
-
?
additional information
?
-
-
the enzyme can utilize both ADP/ATP and GDP/GTP in the respective directions of the reaction. Less than 4% of maximal activity is observed with isobutyrate, valerate, isovalerate, hexanoate, heptanoate, octanoate, succinate, or phenylacetate as the acyl substrate. Activity observed with ATP (representing 100% activity) is nearly double that with GTP (57%) and substantially higher than the activities observed with ITP (15%), CTP (4.1%), or UTP (1.6%), no activity is observed with TTP or diphosphate. Enzymatic activity in the acetate-forming direction is determined by measuring the release of CoA with a sulfhydryl group (CoASH) from acyl-CoA by using Ellman's thiol reagent (DTNB). Production of NTB2- by CoASH cleavage of DTNB is measured spectrophotometrically at 412 nm. Activity in the acetate-forming direction is confirmed using the hexokinase/glucose-6-phosphate dehydrogenase-coupled assay. This assay couples ATP formation to the reduction of NADP+ to NADPH, which is measured spectrophotometrically at 340 nm
-
-
?
additional information
?
-
activity with 2-(imidazol-4-yl)acetate is less than 5% of the activity with acetate
-
-
?
additional information
?
-
-
activity with 2-(imidazol-4-yl)acetate is less than 5% of the activity with acetate
-
-
?
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Fe2+
enzyme activity requires divalent cations. Mg2+(100%), which is the most effective, can be partially replaced by Co2+ (51%), Mn2+ (38%), and to a lesser extent (less than 20%) by Fe2+, Zn2+, Ni2+, Ca2+, and Cu2+
additional information
the metal ion is coordinated by the side chain of Asp351alpha'
Ca2+
enzyme activity requires divalent cations. Mg2+(100%), which is the most effective, can be partially replaced by Co2+ (51%), Mn2+ (38%), and to a lesser extent (less than 20%) by Fe2+, Zn2+, Ni2+, Ca2+, and Cu2+
Ca2+
can slightly substitute for Mg2+
Co2+
enzyme activity requires divalent cations. Mg2+(100%), which is the most effective, can be partially replaced by Co2+ (51%), Mn2+ (38%), and to a lesser extent (less than 20%) by Fe2+, Zn2+, Ni2+, Ca2+, and Cu2+
Co2+
can partially substitute for Mg2+
Cu2+
activity depends on divalent cations. Mg2+which is most effective, could partially be replaced by Mn2+, Zn2+, and Cu2+ (each 30 to 40%)
Cu2+
enzyme activity requires divalent cations. Mg2+(100%), which is the most effective, can be partially replaced by Co2+ (51%), Mn2+ (38%), and to a lesser extent (less than 20%) by Fe2+, Zn2+, Ni2+, Ca2+, and Cu2+
Cu2+
can slightly substitute for Mg2+
Mg2+
activity depends on divalent cations. Mg2+which is most effective, could partially be replaced by Mn2+, Zn2+, and Cu2+ (each 30 to 40%)
Mg2+
enzyme activity requires divalent cations. Mg2+(100%), which is the most effective, can be partially replaced by Co2+ (51%), Mn2+ (38%), and to a lesser extent (less than 20%) by Fe2+, Zn2+, Ni2+, Ca2+, and Cu2+
Mg2+
required for activity, best divalent cation
Mn2+
activity depends on divalent cations. Mg2+which is most effective, could partially be replaced by Mn2+, Zn2+, and Cu2+ (each 30 to 40%)
Mn2+
