EC 1.14.12.23 - Nitroarene dioxygenase

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IntEnz Enzyme Nomenclature
EC 1.14.12.23

Names

Accepted name:
nitroarene dioxygenase
Other name:
cnbA (gene name)
Systematic name:
nitrobenzene,NADH:oxygen oxidoreductase (1,2-hydroxylating, nitrite-releasing)

Reactions

Cofactor

Comments:

This enzyme 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 of a cis-dihydroxylated product that spontaneously rearranges to form a catechol with accompanying release of nitrite. It can typically act on many different nitroaromatic compounds, including chlorinated species. Enzymes found in different strains may have different substrate preferences. Requires Fe2+.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB

References

  1. Parales, J. V., Parales, R. E., Resnick, S. M., Gibson, D. T.
    Enzyme specificity of 2-nitrotoluene 2,3-dioxygenase from Pseudomonas sp. strain JS42 is determined by the C-terminal region of the alpha subunit of the oxygenase component.
    J. Bacteriol. 180: 1194-1199 (1998). [PMID: 9495758]
  2. Lessner, D. J., Johnson, G. R., Parales, R. E., Spain, J. C., Gibson, D. T.
    Molecular characterization and substrate specificity of nitrobenzene dioxygenase from Comamonas sp. strain JS765.
    Appl. Environ. Microbiol. 68: 634-641 (2002). [PMID: 11823201]
  3. Liu, H., Wang, S. J., Zhang, J. J., Dai, H., Tang, H., Zhou, N. Y.
    Patchwork assembly of nag-like nitroarene dioxygenase genes and the 3-chlorocatechol degradation cluster for evolution of the 2-chloronitrobenzene catabolism pathway in Pseudomonas stutzeri ZWLR2-1.
    Appl. Environ. Microbiol. 77: 4547-4552 (2011). [PMID: 21602392]
  4. Singh, D., Kumari, A., Ramaswamy, S., Ramanathan, G.
    Expression, purification and substrate specificities of 3-nitrotoluene dioxygenase from Diaphorobacter sp. strain DS2.
    Biochem. Biophys. Res. Commun. 445: 36-42 (2014). [PMID: 24491551]

[EC 1.14.12.23 created 2015]