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Literature summary for 1.6.3.3 extracted from

  • Reed, D.W.; Millstein, J.; Hartzell, P.L.
    H(2)O(2)-forming NADH oxidase with diaphorase (cytochrome) activity from Archaeoglobus fulgidus (2001), J. Bacteriol., 183, 7007-7016.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
CHAPS 0.2-0.5%, increases activity about twofold Archaeoglobus fulgidus
n-dodecyl beta-D-maltoside 0.5%, increases activity about twofold Archaeoglobus fulgidus
Triton X-100 0.1-0.5%, increases activity about twofold Archaeoglobus fulgidus
Tween 20 1.25%, increases activity about twofold Archaeoglobus fulgidus

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Archaeoglobus fulgidus

Inhibitors

Inhibitors Comment Organism Structure
CaCl2 10 mM, slightly increases activity Archaeoglobus fulgidus
Cd(CH3CH2COO-)2 10 mM, slightly increases activity Archaeoglobus fulgidus
CoCl2 10 mM, slightly increases activity Archaeoglobus fulgidus
EGTA 10 mM, slightly increases activity Archaeoglobus fulgidus
MnCl2 10 mM, slightly increases activity Archaeoglobus fulgidus
SDS 0.5%, completely inhibits the reaction Archaeoglobus fulgidus
sodium deoxycholate 0.5%, slightly decreases activity Archaeoglobus fulgidus
ZnCl2 10 mM, slightly increases activity Archaeoglobus fulgidus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0031
-
NADH pH 6.6, 55°C Archaeoglobus fulgidus

Metals/Ions

Metals/Ions Comment Organism Structure
CuCl2 10 mM, 3-4fold stimulation Archaeoglobus fulgidus
K3Fe(CN)6 10 mM, 3-4fold stimulation Archaeoglobus fulgidus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
47000
-
x * 47000, SDS-PAGE Archaeoglobus fulgidus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
NADH + H+ + O2 Archaeoglobus fulgidus the enzyme may be involved in electron transfer reactions resulting in sulfate respiration NAD+ + H2O2
-
?

Organism

Organism UniProt Comment Textmining
Archaeoglobus fulgidus O29852
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Archaeoglobus fulgidus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.3
-
pH 6.6, 55°C Archaeoglobus fulgidus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme shows diaphorase activity in the presence of electron acceptors such as tetrazolium and cytochrome c Archaeoglobus fulgidus ?
-
?
NADH + H+ + O2 the enzyme may be involved in electron transfer reactions resulting in sulfate respiration Archaeoglobus fulgidus NAD+ + H2O2
-
?
NADH + H+ + O2 no activity with beta-NADPH Archaeoglobus fulgidus NAD+ + H2O2
-
?

Subunits

Subunits Comment Organism
? x * 47000, SDS-PAGE Archaeoglobus fulgidus

Synonyms

Synonyms Comment Organism
AF0395 assay at Archaeoglobus fulgidus
NoxA2
-
Archaeoglobus fulgidus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
assay at Archaeoglobus fulgidus
80
-
-
Archaeoglobus fulgidus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
22 90 active from room temperature to 90°C. At 50°C, the activity of the recombinant enzyme is half that at 80°C Archaeoglobus fulgidus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
83
-
pH 7.6, 40 min, the half-life of the recombinant enzyme is 12 min, the partially purified native enzyme has a half-life of 35 h Archaeoglobus fulgidus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.6
-
assay at Archaeoglobus fulgidus
7.6
-
-
Archaeoglobus fulgidus

pH Range

pH Minimum pH Maximum Comment Organism
4.4 8.4 pH 4.4: about 70% of maximal activity, pH 8.4: about 90% of maximal activity Archaeoglobus fulgidus

Cofactor

Cofactor Comment Organism Structure
FAD required for activity. 1.1 mol of FAD per mol of enzyme. The FAD cofactor is associated noncovalently with the protein Archaeoglobus fulgidus

General Information

General Information Comment Organism
physiological function the enzyme may be involved in electron transfer reactions resulting in sulfate respiration Archaeoglobus fulgidus