enzyme activity requires divalent cations. Mg2+(100%), which is the most effective, can be partially replaced by Co2+ (51%), Mn2+ (38%), and to a lesser extent (less than 20%) by Fe2+, Zn2+, Ni2+, Ca2+, and Cu2+
Mn2+
can substitute for Mg2+
Ni2+
enzyme activity requires divalent cations. Mg2+(100%), which is the most effective, can be partially replaced by Co2+ (51%), Mn2+ (38%), and to a lesser extent (less than 20%) by Fe2+, Zn2+, Ni2+, Ca2+, and Cu2+
Ni2+
can slightly substitute for Mg2+
Zn2+
activity depends on divalent cations. Mg2+which is most effective, could partially be replaced by Mn2+, Zn2+, and Cu2+ (each 30 to 40%)
Zn2+
can slightly substitute for Mg2+
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1.9
GDP
pH 7.3, 37°C, acetate-forming direction, with acetyl-CoA
10
GTP
pH 7.3, 37°C, acetyl-CoA-forming direction, with acetate
1.24
indole-3-acetate
pH 8.0, 55°C
0.017
phenylacetyl-CoA
pH 8.0, 55°C
29
propionate
pH 7.3, 37°C, propionyl-CoA-forming direction, with propionate
0.032
propionyl-CoA
pH 7.3, 37°C, propionate-forming direction, with propionyl-CoA
additional information
acetate
0.34
acetate
pH 8.0, 55°C
2.58
acetate
pH 8.0, 55°C
14
acetate
pH 7.3, 37°C, acetyl-CoA-forming direction
0.01
acetyl-CoA
pH 8.0, 55°C
0.037
acetyl-CoA
pH 8.0, 55°C
0.04
acetyl-CoA
pH 7.3, 37°C, acetate-forming direction
0.007
ADP
pH 8.0, 55°C
0.71
ADP
pH 7.3, 37°C, propionate-forming direction, with propionyl-CoA
1.6
ADP
pH 7.3, 37°C, acetate-forming direction, with acetyl-CoA
0.03
ATP
pH 8.0, 55°C
7.2
ATP
pH 7.3, 37°C, propionyl-CoA-forming direction, with propionate
12
ATP
pH 7.3, 37°C, acetyl-CoA-forming direction, with acetate
0.0056
CoA
pH 6.5, 55°C
0.2
CoA
pH 7.3, 37°C, acetyl-CoA-forming direction, with acetate
1.6
CoA
pH 7.3, 37°C, propionyl-CoA-forming direction, with propionate
0.11
phenylacetate
pH 8.0, 55°C
2.5
phenylacetate
pH 8.0, 55°C
0.11
phosphate
pH 8.0, 55°C
0.47
phosphate
pH 8.0, 55°C
1.5
phosphate
pH 7.3, 37°C, propionate-forming direction, with propionyl-CoA
1.8
phosphate
pH 7.3, 37°C, acetate-forming direction, with acetyl-CoA
additional information
acetate
pH 6.5, 55°C, kinetic constant according to Adair-Pauling kinetic model: 1.5 mM
additional information
acetate
-
pH 6.5, 55°C, kinetic constant according to Adair-Pauling kinetic model: 1.5 mM
additional information
Isobutyrate
pH 6.5, 55°C, kinetic constant according to Adair-Pauling kinetic model: 0.132 mMs
additional information
Isobutyrate
-
pH 6.5, 55°C, kinetic constant according to Adair-Pauling kinetic model: 0.132 mMs
additional information
additional information
Michaelis-Menten steady-state kinetic analysis, pseudo-first-order reaction kinetic determinations are performed in both directions of the reaction
-
additional information
additional information
-
Michaelis-Menten steady-state kinetic analysis, pseudo-first-order reaction kinetic determinations are performed in both directions of the reaction
-
additional information
phenylacetate
pH 6.5, 55°C, kinetic constant according to Adair-Pauling kinetic model: 0.329 mM
additional information
phenylacetate
-
pH 6.5, 55°C, kinetic constant according to Adair-Pauling kinetic model: 0.329 mM
additional information
thioglycolate
pH 6.5, 55°C, kinetic constant according to Adair-Pauling kinetic model: 0.322 mM
