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 | 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 Maximum [Da] | Comment | Organism |
---|---|---|---|
88000 | - |
x * 88000, SDS-PAGE | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
nitrite + NADH + H+ | Escherichia coli | - |
ammonia + NAD+ + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
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 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 | 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 | Comment | Organism |
---|---|---|
? | x * 88000, SDS-PAGE | Escherichia coli |
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 | 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 |