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Literature summary for 1.7.1.15 extracted from
- The steady-state kinetics of the NADH-dependent nitrite reductase from Escherichia coli K12 (1981), Biochem. J., 199, 171-178.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | the apparent maximum velocity with NADH as varied substrate increases as the NAD+ concentration increases from 0.05 to 0.7 mM with 1 mM nitrite or 100 mM hydroxylamine as oxidized substrate | Escherichia coli |  |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | NAD+ shows mixed product inhibition with respect to NADH and mixed or uncompetitive inhibition with respect to hydroxylamine | Escherichia coli | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| nitrite + NADH + H+ | Escherichia coli | - |
ammonia + NAD+ + H2O | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| hydroxylamine + NADH + H+ | - |
Escherichia coli | ? | - |
? | |
| nitrite + NADH + H+ | - |
Escherichia coli | ammonia + NAD+ + H2O | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| NADH-dependent nitrite reductase | - |
Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADH | - |
Escherichia coli | |
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