additional information
thioglycolate
-
pH 6.5, 55°C, kinetic constant according to Adair-Pauling kinetic model: 0.322 mM
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170
GDP
pH 7.3, 37°C, acetate-forming direction, with acetyl-CoA
180
GTP
pH 7.3, 37°C, acetyl-CoA-forming direction, with acetate
3.45
indole-3-acetate
pH 8.0, 55°C
2.3
phenylacetyl-CoA
pH 8.0, 55°C
190
propionate
pH 7.3, 37°C, propionyl-CoA-forming direction, with propionate
21
propionyl-CoA
pH 7.3, 37°C, acetate-forming direction, with propionyl-CoA
additional information
acetate
1.84
acetate
pH 8.0, 55°C
138
acetate
pH 8.0, 55°C
240
acetate
pH 7.3, 37°C, acetyl-CoA-forming direction
95
acetyl-CoA
pH 8.0, 55°C
110
acetyl-CoA
pH 7.3, 37°C, acetate-forming direction
24
ADP
pH 7.3, 37°C, acetate-forming direction, with propionyl-CoA
140
ADP
pH 7.3, 37°C, acetate-forming direction, with acetyl-CoA
3
ATP
pH 8.0, 55°C
240
ATP
pH 7.3, 37°C, propionyl-CoA-forming direction, with propionate
320
ATP
pH 7.3, 37°C, acetyl-CoA-forming direction, with acetate
2.9
CoA
pH 8.0, 55°C
220
CoA
pH 7.3, 37°C, acetyl-CoA-forming direction, with acetate
260
CoA
pH 7.3, 37°C, propionyl-CoA-forming direction, with propionate
3
phenylacetate
pH 8.0, 55°C
11.5
phenylacetate
pH 8.0, 55°C
18
phosphate
pH 7.3, 37°C, acetate-forming direction, with propionyl-CoA
58
phosphate
pH 8.0, 55°C
120
phosphate
pH 7.3, 37°C, acetate-forming direction, with acetyl-CoA
additional information
acetate
pH 6.5, 55°C, kinetic constant according to Adair-Pauling kinetic model: 49.3/s
additional information
acetate
-
pH 6.5, 55°C, kinetic constant according to Adair-Pauling kinetic model: 49.3/s
additional information
Isobutyrate
pH 6.5, 55°C, kinetic constant according to Adair-Pauling kinetic model: 50.9/s
additional information
Isobutyrate
-
pH 6.5, 55°C, kinetic constant according to Adair-Pauling kinetic model: 50.9/s
additional information
phenylacetate
pH 6.5, 55°C, kinetic constant according to Adair-Pauling kinetic model: 40.6/s
additional information
phenylacetate
-
pH 6.5, 55°C, kinetic constant according to Adair-Pauling kinetic model: 40.6/s
additional information
thioglycolate
pH 6.5, 55°C, kinetic constant according to Adair-Pauling kinetic model: 26.1/s
additional information
thioglycolate
-
pH 6.5, 55°C, kinetic constant according to Adair-Pauling kinetic model: 26.1/s
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90
GDP
pH 7.3, 37°C, acetate-forming direction, with acetyl-CoA
18
GTP
pH 7.3, 37°C, acetyl-CoA-forming direction, with acetate
2.7
indole-3-acetate
pH 8.0, 55°C
140
phenylacetyl-CoA
pH 8.0, 55°C
6.3
propionate
pH 7.3, 37°C, propionyl-CoA-forming direction, with propionate
650
propionyl-CoA
pH 7.3, 37°C, acetate-forming direction, with propionyl-CoA
additional information
acetate
0.7
acetate
pH 8.0, 55°C
16
acetate
pH 7.3, 37°C, acetyl-CoA-forming direction
400
acetate
pH 8.0, 55°C
2600
acetyl-CoA
pH 7.3, 37°C, acetate-forming direction
9200
acetyl-CoA
pH 8.0, 55°C
34
ADP
pH 7.3, 37°C, acetate-forming direction, with propionyl-CoA
89
ADP
pH 7.3, 37°C, acetate-forming direction, with acetyl-CoA
27
ATP
pH 7.3, 37°C, acetyl-CoA-forming direction, with acetate
33
ATP
pH 7.3, 37°C, propionyl-CoA-forming direction, with propionate
