ExplorEnz: EC 1.6.3.3

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1.6.3.3

Accepted name:

NADH oxidase (H₂O₂-forming)

Reaction:

NADH + H⁺ + O₂ = NAD⁺ + H₂O₂

Other name(s):

NOX-1; H₂O₂-forming NADH oxidase

Systematic name:

NADH:oxygen oxidoreductase (H₂O₂-forming)

Comments:

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.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Higuchi, M., Shimada, M., Yamamoto, Y., Hayashi, T., Koga, T. and Kamio, Y. Identification of two distinct NADH oxidases corresponding to H₂O₂-forming oxidase and H₂O-forming oxidase induced in Streptococcus mutans. J. Gen. Microbiol. 139 (1993) 2343–2351. [DOI] [PMID: 8254304]
2.	Ward, D.E., Donnelly, C.J., Mullendore, M.E., van der Oost, J., de Vos, W.M. and Crane, E.J., 3rd. The NADH oxidase from Pyrococcus furiosus. Implications for the protection of anaerobic hyperthermophiles against oxidative stress. Eur. J. Biochem. 268 (2001) 5816–5823. [DOI] [PMID: 11722568]
3.	Kengen, S.W., van der Oost, J. and de Vos, W.M. Molecular characterization of H₂O₂-forming NADH oxidases from Archaeoglobus fulgidus. Eur. J. Biochem. 270 (2003) 2885–2894. [DOI] [PMID: 12823559]
4.	Yang, X. and Ma, K. Characterization of an exceedingly active NADH oxidase from the anaerobic hyperthermophilic bacterium Thermotoga maritima. J. Bacteriol. 189 (2007) 3312–3317. [DOI] [PMID: 17293421]
5.	Hirano, J., Miyamoto, K. and Ohta, H. Purification and characterization of thermostable H₂O₂-forming NADH oxidase from 2-phenylethanol-assimilating Brevibacterium sp. KU1309. Appl. Microbiol. Biotechnol. 80 (2008) 71–78. [DOI] [PMID: 18521590]
6.	Case, C.L., Rodriguez, J.R. and Mukhopadhyay, B. Characterization of an NADH oxidase of the flavin-dependent disulfide reductase family from Methanocaldococcus jannaschii. Microbiology 155 (2009) 69–79. [DOI] [PMID: 19118348]

[EC 1.6.3.3 created 2013]