EC 1.14.13.166 - 4-nitrocatechol 4-monooxygenase

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IntEnz Enzyme Nomenclature
EC 1.14.13.166

Names

Accepted name:
4-nitrocatechol 4-monooxygenase
Systematic name:
4-nitrocatechol,NAD(P)H:oxygen 4-oxidoreductase (4-hydroxylating, nitrite-forming)

Reaction

Cofactor

Comments:

Contains FAD. The enzyme catalyses the oxidation of 4-nitrocatechol with the concomitant removal of the nitro group as nitrite. Forms a two-component system with a flavoprotein reductase [1]. The enzymes from the bacteria Lysinibacillus sphaericus JS905 and Rhodococcus sp. strain PN1 were shown to also catalyse EC 1.14.13.29, 4-nitrophenol 2-monooxygenase [1,2] while the enzyme from Pseudomonas sp. WBC-3 was shown to also catalyse EC 1.14.13.167, 4-nitrophenol 4-monooxygenase [3].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0018592
UniProtKB/Swiss-Prot:

References

  1. Kadiyala, V., Spain, J. C.
    A two-component monooxygenase catalyzes both the hydroxylation of p-nitrophenol and the oxidative release of nitrite from 4-nitrocatechol in Bacillus sphaericus JS905.
    Appl. Environ. Microbiol. 64 : 2479-2484 (1998). [PMID: 9647818]
  2. Kitagawa, W., Kimura, N., Kamagata, Y.
    A novel p-nitrophenol degradation gene cluster from a gram-positive bacterium, Rhodococcus opacus SAO101.
    J. Bacteriol. 186 : 4894-4902 (2004). [PMID: 15262926]
  3. Zhang, J. J., Liu, H., Xiao, Y., Zhang, X. E., Zhou, N. Y.
    Identification and characterization of catabolic para-nitrophenol 4-monooxygenase and para-benzoquinone reductase from Pseudomonas sp. strain WBC-3.
    J. Bacteriol. 191 : 2703-2710 (2009). [PMID: 19218392]

[EC 1.14.13.166 created 2012]