5.4
CoA
pH 8.0, 55°C
160
CoA
pH 7.3, 37°C, propionyl-CoA-forming direction, with propionate
1100
CoA
pH 7.3, 37°C, acetyl-CoA-forming direction, with acetate
1.2
phenylacetate
pH 8.0, 55°C
111
phenylacetate
pH 8.0, 55°C
12
phosphate
pH 7.3, 37°C, acetate-forming direction, with propionyl-CoA
65
phosphate
pH 7.3, 37°C, acetate-forming direction, with acetyl-CoA
520
phosphate
pH 8.0, 55°C
additional information
acetate
pH 6.5, 55°C, kinetic constant according to Adair-Pauling kinetic model: 32.8/s*mM
additional information
acetate
-
pH 6.5, 55°C, kinetic constant according to Adair-Pauling kinetic model: 32.8/s*mM
additional information
Isobutyrate
pH 6.5, 55°C, kinetic constant according to Adair-Pauling kinetic model: 385/s*mM
additional information
Isobutyrate
-
pH 6.5, 55°C, kinetic constant according to Adair-Pauling kinetic model: 385/s*mM
additional information
phenylacetate
pH 6.5, 55°C, kinetic constant according to Adair-Pauling kinetic model: 123/s*mM
additional information
phenylacetate
-
pH 6.5, 55°C, kinetic constant according to Adair-Pauling kinetic model: 123/s*mM
additional information
thioglycolate
pH 6.5, 55°C, kinetic constant according to Adair-Pauling kinetic model: 81.0/s*mM
additional information
thioglycolate
-
pH 6.5, 55°C, kinetic constant according to Adair-Pauling kinetic model: 81.0/s*mM
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Musfeldt, M.; Schonheit, P.
Novel type of ADP-forming acetyl coenzyme A synthetase in hyperthermophilic archaea: heterologous expression and characterization of isoenzymes from the sulfate reducer Archaeoglobus fulgidus and the methanogen Methanococcus jannaschii
J. Bacteriol.
184
636-644
2002
Archaeoglobus fulgidus (O28341), Archaeoglobus fulgidus (O29057), Archaeoglobus fulgidus, Methanocaldococcus jannaschii (Q58010), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q58010)
brenda
Awano, T.; Wilming, A.; Tomita, H.; Yokooji, Y.; Fukui, T.; Imanaka, T.; Atomi, H.
Characterization of two members among the five ADP-forming acyl coenzyme A (acyl-CoA) synthetases reveals the presence of a 2-(imidazol-4-yl)acetyl-CoA synthetase in Thermococcus kodakarensis
J. Bacteriol.
196
140-147
2014
Thermococcus kodakarensis (Q5JIA8 and Q5JIA9), Thermococcus kodakarensis
brenda
Weiße, R.H.; Faust, A.; Schmidt, M.; Schönheit, P.; Scheidig, A.J.
Structure of NDP-forming Acetyl-CoA synthetase ACD1 reveals a large rearrangement for phosphoryl transfer
Proc. Natl. Acad. Sci. USA
113
E519-E528
2016
Candidatus Korarchaeum cryptofilum (B1L3C9), Candidatus Korarchaeum cryptofilum OPF8 (B1L3C9)
brenda
Jones, C.P.; Ingram-Smith, C.
Biochemical and kinetic characterization of the recombinant ADP-forming acetyl coenzyme A synthetase from the amitochondriate protozoan Entamoeba histolytica
Eukaryot. Cell
13
1530-1537
2014
Entamoeba histolytica (Q9NAT4), Entamoeba histolytica
brenda
Weiße, R.H.-J. ; Faust, A.; Schmidt, M.; Schönheit, P.; Scheidig, A.J.
Structure of NDP-forming acetyl-CoA synthetase ACD1 reveals a large rearrangement for phosphoryl transfer
Proc. Natl. Acad. Sci. USA
113
E519-E528
2016
Candidatus Korarchaeum cryptofilum (B1L3C9)
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