Cloned (Comment) | Organism |
---|---|
overexpressed in Escherichia coli | Archaeoglobus fulgidus |
overexpressed in Escherichia coli | Methanocaldococcus jannaschii |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.007 | - |
ADP | pH 8.0, 55°C | Archaeoglobus fulgidus | |
0.01 | - |
acetyl-CoA | pH 8.0, 55°C | Archaeoglobus fulgidus | |
0.015 | - |
ADP | pH 8.0, 55°C | Methanocaldococcus jannaschii | |
0.017 | - |
phenylacetyl-CoA | pH 8.0, 55°C | Archaeoglobus fulgidus | |
0.025 | - |
CoA | pH 8.0, 55°C | Archaeoglobus fulgidus | |
0.03 | - |
ATP | pH 8.0, 55°C | Archaeoglobus fulgidus | |
0.037 | - |
acetyl-CoA | pH 8.0, 55°C | Methanocaldococcus jannaschii | |
0.11 | - |
phosphate | pH 8.0, 55°C | Archaeoglobus fulgidus | |
0.11 | - |
phenylacetate | pH 8.0, 55°C | Archaeoglobus fulgidus | |
0.13 | - |
ATP | pH 8.0, 55°C | Archaeoglobus fulgidus | |
0.34 | - |
acetate | pH 8.0, 55°C | Archaeoglobus fulgidus | |
0.47 | - |
phosphate | pH 8.0, 55°C | Methanocaldococcus jannaschii | |
0.53 | - |
CoA | pH 8.0, 55°C | Archaeoglobus fulgidus | |
1.24 | - |
indole-3-acetate | pH 8.0, 55°C | Archaeoglobus fulgidus | |
2.5 | - |
phenylacetate | pH 8.0, 55°C | Archaeoglobus fulgidus | |
2.58 | - |
acetate | pH 8.0, 55°C | Archaeoglobus fulgidus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
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+ | Archaeoglobus fulgidus | |
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+ | Archaeoglobus fulgidus | |
Cu2+ | activity depends on divalent cations. Mg2+which is most effective, could partially be replaced by Mn2+, Zn2+, and Cu2+ (each 30 to 40%) | Archaeoglobus fulgidus | |
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+ | Archaeoglobus fulgidus | |
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+ | Archaeoglobus fulgidus | |
Mg2+ | activity depends on divalent cations. Mg2+which is most effective, could partially be replaced by Mn2+, Zn2+, and Cu2+ (each 30 to 40%) | Archaeoglobus fulgidus | |
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+ | Archaeoglobus fulgidus | |
Mn2+ | activity depends on divalent cations. Mg2+which is most effective, could partially be replaced by Mn2+, Zn2+, and Cu2+ (each 30 to 40%) | Archaeoglobus fulgidus | |
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+ | Archaeoglobus fulgidus | |
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+ | Archaeoglobus fulgidus | |
Zn2+ | activity depends on divalent cations. Mg2+which is most effective, could partially be replaced by Mn2+, Zn2+, and Cu2+ (each 30 to 40%) | Archaeoglobus fulgidus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
7000 | - |
2 * 7000, SDS-PAGE | Archaeoglobus fulgidus |
7400 | - |
2 * 7400, SDS-PAGE | Methanocaldococcus jannaschii |
72000 | - |
2 * 72000, SDS-PAGE | Archaeoglobus fulgidus |
78172 | - |
2 * 78172, calculated from sequence | Methanocaldococcus jannaschii |
140000 | - |
gel filtration | Archaeoglobus fulgidus |
160000 | - |
gel filtration | Methanocaldococcus jannaschii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Archaeoglobus fulgidus | O28341 | - |
- |
Archaeoglobus fulgidus | O29057 | - |
- |
Methanocaldococcus jannaschii | Q58010 | - |
- |
Methanocaldococcus jannaschii DSM 2661 | Q58010 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant enzyme | Archaeoglobus fulgidus |
recombinant enzyme | Methanocaldococcus jannaschii |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ADP + phosphate + acetyl-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 | Methanocaldococcus jannaschii | ATP + acetate + CoA | - |
ir | |
ADP + phosphate + acetyl-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 | Methanocaldococcus jannaschii DSM 2661 | ATP + acetate + CoA | - |
ir | |
