KEGG   ENZYME: 1.14.14.10Help
Entry
EC 1.14.14.10               Enzyme                                 

Name
nitrilotriacetate 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
BRITE hierarchy
Sysname
nitrilotriacetate,FMNH2:oxygen oxidoreductase (glyoxylate-forming)
Reaction(IUBMB)
nitrilotriacetate + FMNH2 + H+ + O2 = iminodiacetate + glyoxylate + FMN + H2O [RN:R09798]
Reaction(KEGG)
Substrate
nitrilotriacetate [CPD:C14695];
FMNH2 [CPD:C01847];
H+ [CPD:C00080];
O2 [CPD:C00007]
Product
iminodiacetate [CPD:C19911];
glyoxylate [CPD:C00048];
FMN [CPD:C00061];
H2O [CPD:C00001]
Comment
Requires Mg2+. The enzyme from Aminobacter aminovorans (previously Chelatobacter heintzii) is part of a two component system that also includes EC 1.5.1.42 (FMN reductase), which provides reduced flavin mononucleotide for this enzyme.
History
EC 1.14.14.10 created 2011
Orthology
K20147  
nitrilotriacetate monooxygenase
Reference
1  [PMID:1735711]
  Authors
Uetz T, Schneider R, Snozzi M, Egli T
  Title
Purification and characterization of a two-component monooxygenase that hydroxylates nitrilotriacetate from "Chelatobacter" strain ATCC 29600.
  Journal
J. Bacteriol. 174 (1992) 1179-88.
  Sequence
Reference
2  [PMID:8892809]
  Authors
Knobel HR, Egli T, van der Meer JR
  Title
Cloning and characterization of the genes encoding nitrilotriacetate monooxygenase of Chelatobacter heintzii ATCC 29600.
  Journal
J. Bacteriol. 178 (1996) 6123-32.
Reference
3  [PMID:9023192]
  Authors
Xu Y, Mortimer MW, Fisher TS, Kahn ML, Brockman FJ, Xun L
  Title
Cloning, sequencing, and analysis of a gene cluster from Chelatobacter heintzii ATCC 29600 encoding nitrilotriacetate monooxygenase and NADH:flavin mononucleotide oxidoreductase.
  Journal
J. Bacteriol. 179 (1997) 1112-6.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
UM-BBD (Biocatalysis/Biodegradation Database): 
BRENDA, the Enzyme Database: 

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