Entry |
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Name |
4-nitrocatechol 4-monooxygenase
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Class |
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
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Sysname |
4-nitrocatechol,NAD(P)H:oxygen 4-oxidoreductase (4-hydroxylating, nitrite-forming)
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Reaction(IUBMB) |
4-nitrocatechol + NAD(P)H + H+ + O2 = 2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H2O
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Substrate |
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Product |
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Comment |
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].
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History |
EC 1.14.13.166 created 2012
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Orthology |
K21725 | 4-nitrocatechol/4-nitrophenol 4-monooxygenase |
K21726 | 4-nitrophenol 2-monooxygenase / 4-nitrocatechol 4-monooxygenase, oxygenase component |
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Genes |
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Reference |
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Authors |
Kadiyala V, Spain JC |
Title |
A two-component monooxygenase catalyzes both the hydroxylation of p-nitrophenol and the oxidative release of nitrite from 4-nitrocatechol in Bacillus sphaericus JS905. |
Journal |
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Reference |
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Authors |
Kitagawa W, Kimura N, Kamagata Y |
Title |
A novel p-nitrophenol degradation gene cluster from a gram-positive bacterium, Rhodococcus opacus SAO101. |
Journal |
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Sequence |
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Reference |
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Authors |
Zhang JJ, Liu H, Xiao Y, Zhang XE, Zhou NY |
Title |
Identification and characterization of catabolic para-nitrophenol 4-monooxygenase and para-benzoquinone reductase from Pseudomonas sp. strain WBC-3. |
Journal |
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Sequence |
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Other DBs |
UM-BBD (Biocatalysis/Biodegradation Database): | 1.14.13.166 |
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