The Enzyme Database

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EC 1.6.3.2     
Accepted name: NAD(P)H oxidase (H2O-forming)
Reaction: 2 NAD(P)H + 2 H+ + O2 = 2 NAD(P)+ + 2 H2O
Systematic name: NAD(P)H:oxygen oxidoreductase (H2O-forming)
Comments: A flavoprotein (FAD). NADPH is a better substrate than NADH [1,3]. By removal of oxygen the enzyme is involved in aerobic tolerance in the thermophilic anaerobic archaeon Thermococcus profundus and in Giardia intestinalis, a microaerophilic single-celled parasite of the order Diplomonadida.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Brown, D.M., Upcroft, J.A. and Upcroft, P. A H2O-producing NADH oxidase from the protozoan parasite Giardia duodenalis. Eur. J. Biochem. 241 (1996) 155–161. [DOI] [PMID: 8898901]
2.  Li, L. and Wang, C.C. A likely molecular basis of the susceptibility of Giardia lamblia towards oxygen. Mol. Microbiol. 59 (2006) 202–211. [DOI] [PMID: 16359329]
3.  Jia, B., Park, S.C., Lee, S., Pham, B.P., Yu, R., Le, T.L., Han, S.W., Yang, J.K., Choi, M.S., Baumeister, W. and Cheong, G.W. Hexameric ring structure of a thermophilic archaeon NADH oxidase that produces predominantly H2O. FEBS J. 275 (2008) 5355–5366. [DOI] [PMID: 18959761]
4.  Jia, B., Lee, S., Pham, B.P., Cho, Y.S., Yang, J.K., Byeon, H.S., Kim, J.C. and Cheong, G.W. An archaeal NADH oxidase causes damage to both proteins and nucleic acids under oxidative stress. Mol. Cells 29 (2010) 363–371. [DOI] [PMID: 20213313]
[EC 1.6.3.2 created 2013]
 
 


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