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Literature summary 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)

EC Number Cloned (Comment) Organism
1.7.1.6
-
 Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.7.1.6 Al3+ 2 mM, 47.9% residual activity Escherichia coli
1.7.1.6 Cu2+ 2 mM, 84.6% residual activity Escherichia coli
1.7.1.6 Mg2+ 2 mM, 81% residual activity Escherichia coli
1.7.1.6 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
1.7.1.6 sodium dodecylsulfate 1 mM, 53% residual activity Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.7.1.6 0.05
-
 Methyl red pH 7.4, 37°C Escherichia coli
1.7.1.6 0.18
-
 NADH pH 7.4, 37°C Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.7.1.6 27000
-
 x * 27000, SDS-PAGE Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.7.1.6 Escherichia coli
-
-
-
1.7.1.6 Escherichia coli CD-2
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.7.1.6
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.1.6 methyl red + NADH + H+
-
 Escherichia coli ? + NAD+
-
 ?
1.7.1.6 methyl red + NADH + H+
-
 Escherichia coli CD-2 ? + NAD+
-
 ?
1.7.1.6 methyl red + NADPH + H+
-
 Escherichia coli ? + NADP+
-
 ?
1.7.1.6 methyl red + NADPH + H+
-
 Escherichia coli CD-2 ? + NADP+
-
 ?
1.7.1.6 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 ?
-
 ?
1.7.1.6 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

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.7.1.6 37
-
-
 Escherichia coli

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.7.1.6 10 50 more than 75% of maximum activity Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.7.1.6 7.5
-
-
 Escherichia coli

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.7.1.6 5.4 7.5 more than 80% of maximum activity Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.7.1.6 NADH
-
 Escherichia coli
1.7.1.6 NADPH
-
 Escherichia coli