Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.6.3.4 extracted from

  • Gao, H.; Tiwari, M.K.; Kang, Y.C.; Lee, J.K.
    Characterization of H2O-forming NADH oxidase from Streptococcus pyogenes and its application in L-rare sugar production (2012), Bioorg. Med. Chem. Lett., 22, 1931-1935.
    View publication on PubMed
Search for more literature for 1.6.3.4

Application

Application Comment Organism
synthesis the enzyme may prove to be useful for NAD+ regeneration in the production rare L--sugars such as L-ribose, L-ribulose, and L-xylulose Streptococcus pyogenes

Cloned(Commentary)

Cloned (Comment) Organism
cloned into the T7 promoter-based plasmid pET28a to give pET28a-SpNox and then heterologously overexpressed in Escherichia coli BL21 (DE3) Streptococcus pyogenes

Protein Variants

Protein Variants Comment Organism
C44A 80% of wild-type activity, production of H2O2 rather than H2O Streptococcus pyogenes
D292A mutant enzyme nearly loses all activity, also loses yellow color, indicating that the amino acid is important for activity Streptococcus pyogenes
G13A mutant enzyme nearly loses all activity, also loses yellow color, indicating that the amino acid is important for activity Streptococcus pyogenes
G169A loses nearly 100% of its activity, indicating that G169 is important for NADH binding Streptococcus pyogenes

Inhibitors

Inhibitors Comment Organism Structure
HgCl2
-
 Streptococcus pyogenes
iodoacetate
-
 Streptococcus pyogenes
p-chloromercuribenzoate
-
 Streptococcus pyogenes
Quinine
-
 Streptococcus pyogenes

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.027
-
 NADH pH and temperature not specified in the publication Streptococcus pyogenes

Metals/Ions

Metals/Ions Comment Organism Structure
additional information the enzyme does not require a metal cofactor for activity Streptococcus pyogenes

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
 2 * 50000, SDS-PAGE Streptococcus pyogenes
100000
-
 gel filtration Streptococcus pyogenes

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 NADH + H+ + O2 Streptococcus pyogenes
-
 NAD+ + 2 H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Streptococcus pyogenes
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Streptococcus pyogenes

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 NADH + H+ + O2
-
 Streptococcus pyogenes NAD+ + 2 H2O
-
 ?
2 NADH + H+ + O2 no production of H2O2 Streptococcus pyogenes NAD+ + 2 H2O
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 50000, SDS-PAGE Streptococcus pyogenes

Synonyms

Synonyms Comment Organism
H2O-forming NADH oxidase
-
 Streptococcus pyogenes
SpNox
-
 Streptococcus pyogenes

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
-
 Streptococcus pyogenes

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 70 30°C: about 75% of maximal activity, 70°C: about 80% of maximal activity Streptococcus pyogenes

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Streptococcus pyogenes

pH Range

pH Minimum pH Maximum Comment Organism
6.5 8.5 higher than 70% of the maximum activity at pH values of 6.5–8.5 Streptococcus pyogenes

Cofactor

Cofactor Comment Organism Structure
FAD contains 0.9 mol of FAD per mol of subunit Streptococcus pyogenes
NADH
-
 Streptococcus pyogenes

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
11000
-
 NADH pH and temperature not specified in the publication Streptococcus pyogenes