ADP + phosphate + butyryl-CoA | the enzyme is specific for acetyl-CoA (100%) and butyryl-CoA (120%) but does not take phenylacetyl-CoA (0%) | Methanocaldococcus jannaschii | ATP + butyrate + CoA | - |
? | |
ADP + phosphate + butyryl-CoA | the enzyme is specific for acetyl-CoA (100%) and butyryl-CoA (120%) but does not take phenylacetyl-CoA (0%) | Methanocaldococcus jannaschii DSM 2661 | ATP + butyrate + CoA | - |
? | |
ADP + phosphate + indole-3-acetyl-CoA | - |
Archaeoglobus fulgidus | ATP + indole-3-acetate + CoA | - |
r | |
ADP + phosphate + phenylacetyl-CoA | - |
Archaeoglobus fulgidus | ATP + phenylacetate + CoA | - |
r | |
ATP + acetate + 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 | Archaeoglobus fulgidus | ADP + phosphate + acetyl-CoA | - |
? | |
ATP + acetate + CoA | GTP is as effective as ATP as a substrate | Archaeoglobus fulgidus | ADP + phosphate + acetyl-CoA | - |
r | |
ATP + butyrate + CoA | activity is 36% compared to activity with phenylacetate | Archaeoglobus fulgidus | ADP + phosphate + butyryl-CoA | - |
? | |
ATP + butyrate + CoA | activity is 84% compared to activity with acetate | Archaeoglobus fulgidus | ADP + phosphate + butyryl-CoA | - |
r | |
ATP + fumarate + CoA | activity is 10% compared to activity with acetate | Archaeoglobus fulgidus | ADP + phosphate + fumaryl-CoA | - |
? | |
ATP + fumarate + CoA | activity is 29% compared to activity with phenylacetate | Archaeoglobus fulgidus | ADP + phosphate + fumaryl-CoA | - |
? | |
ATP + indole-3-acetate + CoA | activity is 4% compared to activity with acetate | Archaeoglobus fulgidus | ADP + phosphate + indole-3-acetyl-CoA | - |
? | |
ATP + indole-3-acetate + CoA | the enzyme shows the highest activity with the aryl acids, indoleacetate (100%) and phenylacetate (65%), as compared to acetate (10-13%) | Archaeoglobus fulgidus | ADP + phosphate + indole-3-acetyl-CoA | - |
r | |
ATP + isobutyrate + CoA | activity is 31% compared to activity with phenylacetate | Archaeoglobus fulgidus | ADP + phosphate + isobutyryl-CoA | - |
? | |
ATP + isobutyrate + CoA | activity is 56% compared to activity with acetate | Archaeoglobus fulgidus | ADP + phosphate + isobutyryl-CoA | - |
? | |
ATP + isovalerate + CoA | activity is 10% compared to activity with acetate | Archaeoglobus fulgidus | ADP + phosphate + isovaleryl-CoA | - |
? | |
ATP + isovalerate + CoA | activity is 18% compared to activity with phenylacetate | Archaeoglobus fulgidus | ADP + phosphate + isovaleryl-CoA | - |
? | |
ATP + phenylacetate + CoA | activity is 10% compared to activity with acetate | Archaeoglobus fulgidus | ADP + phosphate + phenylacetyl-CoA | - |
? | |
ATP + phenylacetate + 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%) | Archaeoglobus fulgidus | ADP + phosphate + phenylacetyl-CoA | - |
r | |
ATP + propionate + CoA | activity is 42% compared to activity with phenylacetate | Archaeoglobus fulgidus | ADP + phosphate + propionyl-CoA | - |
? | |
ATP + propionate + CoA | propionate is as effective as acetate as substrate | Archaeoglobus fulgidus | ADP + phosphate + propionyl-CoA | - |
r | |
ATP + succinate + CoA | activity is 9% compared to activity with acetate | Archaeoglobus fulgidus | ADP + phosphate + succinyl-CoA | - |
? | |
GTP + acetate + CoA | GTP is as effective as ATP as a substrate | Archaeoglobus fulgidus | GDP + phosphate + acetyl-CoA | - |
r | |
GTP + indole-3-acetate + CoA | ATP (100%) is effectively replaced by GTP (70%) | Archaeoglobus fulgidus | GDP + phosphate + indole-3-acetyl-CoA | - |
? | |
GTP + phenylacetate + CoA | ATP (100%) is effectively replaced by GTP (70%) | Archaeoglobus fulgidus | GDP + phosphate + phenylacetyl-CoA | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodimer | 2 * 72000, SDS-PAGE | Archaeoglobus fulgidus |
homodimer | 2 * 7000, SDS-PAGE | Archaeoglobus fulgidus |
