IUBMB Enzyme Nomenclature

EC 1.14.11.83

Accepted name: 2,4-dichlorophenoxyacetate dioxygenase

Reaction: 2,4-dichlorophenoxyacetate + 2-oxoglutarate + O2 = 2,4-dichlorophenol + glyoxylate + succinate + CO2

Other name(s): tfdA (gene name)

Systematic name: 2,4-dichlorophenoxyacetate,2-oxoglutarate:oxygen oxidoreductase (2,4-dichlorophenol-forming)

Comments: Requires Fe(II). The enzyme catalyses the first step in the bacterial degradation of 2,4-dichlorophenoxyacetate. Also acts on 4-chloro-2-methylphenoxyacetate.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Streber, W.R., Timmis, K.N. and Zenk, M.H. Analysis, cloning, and high-level expression of 2,4-dichlorophenoxyacetate monooxygenase gene tfdA of Alcaligenes eutrophus JMP134. J. Bacteriol. 169 (1987) 2950-2955. [PMID: 3036764]

2. Fukumori, F. and Hausinger, R.P. Alcaligenes eutrophus JMP134 "2,4-dichlorophenoxyacetate monooxygenase" is an α-ketoglutarate-dependent dioxygenase. J. Bacteriol. 175 (1993) 2083-2086. [PMID: 8458850]

3. Fukumori, F. and Hausinger, R.P. Purification and characterization of 2,4-dichlorophenoxyacetate/α-ketoglutarate dioxygenase. J. Biol. Chem. 268 (1993) 24311-24317. [PMID: 8226980]

4. Hausinger, R.P. and Fukumori, F. Characterization of the first enzyme in 2,4-dichlorophenoxyacetic acid metabolism. Environ Health Perspect 103 Suppl 5 (1995) 37-39. [PMID: 8565907]

5. Hogan, D.A., Smith, S.R., Saari, E.A., McCracken, J. and Hausinger, R.P. Site-directed mutagenesis of 2,4-dichlorophenoxyacetic acid/α-ketoglutarate dioxygenase. Identification of residues involved in metallocenter formation and substrate binding. J. Biol. Chem. 275 (2000) 12400-12409. [PMID: 10777523]

6. Poh, R., Xia, X., Bruce, I.J. and Smith, A.R. 2,4-dichlorophenoxyacetate/α-ketoglutarate dioxygenases from Burkholderia cepacia 2a and Ralstonia eutropha JMP134. Microbios 105 (2001) 43-63. [PMID: 11368091]

7. Dunning Hotopp, J.C. and Hausinger, R.P. Probing the 2,4-dichlorophenoxyacetate/α-ketoglutarate dioxygenase substrate-binding site by site-directed mutagenesis and mechanism-based inactivation. Biochemistry 41 (2002) 9787-9794. [PMID: 12146944]

[EC 1.14.11.83 created 2026]


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