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Literature summary extracted from

  • Ward, D.E.; Donnelly, C.J.; Mullendore, M.E.; van der Oost, J.; de Vos W.M.; Crane, E.J. 3rd.
    The NADH oxidase from Pyrococcus furiosus. Implications for the protection of anaerobic hyperthermophiles against oxidative stress (2001), Eur. J. Biochem., 268, 5816-5823.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.6.3.3 expression in Escherichia coli Pyrococcus furiosus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.6.3.3 additional information
-
 additional information Km for NADH is below 4 mM, whereas the substrate-level FAD-dependent portion of the activity shows a Km for FAD of 0.044 mM. kcat for the oxidase reaction in the absence of substrate-level FAD is 4.8/s, while kcat for the reaction in the presence of substrate-level FAD is 11.1/s Pyrococcus furiosus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.6.3.3 50000
-
 2 * 50000, SDS-PAGE Pyrococcus furiosus
1.6.3.3 97100
-
 gel filtration Pyrococcus furiosus

Organism

EC Number Organism UniProt Comment Textmining
1.6.3.3 Pyrococcus furiosus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.6.3.3
-
 Pyrococcus furiosus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.6.3.3 2 NADH + H+ + O2 the enzyme produces both H2O and H2O2, It is highly specific for NADH, little or no activity with NADPH. NOX1 produces 23% water and 77% H2O2 as products under the assay conditions given Pyrococcus furiosus NAD+ + 2 H2O
-
 ?
1.6.3.3 NADH + H+ + O2 the enzyme produces both H2O and H2O2, It is highly specific for NADH, little or no activity with NADPH. NOX1 produces 23% water and 77% H2O2 as products under the assay conditions given Pyrococcus furiosus NAD+ + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.6.3.3 dimer 2 * 50000, SDS-PAGE Pyrococcus furiosus

Synonyms

EC Number Synonyms Comment Organism
1.6.3.3 NOX1
-
 Pyrococcus furiosus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.6.3.3 75
-
 assay at Pyrococcus furiosus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.6.3.3 7.5
-
 assay at Pyrococcus furiosus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.6.3.3 5.5 8.5 pH 5.5: 73% of maximal activity (50 mM Mes buffer), pH 8.5: 81% of maximal activity (50 mM Mops buffer) Pyrococcus furiosus

Cofactor

EC Number Cofactor Comment Organism Structure
1.6.3.3 FAD flavoprotein. FAD remains enzyme-bound at room temperature. At least 82% of the FAD remains in the enzyme-bound form at 75°C. FMN is not able to substitute for FAD in the substrate-level FAD-dependent portion of the reaction. The Km-value for O2 is above 0.11 mM Pyrococcus furiosus
1.6.3.3 NADH the enzyme is highly specific for NADH, little or no activity with NADPH Pyrococcus furiosus

Expression

EC Number Organism Comment Expression
1.6.3.3 Pyrococcus furiosus transcriptional analysis demonstrates that NOX1 is constitutively expressed regardless of the carbon source and a single promoter is identified 25 bp upstream of the nox1 gene by primer extension additional information

General Information

EC Number General Information Comment Organism
1.6.3.3 physiological function although Pyrococcus furiosus is a strict anaerobe, it may tolerate oxygen to some extent. NOX1 may be involved in the response to oxygen at high temperatures Pyrococcus furiosus