homodimer | 2 * 7400, SDS-PAGE | Methanocaldococcus jannaschii |
homodimer | 2 * 78172, calculated from sequence | Methanocaldococcus jannaschii |
Synonyms | Comment | Organism |
---|---|---|
acetyl CoA synthetase (ADP forming) | - |
Archaeoglobus fulgidus |
acetyl CoA synthetase (ADP forming) | - |
Methanocaldococcus jannaschii |
acetyl coenzyme A synthetase (ADP forming) | - |
Archaeoglobus fulgidus |
acetyl coenzyme A synthetase (ADP forming) | - |
Methanocaldococcus jannaschii |
ADP-forming acetyl coenzyme A synthetase | - |
Archaeoglobus fulgidus |
ADP-forming acetyl coenzyme A synthetase | - |
Methanocaldococcus jannaschii |
AF1211 | locus name | Archaeoglobus fulgidus |
AF1938 | locus name | Archaeoglobus fulgidus |
MJ0590 | locus name | Methanocaldococcus jannaschii |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
55 | - |
assay at | Methanocaldococcus jannaschii |
77 | - |
- |
Archaeoglobus fulgidus |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
60 | 80 | 60°C: about 55% of maximal activity, 80°C: 80% of maximal activity | Archaeoglobus fulgidus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
70 | - |
5 h, about 30% loss of activity | Archaeoglobus fulgidus |
80 | - |
150 min, about 65% loss of activity | Archaeoglobus fulgidus |
85 | - |
30 min, about 80% loss of activity. Almost complete loss of activity after 100 min | Archaeoglobus fulgidus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.84 | - |
acetate | pH 8.0, 55°C | Archaeoglobus fulgidus | |
2.3 | - |
phenylacetyl-CoA | pH 8.0, 55°C | Archaeoglobus fulgidus | |
2.9 | - |
CoA | pH 8.0, 55°C | Archaeoglobus fulgidus | |
3 | - |
ATP | pH 8.0, 55°C | Archaeoglobus fulgidus | |
3 | - |
phenylacetate | pH 8.0, 55°C | Archaeoglobus fulgidus | |
3.45 | - |
indole-3-acetate | pH 8.0, 55°C | Archaeoglobus fulgidus | |
11.5 | - |
phenylacetate | pH 8.0, 55°C | Archaeoglobus fulgidus | |
58 | - |
phosphate | pH 8.0, 55°C | Archaeoglobus fulgidus | |
70 | - |
ADP | pH 8.0, 55°C | Archaeoglobus fulgidus | |
95 | - |
acetyl-CoA | pH 8.0, 55°C | Archaeoglobus fulgidus | |
110 | - |
CoA | pH 8.0, 55°C | Archaeoglobus fulgidus | |
138 | - |
acetate | pH 8.0, 55°C | Archaeoglobus fulgidus | |
150 | - |
ATP | pH 8.0, 55°C | Archaeoglobus fulgidus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
- |
Archaeoglobus fulgidus |
8 | - |
assay at | Methanocaldococcus jannaschii |
8 | - |
assay at | Archaeoglobus fulgidus |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6 | 8 | about 50% of the maximal activity is found at pH 6 and 8 | Archaeoglobus fulgidus |
General Information | Comment | Organism |
---|---|---|
physiological function | the enzyme is involved in acetate formation and energy conservation | Methanocaldococcus jannaschii |
physiological function | the enzyme is involved in acetate formation and energy conservation | Archaeoglobus fulgidus |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.7 | - |
acetate | pH 8.0, 55°C | Archaeoglobus fulgidus | |
1.2 | - |
phenylacetate | pH 8.0, 55°C | Archaeoglobus fulgidus | |
2.7 | - |
indole-3-acetate | pH 8.0, 55°C | Archaeoglobus fulgidus | |
5.4 | - |
CoA | pH 8.0, 55°C | Archaeoglobus fulgidus | |
100 | - |
ATP | pH 8.0, 55°C | Archaeoglobus fulgidus | |
111 | - |
phenylacetate | pH 8.0, 55°C | Archaeoglobus fulgidus | |
140 | - |
phenylacetyl-CoA | pH 8.0, 55°C | Archaeoglobus fulgidus | |
400 | - |
acetate | pH 8.0, 55°C | Archaeoglobus fulgidus | |
520 | - |
phosphate | pH 8.0, 55°C | Archaeoglobus fulgidus | |
1120 | - |
ATP | pH 8.0, 55°C | Archaeoglobus fulgidus | |
4000 | - |
CoA | pH 8.0, 55°C | Archaeoglobus fulgidus | |
9200 | - |
acetyl-CoA | pH 8.0, 55°C | Archaeoglobus fulgidus | |
10000 | - |
ADP | pH 8.0, 55°C | Archaeoglobus fulgidus |