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Literature summary extracted from

  • Schmidt, H.L.; Stöcklein, W.; Danzer, J.; Kirch, P.; Limbach, B.
    Isolation and properties of an H2O-forming NADH oxidase from Streptococcus faecalis (1986), Eur. J. Biochem., 156, 149-155.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.6.3.4 additional information metal-free enzyme Enterococcus faecalis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.6.3.4 51000
-
 1 * 51000, SDS-PAGE Enterococcus faecalis
1.6.3.4 60000
-
 gel filtration Enterococcus faecalis

Organism

EC Number Organism UniProt Comment Textmining
1.6.3.4 Enterococcus faecalis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.6.3.4
-
 Enterococcus faecalis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.6.3.4 2 NADH + H+ + O2 the enzyme is highly specific for NADH, no activity with NADPH. O2 is the preferred electron acceptor, in addition FAD and, very slowly, one-electron acceptors are reduced. NO formation of H2O2 Enterococcus faecalis NAD+ + 2 H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.6.3.4 monomer 1 * 51000, SDS-PAGE Enterococcus faecalis

Synonyms

EC Number Synonyms Comment Organism
1.6.3.4 H2O-forming NADH oxidase
-
 Enterococcus faecalis

Cofactor

EC Number Cofactor Comment Organism Structure
1.6.3.4 FAD the enzyme contains 1 mol FAD per mol of protein Enterococcus faecalis