KEGG   ENZYME: 1.6.3.3Help
Entry
EC 1.6.3.3                  Enzyme                                 

Name
NADH oxidase (H2O2-forming);
NOX-1;
H2O2-forming NADH oxidase
Class
Oxidoreductases;
Acting on NADH or NADPH;
With oxygen as acceptor
BRITE hierarchy
Sysname
NADH:oxygen oxidoreductase (H2O2-forming)
Reaction(IUBMB)
NADH + H+ + O2 = NAD+ + H2O2 [RN:R07171]
Reaction(KEGG)
Substrate
NADH [CPD:C00004];
H+ [CPD:C00080];
O2 [CPD:C00007]
Product
NAD+ [CPD:C00003];
H2O2 [CPD:C00027]
Comment
A flavoprotein (FAD). The bacterium Streptococcus mutans contains two distinct NADH oxidases, a H2O2-forming enzyme and a H2O-forming enzyme (cf. EC 1.6.3.4, NADH oxidase (H2O-forming)) [1]. The enzymes from the anaerobic archaea Methanocaldococcus jannaschii [6] and Pyrococcus furiosus [3] also produce low amounts of H2O. Unlike EC 1.6.3.1 (NAD(P)H oxidase) it has no activity towards NADPH.
History
EC 1.6.3.3 created 2013
Orthology
K17870  
NADH oxidase (H2O2-forming)
Genes
MJA: 
MFE: 
MVU: 
MFS: 
MIF: 
MJH: 
MIG: 
MMP: 
MMQ: 
MMX: 
MMZ: 
MMD: 
MMAK: 
MMAO: 
MAE: 
MVN: 
MVO: 
MOK: 
MAC: 
MA_4636(ndh)
MBA: 
MBY: 
MBW: 
MBAR: 
MBAK: 
MMA: 
MMAZ: 
MMJ: 
MMAC: 
MVC: 
MEK: 
MLS: 
METM: 
MEF: 
MEQ: 
MSJ: 
MSZ: 
MSW: 
MTHE: 
MTHR: 
MHOR: 
MBU: 
MMET: 
MEV: 
MPY: 
MHZ: 
MCJ: 
MPD: 
MEZ: 
RCI: 
RCIX501(ndh)
MTH: 
MMG: 
METC: 
MWO: 
MST: 
MSI: 
MRU: 
MEB: 
MMIL: 
MEYE: 
MOL: 
MEL: 
MEW: 
METH: 
MFC: 
MFI: 
MCUB: 
MFV: 
MKA: 
TAR: 
MAX: 
MER: 
MEAR: 
MARC: 
PHO: 
PH1509(PH1509)
PAB: 
PFU: 
PFI: 
PYN: 
PYA: 
PYS: 
PYC: 
TKO: 
TON: 
TGA: 
TSI: 
TBA: 
THE: 
THA: 
THM: 
TLT: 
THS: 
TNU: 
TEU: 
TGY: 
THV: 
TCH: 
TPEP: 
TPIE: 
PPAC: 
ACF: 
KCR: 
BARC: 
 » show all
Taxonomy
Reference
1  [PMID:8254304]
  Authors
Higuchi M, Shimada M, Yamamoto Y, Hayashi T, Koga T, Kamio Y
  Title
Identification of two distinct NADH oxidases corresponding to H2O2-forming oxidase and H2O-forming oxidase induced in Streptococcus mutans.
  Journal
J. Gen. Microbiol. 139 (1993) 2343-51.
  Sequence
[smu:SMU_765]
Reference
2  [PMID:11722568]
  Authors
Ward DE, Donnelly CJ, Mullendore ME, van der Oost J, de Vos WM, Crane EJ 3rd
  Title
The NADH oxidase from Pyrococcus furiosus. Implications for the protection of anaerobic hyperthermophiles against oxidative stress.
  Journal
Eur. J. Biochem. 268 (2001) 5816-23.
  Sequence
[pfu:PF1532]
Reference
3  [PMID:12823559]
  Authors
Kengen SW, van der Oost J, de Vos WM
  Title
Molecular characterization of H2O2-forming NADH oxidases from Archaeoglobus fulgidus.
  Journal
Eur. J. Biochem. 270 (2003) 2885-94.
  Sequence
Reference
4  [PMID:17293421]
  Authors
Yang X, Ma K
  Title
Characterization of an exceedingly active NADH oxidase from the anaerobic hyperthermophilic bacterium Thermotoga maritima.
  Journal
J. Bacteriol. 189 (2007) 3312-7.
  Sequence
Reference
5  [PMID:18521590]
  Authors
Hirano J, Miyamoto K, Ohta H
  Title
Purification and characterization of thermostable H2O2-forming NADH oxidase from  2-phenylethanol-assimilating Brevibacterium sp. KU1309.
  Journal
Appl. Microbiol. Biotechnol. 80 (2008) 71-8.
Reference
6  [PMID:19118348]
  Authors
Case CL, Rodriguez JR, Mukhopadhyay B
  Title
Characterization of an NADH oxidase of the flavin-dependent disulfide reductase family from Methanocaldococcus jannaschii.
  Journal
Microbiology. 155 (2009) 69-79.
  Sequence
[mja:MJ_0649]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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