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Literature summary for 1.6.3.3 extracted from

  • Hirano, J.; Miyamoto, K.; Ohta, H.
    Purification and characterization of thermostable H2O2-forming NADH oxidase from 2-phenylethanol-assimilating Brevibacterium sp. KU1309 (2008), Appl. Microbiol. Biotechnol., 80, 71-78.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
(NH4)2SO4 250 mM, 10fold activation Brevibacterium sp.
p-chloromercuribenzoate 1 mM, 1.9fold activation Brevibacterium sp.

Application

Application Comment Organism
synthesis regeneration of NAD+ utilizing this enzyme made selective oxidation of mandelic acid or L-phenylalanine possible. This thermostable enzyme is expected to be applicable as a useful biocatalyst for NAD+ recycling Brevibacterium sp.

Inhibitors

Inhibitors Comment Organism Structure
AgNO3 1 mM, 63% inhibition Brevibacterium sp.
CuCl2 1 mM, 58% inhibition Brevibacterium sp.
HgCl2 1 mM, 29% inhibition Brevibacterium sp.
ZnCl2 1 mM, 61% inhibition Brevibacterium sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.022
-
NADH pH 8.8, 25°C Brevibacterium sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Brevibacterium sp. 5737
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
57000
-
2 * 57000, SDS-PAGE Brevibacterium sp.
102000
-
gel filtration Brevibacterium sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
NADH + H+ + O2 Brevibacterium sp. the enzyme is highly specific for NADH, no activity with NADPH NAD+ + H2O2
-
?
NADH + H+ + O2 Brevibacterium sp. KU1309 the enzyme is highly specific for NADH, no activity with NADPH NAD+ + H2O2
-
?

Organism

Organism UniProt Comment Textmining
Brevibacterium sp.
-
-
-
Brevibacterium sp. KU1309
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Brevibacterium sp.

Source Tissue

Source Tissue Comment Organism Textmining
culture condition:2-phenylethanol-grown cell
-
Brevibacterium sp.
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.2
-
pH 8.8, 25°C Brevibacterium sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NADH + H+ + O2 the enzyme is highly specific for NADH, no activity with NADPH Brevibacterium sp. NAD+ + H2O2
-
?
NADH + H+ + O2 the enzyme is highly specific for NADH, no activity with NADPH Brevibacterium sp. KU1309 NAD+ + H2O2
-
?

Subunits

Subunits Comment Organism
dimer 2 * 57000, SDS-PAGE Brevibacterium sp.

Synonyms

Synonyms Comment Organism
H2O2-forming NADH oxidase
-
Brevibacterium sp.
NOX
-
Brevibacterium sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Brevibacterium sp.
70
-
-
Brevibacterium sp.

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 70 activity at 30°C is about 40% of the maximal at 70°C Brevibacterium sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
70
-
1 h, no significant loss of activity Brevibacterium sp.
80
-
1 h, about 30% loss of activity Brevibacterium sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.8
-
assay at Brevibacterium sp.
9
-
-
Brevibacterium sp.

pH Range

pH Minimum pH Maximum Comment Organism
7.9 11 pH 7.8: about 60% of maximal activity, pH 11.0: about 90% of maximal activity Brevibacterium sp.

pH Stability

pH Stability pH Stability Maximum Comment Organism
6 10 1 h, stable Brevibacterium sp.

Cofactor

Cofactor Comment Organism Structure
NADH the enzyme is highly specific for NADH, relative activity with NADPH is 2% compared to the activity with NADH Brevibacterium sp.