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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
1.6.3.3
722311
Streptococcus mutans H2O2-forming NADH oxidase is an alkyl hydroperoxide reductase protein
Free Radic. Biol. Med.
28
108-120
2000
Streptococcus mutans
10656297
1.6.3.3
721855
Molecular cloning and sequence analysis of the gene encoding the H2O2-forming NADH oxidase from Streptococcus mutans
Biosci. Biotechnol. Biochem.
58
1603-1607
1994
Streptococcus mutans
7765479
1.6.3.3
721855
Molecular cloning and sequence analysis of the gene encoding the H2O2-forming NADH oxidase from Streptococcus mutans
Biosci. Biotechnol. Biochem.
58
1603-1607
1994
Streptococcus mutans NCBI 11723
7765479
1.6.3.3
722881
Identification of two distinct NADH oxidases corresponding to H2O2-forming oxidase and H2O-forming oxidase induced in Streptococcus mutans
J. Gen. Microbiol.
139
2343-2351
1993
Streptococcus mutans
8254304
1.6.3.3
722881
Identification of two distinct NADH oxidases corresponding to H2O2-forming oxidase and H2O-forming oxidase induced in Streptococcus mutans
J. Gen. Microbiol.
139
2343-2351
1993
Streptococcus mutans NCBI 11723
8254304
1.6.3.3
722179
Molecular characterization of H2O2-forming NADH oxidases from Archaeoglobus fulgidus
Eur. J. Biochem.
270
2885-2994
2003
Archaeoglobus fulgidus
12823559
1.6.3.3
721957
Discovery and characterization of a thermostable NADH oxidase from Pyrococcus horikoshii OT3
Bull. Korean Chem. Soc.
30
2984-2988
2009
Pyrococcus horikoshii
-
1.6.3.3
721957
Discovery and characterization of a thermostable NADH oxidase from Pyrococcus horikoshii OT3
Bull. Korean Chem. Soc.
30
2984-2988
2009
Pyrococcus horikoshii OT-3
-
1.6.3.3
721455
Purification and characterization of an NADH oxidase from extremely thermophilic anaerobic bacterium Thermotoga hypogea
Arch. Microbiol.
183
331-337
2005
Pseudothermotoga hypogea
15912375
1.6.3.3
721455
Purification and characterization of an NADH oxidase from extremely thermophilic anaerobic bacterium Thermotoga hypogea
Arch. Microbiol.
183
331-337
2005
Pseudothermotoga hypogea DSM 11164
15912375
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