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Literature summary for 2.7.2.12 extracted from
- Structural and mutational analysis of amino acid residues involved in ATP specificity of Escherichia coli acetate kinase (2014), J. Biosci. Bioeng., 118, 502-507.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| sequence comparisons, recombinant overexpression of His-tagged enzyme in Escherichia coli strain MK3648 | Entamoeba histolytica |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics | Entamoeba histolytica | |
| 3.3 | - |
diphosphate | pH 6.5-7.5, 30°C, recombinant enzyme | Entamoeba histolytica |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Entamoeba histolytica | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 44000 | - |
x * 44000, recombinant His-tagged enzyme, SDS-PAGE | Entamoeba histolytica |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| diphosphate + acetate | Entamoeba histolytica | - |
phosphate + acetyl phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Entamoeba histolytica | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| diphosphate + acetate | - |
Entamoeba histolytica | phosphate + acetyl phosphate | - |
? | |
| additional information | no activity with ATP | Entamoeba histolytica | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 44000, recombinant His-tagged enzyme, SDS-PAGE | Entamoeba histolytica |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| diphosphate-specific AK | - |
Entamoeba histolytica |
| PPi-dependent AK | - |
Entamoeba histolytica |
| PPi-ehiAK | - |
Entamoeba histolytica |
| pyrophosphate-dependent AK | - |
Entamoeba histolytica |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Entamoeba histolytica |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 2.6 | - |
diphosphate | pH 6.5-7.5, 30°C, recombinant enzyme | Entamoeba histolytica | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | - |
assay at, diphosphate forming reaction direction | Entamoeba histolytica |
| 6.5 | 7.5 | acetyl phosphate-forming reaction direction, assay at | Entamoeba histolytica |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| diphosphate | purified enzyme PPi-ehiAK utilizes diphosphate, but not ATP, as a phosphoryl donor | Entamoeba histolytica | |
| additional information | no activity with ATP | Entamoeba histolytica |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | residue Asn337 of ATP-ecoAK is particularly significant for the specificity to ATP. The five residues are highly conserved in 2625 PPi-ehiAK homologue implying that almost all organisms have ATP-dependent acetate kinase, EC 2.7.2.1, rather than diphosphate-dependent acetate kinase, EC 2.7.2.12 | Entamoeba histolytica |
| additional information | substrate-binding site structure and comparison with ATP-dependent acetate kinase, EC 2.7.2.1, overview | Entamoeba histolytica |
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