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Literature summary for 1.6.3.3 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
Search for more literature for 1.6.3.3

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Pyrococcus furiosus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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]

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

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pyrococcus furiosus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
 ?
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

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

Synonyms

Synonyms Comment Organism
NOX1
-
 Pyrococcus furiosus

Temperature Optimum [°C]

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

pH Optimum

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

pH Range

pH Minimum pH Maximum Comment Organism
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

Cofactor Comment Organism Structure
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
NADH the enzyme is highly specific for NADH, little or no activity with NADPH Pyrococcus furiosus

Expression

Organism Comment Expression
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

General Information Comment Organism
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