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EC 1.14.12.24 Details

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EC number

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)

Comment

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.

History

created 2015

EC Tree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

1.2 Acting on the aldehyde or oxo group of donors

1.3 Acting on the CH-CH group of donors

1.4 Acting on the CH-NH₂ group of donors

1.5 Acting on the CH-NH group of donors

1.6 Acting on NADH or NADPH

1.6.1 With NAD⁺ or NADP⁺ as acceptor

1.6.2 With a heme protein as acceptor

1.6.3 With oxygen as acceptor

1.6.4 With a disulfide as acceptor (deleted sub-subclass)

1.6.5 With a quinone or similar compound as acceptor

1.6.6 With a nitrogenous group as acceptor

1.6.7 With an iron-sulfur protein as acceptor (deleted sub-subclass)

1.6.8 With a flavin as acceptor (deleted sub-subclass)

1.6.99 With unknown physiological acceptors

1.7 Acting on other nitrogenous compounds as donors

1.8 Acting on a sulfur group of donors

1.9 Acting on a heme group of donors

1.10 Acting on diphenols and related substances as donors

1.11 Acting on a peroxide as acceptor

1.12 Acting on hydrogen as donor

1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)

1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

1.14.1 With NADH or NADPH as one donor (deleted sub-subclass)

1.14.2 With ascorbate as one donor (deleted sub-subclass)

1.14.3 With reduced pteridine as one donor (deleted sub-subclass)

1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor

1.14.12 With NADH or NADPH as one donor, and incorporation of two atoms of oxygen into the other donor

1.14.12.1 anthranilate 1,2-dioxygenase (deaminating, decarboxylating)

1.14.12.2 created 1972, deleted 1990

1.14.12.3 benzene 1,2-dioxygenase

1.14.12.4 3-hydroxy-2-methylpyridinecarboxylate dioxygenase

1.14.12.5 5-pyridoxate dioxygenase

1.14.12.6 created 1978, deleted 1999

1.14.12.7 phthalate 4,5-dioxygenase

1.14.12.8 4-sulfobenzoate 3,4-dioxygenase

1.14.12.9 4-chlorophenylacetate 3,4-dioxygenase

1.14.12.10 benzoate 1,2-dioxygenase

1.14.12.11 toluene dioxygenase

1.14.12.12 naphthalene 1,2-dioxygenase

1.14.12.13 2-halobenzoate 1,2-dioxygenase

1.14.12.14 2-aminobenzenesulfonate 2,3-dioxygenase

1.14.12.15 terephthalate 1,2-dioxygenase

1.14.12.16 2-hydroxyquinoline 5,6-dioxygenase

1.14.12.17 nitric oxide dioxygenase

1.14.12.18 biphenyl 2,3-dioxygenase

1.14.12.19 3-phenylpropanoate dioxygenase

1.14.12.20 pheophorbide a oxygenase

1.14.12.21 benzoyl-CoA 2,3-dioxygenase

1.14.12.22 carbazole 1,9a-dioxygenase

1.14.12.23 nitroarene dioxygenase

1.14.12.24 2,4-dinitrotoluene dioxygenase

1.14.12.25 p-cumate 2,3-dioxygenase

1.14.12.26 chlorobenzene dioxygenase

1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor

1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor

1.14.15 With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor

1.14.16 With reduced pteridine as one donor, and incorporation of one atom of oxygen into the other donor

1.14.17 With reduced ascorbate as one donor, and incorporation of one atom of oxygen into the other donor

1.14.18 With another compound as one donor, and incorporation of one atom of oxygen into the other donor

1.14.19 With oxidation of a pair of donors resulting in the reduction of O₂ to two molecules of water

1.14.20 With 2-oxoglutarate as one donor, and the other dehydrogenated

1.14.21 With NADH or NADPH as one donor, and the other dehydrogenated

1.14.99 Miscellaneous

1.15 Acting on superoxide as acceptor

1.16 Oxidizing metal ions

1.17 Acting on CH or CH₂ groups

1.18 Acting on iron-sulfur proteins as donors

1.19 Acting on reduced flavodoxin as donor

1.20 Acting on phosphorus or arsenic in donors

1.21 Catalysing the reaction X-H + Y-H = X-Y

1.21.1 With NAD⁺ or NADP⁺ as acceptor

1.21.3 With oxygen as acceptor

1.21.3.1 isopenicillin-N synthase

1.21.3.2 columbamine oxidase

1.21.3.3 reticuline oxidase

1.21.3.4 sulochrin oxidase [(+)-bisdechlorogeodin-forming]

1.21.3.5 sulochrin oxidase [(-)-bisdechlorogeodin-forming]

1.21.3.6 aureusidin synthase

1.21.3.7 tetrahydrocannabinolic acid synthase

1.21.3.8 cannabidiolic acid synthase

1.21.3.9 dichlorochromopyrrolate synthase

1.21.3.10 hercynylcysteine S-oxide synthase

1.21.4 With a disulfide as acceptor

1.21.98 With other, known, physiological acceptors

1.21.99 With unknown physiological acceptors

1.22 Acting on halogen in donors

1.23 Reducing C-O-C group as acceptor

1.97 Other oxidoreductases

1.97.1 Sole sub-subclass for oxidoreductases that do not belong in the other subclasses

1.98 Enzymes using H₂ as reductant (deleted subclass)

1.99 Other enzymes using O₂ as oxidant (deleted subclass)

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Release 2023.1 (January 2023)