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Literature summary for 1.17.1.9 extracted from
- Formate dehydrogenase. Subunit and mechanism of inhibition by cyanide and azide (1975), J. Biochem., 77, 845-852.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| CN- | - |
Pisum sativum |  |
| N3- | - |
Pisum sativum | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | the enzyme has two sites with about equal catalytic activity. The Km-values for formate are different for the two catalytic sites: 1.67 mM and 6.25 mM | Pisum sativum | |
| 1.67 | - |
formate | and 6.25 mM at the second catalytic site | Pisum sativum | |
| 6.25 | - |
formate | and 1.67 mM at the second catalytic site | Pisum sativum | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pisum sativum | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| formate + NAD+ | - |
Pisum sativum | CO2 + NADH + H+ | - |
? | |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | enzyme binds one NAD+ molecule per subunit | Pisum sativum | |
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