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Literature summary for 2.3.3.8 extracted from
- Effects of phosphorylation on the kinetic properties of rat liver ATP-citrate lyase (1985), Biochim. Biophys. Acta, 844, 233-239.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | - |
Rattus norvegicus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| side-chain modification | phosphoprotein | Rattus norvegicus |
| side-chain modification | maximum level of phosphorylation is 2 mol phosphate per mol of tetramer, phosphorylation can affect the activity of the enzyme | Rattus norvegicus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Rattus norvegicus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + citrate + CoA | - |
Rattus norvegicus | ADP + phosphate + acetyl-CoA + oxaloacetate | - |
? |  |
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Release 2023.1 (January 2023)
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