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Literature summary for 2.3.1.8 extracted from
- Kinetic studies with phosphotransacetylase. 3. The acylation of phosphate ions by acetyl coenzyme A (1972), Biochim. Biophys. Acta, 276, 376-382.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetic studies | Clostridium kluyveri |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetyl-CoA + phosphate | Clostridium kluyveri | - |
CoA + acetyl phosphate | - |
r |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Clostridium kluyveri | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| acetyl-CoA + phosphate = CoA + acetyl phosphate | reaction mechanism | Clostridium kluyveri |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetyl-CoA + phosphate | - |
Clostridium kluyveri | CoA + acetyl phosphate | - |
r | |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
pH effects on enzymatic reaction | Clostridium kluyveri |
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Release 2023.1 (January 2023)
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