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Literature summary extracted from

  • Kengen, S.W.; van der Oost, J.; de Vos, W.M.
    Molecular characterization of H2O2-forming NADH oxidases from Archaeoglobus fulgidus (2003), Eur. J. Biochem., 270, 2885-2994.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.6.3.3 2-mercaptoethanol 2 mM, stimulates up to 2fold Archaeoglobus fulgidus
1.6.3.3 dithiothreitol 2 mM, stimulates up to 2fold Archaeoglobus fulgidus
1.6.3.3 FAD flavoprotein, addition of 0.06 mM results in 3.7fold stimulation Archaeoglobus fulgidus
1.6.3.3 FAD flavoprotein, Addition of 0.06 mM results in about 2.5fold stimulation Archaeoglobus fulgidus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.6.3.3 expression in Escherichia coli Archaeoglobus fulgidus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.6.3.3 dithiothreitol 2 mM, rapid decrease in activity to less than 10% of the activity Archaeoglobus fulgidus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.6.3.3 0.011
-
 NADH pH 7.0, 70°C Archaeoglobus fulgidus
1.6.3.3 0.06
-
 O2 pH 7.0, 80°C Archaeoglobus fulgidus
1.6.3.3 0.13
-
 NADH pH 7.0, 80°C Archaeoglobus fulgidus
1.6.3.3 2.9
-
 O2 pH 7.0, 70°C Archaeoglobus fulgidus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.6.3.3 additional information divalent cations are not required for activity Archaeoglobus fulgidus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.6.3.3 48000
-
 2 * 48000, the enzyme exists as a dimer and to some extent as a tetramer, SDS-PAGE Archaeoglobus fulgidus
1.6.3.3 48000
-
 4 * 48000, the enzyme exists as a dimer and to some extent as a tetramer, SDS-PAGE Archaeoglobus fulgidus
1.6.3.3 68000
-
 1 * 68000, the enzyme exists as a monomer and to some extent as a dimer, SDS-PAGE Archaeoglobus fulgidus
1.6.3.3 68000
-
 2 * 68000, the enzyme exists as a monomer and to some extent as a dimer, SDS-PAGE Archaeoglobus fulgidus
1.6.3.3 70000
-
 dimeric enzyme form, gel filtration Archaeoglobus fulgidus
1.6.3.3 94000
-
 dimeric enzyme form, gel filtration Archaeoglobus fulgidus
1.6.3.3 152000
-
 tetrameric enzyme form, gel filtration Archaeoglobus fulgidus
1.6.3.3 178000
-
 tetrameric enzyme form, gel filtration Archaeoglobus fulgidus

Organism

EC Number Organism UniProt Comment Textmining
1.6.3.3 Archaeoglobus fulgidus O29794
-
-
1.6.3.3 Archaeoglobus fulgidus O29985
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.6.3.3
-
 Archaeoglobus fulgidus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.6.3.3 4.05
-
 pH 8.0, 80°C Archaeoglobus fulgidus
1.6.3.3 5.81
-
 pH 8.0, 80°C Archaeoglobus fulgidus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.6.3.3 NADH + H+ + O2 the enzyme predominantly produces H2O2. No activity with NADPH. The enzyme also shows activity with 2,6-dichloroindophenol, ferricyanide, menadione, and 2,3-dimethyl-1,4-naphthoquinone Archaeoglobus fulgidus NAD+ + H2O2
-
 ?
1.6.3.3 NADH + H+ + O2 the enzyme predominantly produces H2O2. No activity with NADPH. The enzyme also shows activity with 2,6-dichloroindophenol, ferricyanide, menadione, and 2,3-dimethyl-1,4-naphthoquinone. Very low activity with cytochrome c Archaeoglobus fulgidus NAD+ + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.6.3.3 dimer 2 * 48000, the enzyme exists as a dimer and to some extent as a tetramer, SDS-PAGE Archaeoglobus fulgidus
1.6.3.3 dimer 2 * 68000, the enzyme exists as a monomer and to some extent as a dimer, SDS-PAGE Archaeoglobus fulgidus
1.6.3.3 monomer 1 * 68000, the enzyme exists as a monomer and to some extent as a dimer, SDS-PAGE Archaeoglobus fulgidus
1.6.3.3 tetramer 4 * 48000, the enzyme exists as a dimer and to some extent as a tetramer, SDS-PAGE Archaeoglobus fulgidus

Synonyms

EC Number Synonyms Comment Organism
1.6.3.3 NoxA-1
-
 Archaeoglobus fulgidus
1.6.3.3 NoxB-1
-
 Archaeoglobus fulgidus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.6.3.3 80
-
-
 Archaeoglobus fulgidus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.6.3.3 60 90 60°C: about 50% of maximal activity, 90°C: about 95% of maximal activity Archaeoglobus fulgidus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.6.3.3 80
-
 half-life: 40 min Archaeoglobus fulgidus
1.6.3.3 80
-
 half-life: 40 h Archaeoglobus fulgidus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.6.3.3 6.5
-
-
 Archaeoglobus fulgidus
1.6.3.3 7
-
 assay at Archaeoglobus fulgidus
1.6.3.3 8
-
-
 Archaeoglobus fulgidus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.6.3.3 5 8 pH 5.0: about 50% of maximal activity, pH 8.0: about 50% of maximal activity Archaeoglobus fulgidus
1.6.3.3 6.5 9 pH 6.5: about 55% of maximal activity, pH 9.0: about 55% of maximal activity Archaeoglobus fulgidus

Cofactor

EC Number Cofactor Comment Organism Structure
1.6.3.3 NADH no activity with NADPH Archaeoglobus fulgidus

Expression

EC Number Organism Comment Expression
1.6.3.3 Archaeoglobus fulgidus expressed constitutively under strictly anaerobic conditions. The fact that the expression of the Nox enzymes is not regulated suggests that they have some fundamental metabolic role, and not an occasional role during oxygen stress additional information

General Information

EC Number General Information Comment Organism
1.6.3.3 physiological function the fact that the expression of the Nox enzymes is not regulated suggests that they have some fundamental metabolic role, and not an occasional role during oxygen stress Archaeoglobus fulgidus