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Literature summary for 1.7.1.6 extracted from

  • Cui, D.; Li, G.; Zhao, D.; Gu, X.; Wang, C.; Zhao, M.
    Purification and characterization of an azoreductase from Escherichia coli CD-2 possessing quinone reductase activity (2012), Process Biochem., 47, 544-549.
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Al3+ 2 mM, 47.9% residual activity Escherichia coli
Cu2+ 2 mM, 84.6% residual activity Escherichia coli
Mg2+ 2 mM, 81% residual activity Escherichia coli
additional information changes in salinity from 0 to 2% do not affect the activity of the enzyme very much. After a 1-h incubation, more than 80% relative activity is indicated at 0-5% salt concentrations Escherichia coli
sodium dodecylsulfate 1 mM, 53% residual activity Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.05
-
Methyl red pH 7.4, 37°C Escherichia coli
0.18
-
NADH pH 7.4, 37°C Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
27000
-
x * 27000, SDS-PAGE Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli CD-2
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
methyl red + NADH + H+
-
Escherichia coli ? + NAD+
-
?
methyl red + NADH + H+
-
Escherichia coli CD-2 ? + NAD+
-
?
methyl red + NADPH + H+
-
Escherichia coli ? + NADP+
-
?
methyl red + NADPH + H+
-
Escherichia coli CD-2 ? + NADP+
-
?
additional information enzyme additionally shows quinone reductase activity. When NAD(P)H is used as an electron donor, the purified enzyme can reduce menadione effectively with a quinone reductase activity of approximately 3.4 U ml-1 Escherichia coli ?
-
?
additional information enzyme additionally shows quinone reductase activity. When NAD(P)H is used as an electron donor, the purified enzyme can reduce menadione effectively with a quinone reductase activity of approximately 3.4 U ml-1 Escherichia coli CD-2 ?
-
?

Subunits

Subunits Comment Organism
? x * 27000, SDS-PAGE Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
Escherichia coli

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
10 50 more than 75% of maximum activity Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
5.4 7.5 more than 80% of maximum activity Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NADH
-
Escherichia coli
NADPH
-
Escherichia coli