EC 1 - Oxidoreductases
EC 1.14 - Acting on paired donors, with incorporation or reduction of molecular oxygen. The oxygen incorporated need not be derived from O2
EC 1.14.12 - With NADH or NADPH as one donor, and incorporation of two atoms of oxygen into one donor
EC 1.14.12.24 - 2,4-dinitrotoluene dioxygenase
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 1.14.12.24
Names
Accepted name:
2,4-dinitrotoluene dioxygenase
Other
name:
dntA (gene name)
Systematic name:
2,4-dinitrotoluene,NADH:oxygen oxidoreductase (4,5-hydroxylating,nitrite-releasing)
Reaction
-
46760 [IUBMB]+2,4-dinitrotolueneName origin: UniProt - CHECKED (C)Formula: C7H6N2O4
Charge: 0ChEBI compound status: CHECKED (C)+NADHName origin: UniProt - CHECKED (C)Formula: C21H27N7O14P2
Charge: -2ChEBI compound status: CHECKED (C)O2Name origin: UniProt - CHECKED (C)Formula: O2
Charge: 0ChEBI compound status: CHECKED (C)=+4-methyl-5-nitrocatecholName origin: UniProt - CHECKED (C)Formula: C7H7NO4
Charge: 0ChEBI compound status: CHECKED (C)+NAD+Name origin: UniProt - CHECKED (C)Formula: C21H26N7O14P2
Charge: -1ChEBI compound status: CHECKED (C)
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
UniProtKB/Swiss-Prot:
DNTAC_BURSR
References
-
2,4-Dinitrotoluene dioxygenase from Burkholderia sp. strain DNT: similarity to naphthalene dioxygenase.J. Bacteriol. 178 : 4926-4934 (1996). [PMID: 8759857]
[EC 1.14.12.24 created 2015]