EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
4.1.1.32 | Co3+-GDP | competitive inhibitor | Gallus gallus | |
4.1.1.32 | Co3+-GTP | competitive inhibitor | Gallus gallus | |
4.1.1.32 | Cr3+-GDP | competitive inhibitor | Gallus gallus | |
4.1.1.32 | Cr3+-GTP | competitive inhibitor | Gallus gallus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.1.1.32 | additional information | - |
additional information | kinetic data for Mn2+ binding | Gallus gallus | |
4.1.1.32 | 0.111 | - |
oxaloacetate | 25°C, apoenzyme | Gallus gallus | |
4.1.1.32 | 0.123 | - |
oxaloacetate | 25°C, Co3+(n1)-PEPCK | Gallus gallus | |
4.1.1.32 | 0.131 | - |
oxaloacetate | 25°C, Co3+(n1)-PEPCK-Co3+(n2)-GTP | Gallus gallus |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
4.1.1.32 | mitochondrion | mitochondrial isoenzyme | Gallus gallus | 5739 | - |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
4.1.1.32 | Ca2+ | poor activating cation | Gallus gallus | |
4.1.1.32 | Co3+ | study of Co3+-PEPCK with Co3+ bound to enzyme at site n1 | Gallus gallus | |
4.1.1.32 | Cr3+ | study of Co3+-PEPCK with Cr3+ bound to enzyme at site n1 | Gallus gallus | |
4.1.1.32 | Mn2+ | best activator, enzyme requires two divalent cations, one activates through a direct interaction with enzyme at site n1, located at Asp-295 and Asp-296, the second cation, at site n2, acts in the cation-nucleotide complex that serves as a substrate, role and binding mode of Mn2+, may be a regulator for enzyme in vivo | Gallus gallus |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
4.1.1.32 | 67000 | - |
1 * 67000 | Gallus gallus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.1.32 | GTP + oxaloacetate | Gallus gallus | committed step in gluconeogenesis | GDP + phosphoenolpyruvate + CO2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.1.1.32 | Gallus gallus | - |
- |
- |
EC Number | Oxidation Stability | Organism |
---|---|---|
4.1.1.32 | PEPCK is very stable toward oxidative treatment | Gallus gallus |
EC Number | Purification (Comment) | Organism |
---|---|---|
4.1.1.32 | - |
Gallus gallus |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
4.1.1.32 | liver | - |
Gallus gallus | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
4.1.1.32 | additional information | - |
- |
Gallus gallus |
EC Number | Storage Stability | Organism |
---|---|---|
4.1.1.32 | 4°C, Co3+-PEPCK with Co3+ bound to enzyme at site n1, 1 week, stable | Gallus gallus |
4.1.1.32 | 4°C, Cr3+-PEPCK with Cr3+ bound to enzyme at site n1, at least 3 days, stable | Gallus gallus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.1.32 | GTP + oxaloacetate | metal-nucleotide complex serves as substrate, active site structure, a conformational change at the active site occurs during catalysis | Gallus gallus | GDP + phosphoenolpyruvate + CO2 | - |
r | |
4.1.1.32 | GTP + oxaloacetate | committed step in gluconeogenesis | Gallus gallus | GDP + phosphoenolpyruvate + CO2 | - |
? | |
4.1.1.32 | ITP + oxaloacetate | - |
Gallus gallus | IDP + phosphoenolpyruvate + CO2 | - |
r | |
4.1.1.32 | additional information | not: ATP | Gallus gallus | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
4.1.1.32 | monomer | 1 * 67000 | Gallus gallus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
4.1.1.32 | 25 | - |
assay at | Gallus gallus |