| EC |
1.14.12.24 |
| Accepted name: |
2,4-dinitrotoluene dioxygenase |
| Reaction: |
2,4-dinitrotoluene + NADH + O2 = 4-methyl-5-nitrocatechol + nitrite + NAD+ |
| Other name(s): |
dntA (gene name) |
| Systematic name: |
2,4-dinitrotoluene,NADH:oxygen oxidoreductase (4,5-hydroxylating, nitrite-releasing) |
| Comments: |
This enzyme, characterized from the bacterium Burkholderia sp. strain DNT, is a member of the naphthalene family of bacterial Rieske non-heme iron dioxygenases. It comprises a multicomponent system, containing a Rieske [2Fe-2S] ferredoxin, an NADH-dependent flavoprotein reductase (EC 1.18.1.3, ferredoxin—NAD+ reductase), and an α3β3 oxygenase. The enzyme forms a cis-dihydroxylated product that spontaneously rearranges to form a catechol with accompanying release of nitrite. It does not act on nitrobenzene. cf. EC 1.14.12.23, nitroarene dioxygenase. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Suen, W.C., Haigler, B.E. and Spain, J.C. 2,4-Dinitrotoluene dioxygenase from Burkholderia sp. strain DNT: similarity to naphthalene dioxygenase. J. Bacteriol. 178 (1996) 4926–4934. [DOI] [PMID: 8759857] |
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| [EC 1.14.12.24 created 2015] |
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