| EC |
1.7.1.15 |
| Accepted name: |
nitrite reductase (NADH) |
| Reaction: |
NH3 + 3 NAD+ + 2 H2O = nitrite + 3 NADH + 5 H+ |
| Other name(s): |
nitrite reductase (reduced nicotinamide adenine dinucleotide); NADH-nitrite oxidoreductase; assimilatory nitrite reductase (ambiguous); nirB (gene name); nirD (gene name) |
| Systematic name: |
ammonia:NAD+ oxidoreductase |
| Comments: |
An iron-sulfur flavoprotein (FAD) containing siroheme. This prokaryotic enzyme is specific for NADH. In addition to catalysing the 6-electron reduction of nitrite to ammonia, the enzyme from Escherichia coli can also catalyse the 2-electron reduction of hydroxylamine to ammonia. cf. EC 1.7.1.4, nitrite reductase [NAD(P)H]. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9029-29-2 |
| References: |
| 1. |
Vega, J.M., Guerrero, M.G., Leadbetter, E. and Losada, M. Reduced nicotinamide-adenine dinucleotide-nitrite reductase from Azotobacter chroococcum. Biochem. J. 133 (1973) 701–708. [PMID: 4147887] |
| 2. |
Jackson, R.H., Cornish-Bowden, A. and Cole, J.A. Prosthetic groups of the NADH-dependent nitrite reductase from Escherichia coli K12. Biochem. J. 193 (1981) 861–867. [PMID: 7030314] |
| 3. |
Cammack, R., Jackson, R.H., Cornish-Bowden, A. and Cole, J.A. Electron-spin-resonance studies of the NADH-dependent nitrite reductase from Escherichia coli K12. Biochem. J. 207 (1982) 333–339. [PMID: 6297458] |
| 4. |
Harborne, N.R., Griffiths, L., Busby, S.J. and Cole, J.A. Transcriptional control, translation and function of the products of the five open reading frames of the Escherichia coli nir operon. Mol. Microbiol. 6 (1992) 2805–2813. [DOI] [PMID: 1435259] |
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| [EC 1.7.1.15 created 2013] |
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