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Literature summary extracted from

  • Yang, X.; Ma, K.
    Characterization of an exceedingly active NADH oxidase from the anaerobic hyperthermophilic bacterium Thermotoga maritima (2007), J. Bacteriol., 189, 3312-3317.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.6.3.3 CuCl2 3 mM, 60% inhibition Thermotoga maritima
1.6.3.3 HgCl2 3 mM, 98% inhibition Thermotoga maritima
1.6.3.3 hydrocortisone 3 mM, 5% inhibition Thermotoga maritima
1.6.3.3 Quinacrine 3 mM, 46% inhibition Thermotoga maritima
1.6.3.3 Quinine 3 mM, 23% inhibition Thermotoga maritima

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.6.3.3 0.042
-
NADH pH 7.8, 80°C Thermotoga maritima
1.6.3.3 0.043
-
O2 pH 7.8, 80°C Thermotoga maritima

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.6.3.3 46000
-
1 * 54000 + 1 * 46000, SDS-PAGE Thermotoga maritima
1.6.3.3 54000
-
1 * 54000 + 1 * 46000, SDS-PAGE Thermotoga maritima
1.6.3.3 90000
-
gel filtration Thermotoga maritima

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.6.3.3 NADH + H+ + O2 Thermotoga maritima an oxygen-removing system present in Thermotoga maritima is proposed to work in two steps: firstly by converting O2 to hydrogen peroxide by the NADH oxidase, and secondly by reducing the hydrogen peroxide to water by an NADH peroxidase or rubrerythrin or alkyl hydroperoxide reductase NAD+ + H2O2
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Organism

EC Number Organism UniProt Comment Textmining
1.6.3.3 Thermotoga maritima
-
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
1.6.3.3 apparently, the enzyme in the cell extract is more resistant to oxygen inactivation than the purified enzyme. Purified enzyme samples exposed to air exhibit a decrease in enzyme activity. The inactivation rate of NADH oxidase activity is dependent on oxygen concentration. The times required for the loss of 50% of the enzyme activity from the purified enzyme are about 20 min and 40 min for oxygen concentrations of 20% (v/v) and 1% (v/v), respectively. However, the times required for the loss of 50% of the enzyme activity from the cell extract aree about 60 min and 360 min for oxygen concentration of 20% (v/v) and 1% (v/v), respectively Thermotoga maritima

Purification (Commentary)

EC Number Purification (Comment) Organism
1.6.3.3 purified under strictly anaerobic conditions Thermotoga maritima

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.6.3.3 144
-
pH 7.0, 80°C Thermotoga maritima

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.6.3.3 NADH + H+ + O2 an oxygen-removing system present in Thermotoga maritima is proposed to work in two steps: firstly by converting O2 to hydrogen peroxide by the NADH oxidase, and secondly by reducing the hydrogen peroxide to water by an NADH peroxidase or rubrerythrin or alkyl hydroperoxide reductase Thermotoga maritima NAD+ + H2O2
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?
1.6.3.3 NADH + H+ + O2 the enzyme is highly specific for NADH, no activity with NADPH. Highest activity using O2 as an electron acceptor. Compared to lower activities for benzyl viologen (20%) and 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB, 7%), while no activity is observed when FAD, FMN, or riboflavin is used as the electron acceptor Thermotoga maritima NAD+ + H2O2
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Subunits

EC Number Subunits Comment Organism
1.6.3.3 dimer 1 * 54000 + 1 * 46000, SDS-PAGE Thermotoga maritima

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.6.3.3 80
-
-
Thermotoga maritima

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.6.3.3 80
-
t1/2: 100 min Thermotoga maritima

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.6.3.3 7
-
at 80°C Thermotoga maritima

Cofactor

EC Number Cofactor Comment Organism Structure
1.6.3.3 FAD flavoprotein. The enzyme contains 1.9 mol of FAD per mol native enzyme Thermotoga maritima
1.6.3.3 NADH the enzyme is highly specific for NADH, no activity with NADPH Thermotoga maritima