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1.14.14.33

Accepted name:

ethylenediaminetetraacetate monooxygenase

Reaction:

ethylenediaminetetraacetate + 2 FMNH₂ + 2 O₂ = ethylenediamine-N,N′-diacetate + 2 glyoxylate + 2 FMN + 2 H₂O (overall reaction)
(1a) ethylenediaminetetraacetate + FMNH₂ + O₂ = ethylenediaminetriacetate + glyoxylate + FMN + H₂O
(1b) ethylenediaminetriacetate + FMNH₂ + O₂ = ethylenediamine-N,N′-diacetate + glyoxylate + FMN + H₂O

Glossary:

ethylenediaminetetraacetate = EDTA

Systematic name:

ethylenediaminetetraacetate,FMNH₂:O₂ oxidoreductase (glyoxylate-forming)

Comments:

The enzyme is part of a two component system that also includes EC 1.5.1.42, FMN reductase (NADH), which provides reduced flavin mononucleotide for this enzyme. It acts on EDTA only when it is complexed with divalent cations such as Mg²⁺, Zn²⁺, Mn²⁺, Co²⁺, or Cu²⁺. While the enzyme has a substrate overlap with EC 1.14.14.10, nitrilotriacetate monooxygenase, it has a much wider substrate range, which includes nitrilotriacetate (NTA) and diethylenetriaminepentaacetate (DTPA) in addition to EDTA.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Witschel, M., Nagel, S. and Egli, T. Identification and characterization of the two-enzyme system catalyzing oxidation of EDTA in the EDTA-degrading bacterial strain DSM 9103. J. Bacteriol. 179 (1997) 6937–6943. [DOI] [PMID: 9371437]
2.	Payne, J.W., Bolton, H., Jr., Campbell, J.A. and Xun, L. Purification and characterization of EDTA monooxygenase from the EDTA-degrading bacterium BNC1. J. Bacteriol. 180 (1998) 3823–3827. [PMID: 9683478]
3.	Bohuslavek, J., Payne, J.W., Liu, Y., Bolton, H., Jr. and Xun, L. Cloning, sequencing, and characterization of a gene cluster involved in EDTA degradation from the bacterium BNC1. Appl. Environ. Microbiol. 67 (2001) 688–695. [DOI] [PMID: 11157232]

[EC 1.14.14.33 created 2016]