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Literature summary for 2.3.3.8 extracted from
- Effect of oxaloacetate and phosphorylation on ATP-citrate lyase activity (1995), Biochemistry, 34, 10961-10969.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| oxaloacetate | - |
Rattus norvegicus |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| side-chain modification | phosphoprotein | Rattus norvegicus |
| side-chain modification | citrate lyase phosphorylation by cAMP-dependent protein kinase or this kinase plus glycogen synthase kinase-3 decreases the maximal velocity whereas the apparent Km for citrate is unchanged | Rattus norvegicus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Rattus norvegicus | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
- |
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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