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Literature summary for 1.6.3.4 extracted from

  • Kawasaki, S.; Ishikura, J.; Chiba, D.; Nishino, T.; Niimura, Y.
    Purification and characterization of an H2O-forming NADH oxidase from Clostridium aminovalericum: existence of an oxygen-detoxifying enzyme in an obligate anaerobic bacteria (2004), Arch. Microbiol., 181, 324-330.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
iodoacetate strong inhibition Anaerocolumna aminovalerica
p-chloromercuribenzoate strong inhibition Anaerocolumna aminovalerica
quinacrin strong inhibition Anaerocolumna aminovalerica
Quinine strong inhibition Anaerocolumna aminovalerica

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0192
-
NADH pH 7.0, 25°C Anaerocolumna aminovalerica
0.0619
-
O2 pH 7.0, 25°C Anaerocolumna aminovalerica

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
180000
-
gel filtration Anaerocolumna aminovalerica

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 NADH + H+ + O2 Anaerocolumna aminovalerica the enzyme is involved detoxification of oxygen to water NAD+ + 2 H2O
-
?
2 NADH + H+ + O2 Anaerocolumna aminovalerica NRIC0223 the enzyme is involved detoxification of oxygen to water NAD+ + 2 H2O
-
?

Organism

Organism UniProt Comment Textmining
Anaerocolumna aminovalerica Q2WFW5
-
-
Anaerocolumna aminovalerica NRIC0223 Q2WFW5
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Anaerocolumna aminovalerica

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
130
-
pH 7.0, 37°C Anaerocolumna aminovalerica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 NADH + H+ + O2 the enzyme is involved detoxification of oxygen to water Anaerocolumna aminovalerica NAD+ + 2 H2O
-
?
2 NADH + H+ + O2 the enzyme can catalyze electron transfers from NADH to ferricyanide, 2,6-dichloroindophenol, and menadione, although the activities with these acceptors are extremely low relative to O2. Thus, O2 must be a natural electron acceptor for this enzyme Anaerocolumna aminovalerica NAD+ + 2 H2O
-
?
2 NADH + H+ + O2 the enzyme is involved detoxification of oxygen to water Anaerocolumna aminovalerica NRIC0223 NAD+ + 2 H2O
-
?
2 NADH + H+ + O2 the enzyme can catalyze electron transfers from NADH to ferricyanide, 2,6-dichloroindophenol, and menadione, although the activities with these acceptors are extremely low relative to O2. Thus, O2 must be a natural electron acceptor for this enzyme Anaerocolumna aminovalerica NRIC0223 NAD+ + 2 H2O
-
?

Subunits

Subunits Comment Organism
homotetramer 4 * 4500, SDS-PAGE Anaerocolumna aminovalerica

Synonyms

Synonyms Comment Organism
H2O-forming NADH oxidase
-
Anaerocolumna aminovalerica

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
20 min, stable Anaerocolumna aminovalerica

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
Anaerocolumna aminovalerica

Cofactor

Cofactor Comment Organism Structure
FAD flavoprotein, contains 3–4 mol FAD per mol native enzyme. The NADH oxidase activity is not stimulated by the addition of free flavin adenine dinucleotide (FAD), flavin mononucleotide (FMN), or riboflavin to the reaction mixture (final concentrations were 0.1 mM) Anaerocolumna aminovalerica