Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | no inhibition by ferredoxin | Pyrococcus furiosus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | binding affinity of CoA is 0.11 mM | Pyrococcus furiosus | |
1.1 | - |
pyruvate | pH and temperature not specified in the publication | Pyrococcus furiosus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pyrococcus furiosus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Pyrococcus furiosus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pyruvate | pyruvate ferredoxin oxidoreductase functions as a CoA-dependent pyruvate decarboxylase. Ferredoxin is not necessary for the pyruvate decarboxylase activity of POR. At 80°C (pH 8.0), the apparent Vm value for pyruvate decarboxylation is about 40% of the apparent Vm value for pyruvate oxidation rate (using Pyrococcus furiosus ferredoxin as the electron acceptor), 60% at pH 10.2 (80°C) | Pyrococcus furiosus | acetaldehyde + CO2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
POR | bifunctional enzyme that catalyzes both the oxidative and nonoxidative decarboxylation of pyruvate | Pyrococcus furiosus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
90 | - |
above | Pyrococcus furiosus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
10 | - |
- |
Pyrococcus furiosus |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
8 | 11.5 | pH 8.0: about 60% of maximal activity, pH 10.0: about 50% of maximal activity | Pyrococcus furiosus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
CoA | desulfocoenzyme A can substitute for CoA showing that the cofactor plays a structural rather than a catalytic role | Pyrococcus furiosus |