Any feedback?
Literature summary for 6.2.1.B11 extracted from
- 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 (2002), J. Bacteriol., 184, 636-644.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| overexpressed in Escherichia coli | Archaeoglobus fulgidus |
| overexpressed in Escherichia coli | Methanocaldococcus jannaschii |
KM Value [mM]
| 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
| 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 [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
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Archaeoglobus fulgidus | O28341 | - |
- |
| Archaeoglobus fulgidus | O29057 | - |
- |
| Methanocaldococcus jannaschii | Q58010 | - |
- |
| Methanocaldococcus jannaschii DSM 2661 | Q58010 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme | Archaeoglobus fulgidus |
| recombinant enzyme | Methanocaldococcus jannaschii |
Substrates and Products (Substrate)
| 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
| 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
| 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 [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 55 | - |
assay at | Methanocaldococcus jannaschii |
| 77 | - |
- |
Archaeoglobus fulgidus |
Temperature Range [°C]
| 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 [°C]
| 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 [1/s]
| 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
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
- |
Archaeoglobus fulgidus |
| 8 | - |
assay at | Methanocaldococcus jannaschii |
| 8 | - |
assay at | Archaeoglobus fulgidus |
pH Range
| 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
| 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 [mM/s]
| 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 | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
