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2,6-dimethyl-1,4-benzoquinone + O2 = ? + H2O2
-
D-glucose + 2,6-dimethyl-1,4-benzoquinone = ?
-
2,6-dimethyl-1,4-benzoquinone + NADPH = 2,6-dimethyl-1,4-benzoquinol + NADP+
-
2,6-dimethyl-1,4-benzoquinone + NADPH + H+ = 2,6-dimethyl-1,4-benzoquinol + NADP+
-
2,6-dimethylbenzoquinone + NADPH = ?
-
2,6-dimethyl-1,4-benzoquinone + NADH = 2,6-dimethyl-1,4-benzoquinol + NAD+
-
2,6-dimethyl-1,4-benzoquinone + NADPH = ?
-
2,6-dimethyl-1,4-benzoquinone + NAD(P)H = 2,6-dimethyl-1,4-benzoquinol + NAD(P)+
-
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0.4
-
pH 6.5, 30°C, recombinant enzyme
8.69
-
substrate 2,6-dimethyl-1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
1.1
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.0077
-
pH 7.5, 25°C, NADPH
2.8
-
pH 7.5, 25°C, NADH
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0.4
-
pH 6.5, 30°C, recombinant enzyme
0.83
-
pH 4.5, substrate: D-glucose
1.59
-
substrate 2,6-dimethyl-1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5
2.1
-
pH 6.5, substrate: D-glucose
0.0016
-
pH 7.5, 25°C, NADPH
0.011
-
pH 7.5, 25°C, NADH
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Expression, purification, and characterization of Mycobacterium tuberculosis mycothione reductase
1999
Patel, M.P.; Blanchard, J.S.
Biochemistry
38
11827-11833
Purification and characterization of pyranose oxidase from the white rot fungus Trametes multicolor
2001
Leitner, C.; Volc, J.; Haltrich, D.
Appl. Environ. Microbiol.
67
3636-3644
Mycobacterium tuberculosis lipoamide dehydrogenase is encoded by Rv0462 and not by the lpdA or lpdB genes
2001
Argyrou, A.; Blanchard, J.S.
Biochemistry
40
11353-11363
Two-electron reduction of quinones by rat liver NAD(P)H:quinone oxidoreductase: quantitative structure-activity relationships
2002
Anusevicius, