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: MJ_0649
MFE: Mefer_0567
MVU: Metvu_1320
MFS: MFS40622_1061
MIF: Metin_1169
MJH: JH146_0868
MIG: Metig_1551
MMP: MMP1259
MMQ: MmarC5_0332
MMX: MmarC6_1414
MMD: GYY_07130
MAE: Maeo_0747
MVO: Mvol_0824
MAC: MA_4636(ndh)
MBAR: MSBR2_0039
MBAK: MSBR3_0021
MMA: MM_1296
MMAC: MSMAC_0018
METM: MSMTP_0021
MTHE: MSTHC_1482
MTHR: MSTHT_1804
MHOR: MSHOH_0020
MBU: Mbur_1767
MMET: MCMEM_0025
MPY: Mpsy_1794
MCJ: MCON_0597
MPD: MCP_2598
MEZ: Mtc_0825(ndh)
RCI: RCIX501(ndh)
MTH: MTH_1354
METC: MTCT_1228
METE: tca_01308(nasD)
MST: Msp_1460
MSI: Msm_0046
MRU: mru_0958(nox)
MEB: Abm4_1204(nox)
MMIL: sm9_1318(nox)
MEYE: TL18_05295
MOL: YLM1_0518
METH: MBMB1_1976
MFC: BRM9_2319(nox)
MCUB: MCBB_2276
MFV: Mfer_0405
MKA: MK0881
MARC: AR505_0212
PHO: PH1509(PH1509)
PAB: PAB1931
PFU: PF1532
PFI: PFC_06890
PYN: PNA2_0095
PYS: Py04_1402
TKO: TK0304
TON: TON_1271
TGA: TGAM_0364(nox)
TSI: TSIB_1323
THA: TAM4_1450
THM: CL1_1373
TLT: OCC_08789
THS: TES1_1046
TNU: BD01_1539
TEU: TEU_04150
PPAC: PAP_07680
KCR: Kcr_1220
BARC: AOA65_1542
 » 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 139:2343-51 (1993)
DOI:10.1099/00221287-139-10-2343
  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 268:5816-23 (2001)
DOI:10.1046/j.0014-2956.2001.02526.x
  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 270:2885-94 (2003)
DOI:10.1046/j.1432-1033.2003.03668.x
  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 189:3312-7 (2007)
DOI:10.1128/JB.01525-06
  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 80:71-8 (2008)
DOI:10.1007/s00253-008-1535-x
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 155:69-79 (2009)
DOI:10.1099/mic.0.024265-0
  Sequence
[mja:MJ_0649]
Other DBs
ExplorEnz - The Enzyme Database: 1.6.3.3
IUBMB Enzyme Nomenclature: 1.6.3.3
ExPASy - ENZYME nomenclature database: 1.6.3.3
BRENDA, the Enzyme Database: 1.6.3.3

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