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Literature summary for 1.6.3.3 extracted from

  • Higuchi, M.; Shimada, M.; Yamamoto, Y.; Hayashi, T.; Koga, T.; Kamio, Y.
    Identification of two distinct NADH oxidases corresponding to H2O2-forming oxidase and H2O-forming oxidase induced in Streptococcus mutans (1993), J. Gen. Microbiol., 139, 2343-2351.
    View publication on PubMed
Search for more literature for 1.6.3.3

Activating Compound

Activating Compound Comment Organism Structure
dithiothreitol 1 mM, slight stimulation to 103% Streptococcus mutans

Inhibitors

Inhibitors Comment Organism Structure
4-chloromercuribenzoate 0.1 mM, 40% inhibition Streptococcus mutans
ascorbate 1 mM, 81% inhibition Streptococcus mutans
Ba2+ 0.1 mM, 86% inhibition Streptococcus mutans
Ca2+ 0.1 mM, about 20% inhibition Streptococcus mutans
Co2+ 0.1 mM, 31% inhibition Streptococcus mutans
Cr2+ 0.1 mM, 49% inhibition Streptococcus mutans
Cu2+ 0.1 mM, complete inhibition Streptococcus mutans
cysteine 1 mM, 54% inhibition Streptococcus mutans
Fe2+ 0.1 mM, 56% inhibition Streptococcus mutans
Hg2+ 0.1 mM, complete inhibition Streptococcus mutans
Mn2+ 0.1 mM, about 20% inhibition Streptococcus mutans
Ni2+ 0.1 mM, 73% inhibition Streptococcus mutans
Sn2+ 0.1 mM, complete inhibition Streptococcus mutans
Zn2+ 0.1 mM, 53% inhibition Streptococcus mutans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.05
-
 NADH 30°C, pH not specified in the publication Streptococcus mutans

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ 0.1 mM, 130% stimulation Streptococcus mutans

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
56000
-
 4 * 56000, SDS-PAGE Streptococcus mutans
220000
-
 gel filtration Streptococcus mutans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
NADH + H+ + O2 Streptococcus mutans Streptococcus mutans NCBI 11723 contains two distinct NADH oxidases, a H2O2-forming and a H2O-forming enzyme NAD+ + H2O2
-
 ?
NADH + H+ + O2 Streptococcus mutans NCBI 11723 Streptococcus mutans NCBI 11723 contains two distinct NADH oxidases, a H2O2-forming and a H2O-forming enzyme NAD+ + H2O2
-
 ?

Organism

Organism UniProt Comment Textmining
Streptococcus mutans O66266
-
-
Streptococcus mutans NCBI 11723 O66266
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Streptococcus mutans

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
37
-
 30°C, pH not specified in the publication Streptococcus mutans

Storage Stability

Storage Stability Organism
-80°C, 6 months, enzyme retains full activity Streptococcus mutans
4°C. pH 7.0, 1 week, activity decreases by 80% Streptococcus mutans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NADH + H+ + O2 Streptococcus mutans NCBI 11723 contains two distinct NADH oxidases, a H2O2-forming and a H2O-forming enzyme Streptococcus mutans NAD+ + H2O2
-
 ?
NADH + H+ + O2 the enzyme is highly specific for NADH, no activity with NADPH Streptococcus mutans NAD+ + H2O2
-
 ?
NADH + H+ + O2 Streptococcus mutans NCBI 11723 contains two distinct NADH oxidases, a H2O2-forming and a H2O-forming enzyme Streptococcus mutans NCBI 11723 NAD+ + H2O2
-
 ?
NADH + H+ + O2 the enzyme is highly specific for NADH, no activity with NADPH Streptococcus mutans NCBI 11723 NAD+ + H2O2
-
 ?

Subunits

Subunits Comment Organism
tetramer 4 * 56000, SDS-PAGE Streptococcus mutans

Synonyms

Synonyms Comment Organism
H2O2-forming NADH oxidase
-
 Streptococcus mutans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
 Streptococcus mutans

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 50 30°C; about 75% of maximal activity, 50°C: about 80% of maximal activity Streptococcus mutans

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
 pH 7.0, 1 h, enzyme retains full activity Streptococcus mutans
55
-
 pH 7.0, 1 h, activity markedly decreases Streptococcus mutans
60
-
 30 min, enzyme retains 5% of its activity Streptococcus mutans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
 Streptococcus mutans

pH Range

pH Minimum pH Maximum Comment Organism
4.5 8 pH 4.5: about 90% of maximal activity, pH 8.0: about 50% of maximal activity Streptococcus mutans

pH Stability

pH Stability pH Stability Maximum Comment Organism
5 8 37°C, 1 h, the enzyme retains full activity at pH 7.0, but activity declines following incubation at either acidic or alkaline pH Streptococcus mutans

Cofactor

Cofactor Comment Organism Structure
FAD contains 1 mol of FAD per monomer Streptococcus mutans
NADH the enzyme is highly specific for NADH, no activity with NADPH Streptococcus mutans

pI Value

Organism Comment pI Value Maximum pI Value
Streptococcus mutans isoelectric focusing
-
 6.6

Expression

Organism Comment Expression
Streptococcus mutans aerobically induced up