KEGG   ENZYME: 1.14.14.33
Entry
EC 1.14.14.33               Enzyme                                 

Name
ethylenediaminetetraacetate monooxygenase
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
Sysname
ethylenediaminetetraacetate,FMNH2:O2 oxidoreductase (glyoxylate-forming)
Reaction(IUBMB)
ethylenediaminetetraacetate + 2 FMNH2 + 2 O2 = ethylenediamine-N,N'-diacetate + 2 glyoxylate + 2 FMN + 2 H2O (overall reaction) [RN:R11456];
(1a) ethylenediaminetetraacetate + FMNH2 + O2 = ethylenediaminetriacetate + glyoxylate + FMN + H2O [RN:R11454];
(1b) ethylenediaminetriacetate + FMNH2 + O2 = ethylenediamine-N,N'-diacetate + glyoxylate + FMN + H2O [RN:R11455]
Reaction(KEGG)
Substrate
ethylenediaminetetraacetate [CPD:C00284];
FMNH2 [CPD:C01847];
O2 [CPD:C00007];
ethylenediaminetriacetate [CPD:C21396]
Product
ethylenediamine-N,N'-diacetate;
glyoxylate [CPD:C00048];
FMN [CPD:C00061];
H2O [CPD:C00001];
ethylenediaminetriacetate [CPD:C21396]
Comment
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.
History
EC 1.14.14.33 created 2016
Reference
1  [PMID:9371437]
  Authors
Witschel M, Nagel S, Egli T
  Title
Identification and characterization of the two-enzyme system catalyzing oxidation of EDTA in the EDTA-degrading bacterial strain DSM 9103.
  Journal
J Bacteriol 179:6937-43 (1997)
DOI:10.1128/JB.179.22.6937-6943.1997
Reference
2  [PMID:9683478]
  Authors
Payne JW, Bolton H Jr, Campbell JA, Xun L
  Title
Purification and characterization of EDTA monooxygenase from the EDTA-degrading bacterium BNC1.
  Journal
J Bacteriol 180:3823-7 (1998)
DOI:10.1128/JB.180.15.3823-3827.1998
Reference
3  [PMID:11157232]
  Authors
Bohuslavek J, Payne JW, Liu Y, Bolton H Jr, Xun L
  Title
Cloning, sequencing, and characterization of a gene cluster involved in EDTA degradation from the bacterium BNC1.
  Journal
Appl Environ Microbiol 67:688-95 (2001)
DOI:10.1128/AEM.67.2.688-695.2001
Other DBs
ExplorEnz - The Enzyme Database: 1.14.14.33
IUBMB Enzyme Nomenclature: 1.14.14.33
ExPASy - ENZYME nomenclature database: 1.14.14.33
BRENDA, the Enzyme Database: 1.14.14.33

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