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Literature summary for 2.7.2.1 extracted from
- Acetate kinase (1962), The Enzymes, 2nd. Ed. (Boyer, P. D. , Lardy, H. , Myrbaeck, K. , eds. ), 6, 115-118.
No PubMed abstract available
General Stability
| General Stability | Organism |
|---|---|
| stabilized during storage by L-cysteine | Escherichia coli |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| HgCl2 | - |
Escherichia coli |  |
| Iodosobenzoate | - |
Escherichia coli | |
| p-mercuribenzoate | - |
Escherichia coli | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.5 | - |
ADP | pH 7.4 | Escherichia coli | |
| 5 | - |
acetyl phosphate | pH 7.4 | Escherichia coli | |
| 90 | - |
acetate | pH 7.4 | Streptococcus pyogenes | |
| 300 | - |
acetate | pH 7.4 | Escherichia coli | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | absolute requirement at pH 7.4 | Escherichia coli | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + acetate | Streptococcus pyogenes | - |
ADP + acetyl phosphate | - |
r | |
| ATP + acetate | Lactobacillus delbrueckii | - |
ADP + acetyl phosphate | - |
r | |
| ATP + acetate | Escherichia coli | acetate kinase/phosphotransacetylase, major role of this two-enzyme sequence is to provide acetyl coenzyme A which may participate in fatty acid synthesis, citrate formation and subsequent oxidation | ADP + acetyl phosphate | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
| Lactobacillus delbrueckii | - |
- |
- |
| Streptococcus pyogenes | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Escherichia coli |
- |
Streptococcus pyogenes |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 282 | - |
- |
Streptococcus pyogenes |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + acetate | - |
Escherichia coli | ADP + acetyl phosphate | - |
r | |
| ATP + acetate | - |
Streptococcus pyogenes | ADP + acetyl phosphate | - |
r | |
| ATP + acetate | - |
Lactobacillus delbrueckii | ADP + acetyl phosphate | - |
r | |
| ATP + acetate | acetate kinase/phosphotransacetylase, major role of this two-enzyme sequence is to provide acetyl coenzyme A which may participate in fatty acid synthesis, citrate formation and subsequent oxidation | Escherichia coli | ADP + acetyl phosphate | - |
r | |
| ATP + propionate | one-tenth of the rate shown with acetate | Escherichia coli | ADP + propionyl phosphate | - |
r | |
| ITP + acetate | - |
Escherichia coli | IDP + acetyl phosphate | - |
r | |
| additional information | formate, butyrate and various holo and hydroxy derivatives of acetate and propionate are not phosphorylated | Escherichia coli | ? | - |
? | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
- |
Escherichia coli |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | 7.8 | enzyme undergoes irreversible inactivation outside this range | Escherichia coli |
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