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Literature summary for 1.7.1.15 extracted from
- Prosthetic groups of the NADH-dependent nitrite reductase from Escherichia coli K12 (1981), Biochem. J., 193, 861-867.
General Stability
| General Stability | Organism |
|---|---|
| 1 mM nitrite and 5O mM hydroxylamine are equally effective in decreasing the loss of activity after 24h at 40°C from 40% to 10%. No increase in catalytic activity is detected when enzyme is pre-incubated for 15 min with either of these substrates, even when NAD+ is omitted from the assay mixture | Escherichia coli |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| KCN | although 1 mM KCN completely inhibits hydroxylamine reduction, it does not inhibit the reduction of K3Fe(CN)6 and only decreases the rate of cytochrome c reduction by 12% | Escherichia coli |  |
| p-chloromercuribenzoate | the reduction of cytochrome c, K3Fe(CN)6 and hydroxylamine is completely inhibited (more than 99%) by 0.02 mM p-chloromercuribenzoate | Escherichia coli | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 88000 | - |
x * 88000, SDS-PAGE | 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 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| purified in the presence of 1 mM NO2- and 0.01 mM FAD by ammonium sulfate precipitation, DEAE-cellulose column chromatography, DEAE-Sephadex gel filtration, and Sephadex G-25 gel filtration | Escherichia coli |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.052 | - |
crude extract, at pH 8.0 and 30°C | Escherichia coli |
| 62.4 | - |
after 121fold purification, at pH 8.0 and 30°C | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| horse heart cytochrome c + NADH + H+ | - |
Escherichia coli | ? | - |
? | |
| K3Fe(CN)6 + NADH + H+ | - |
Escherichia coli | ? | - |
? | |
| NADH + H+ + oxidized 2,6-dichlorophenolindophenol | - |
Escherichia coli | NAD+ + reduced 2,6-dichlorophenolindophenol | - |
? | |
| nitrite + NADH + H+ | - |
Escherichia coli | ammonia + NAD+ + H2O | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 88000, SDS-PAGE | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| EC 1.6.6.4 | formerly | Escherichia coli |
| NADH-dependent nitrite reductase | - |
Escherichia coli |
| NADH-nitrite oxidoreductase | - |
Escherichia coli |
| nirB | - |
Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | the enzyme contains one non-covalently bound FAD molecule | Escherichia coli | |
| Fe-S center | the enzyme contains 5 Fe atoms and 4 acid-labile S atoms per subunit | Escherichia coli | |
| additional information | the enzyme does not contain FMN | Escherichia coli | |
| NADH | - |
Escherichia coli | |
| siroheme | - |
Escherichia coli | |
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Release 2023.1 (January 2023)
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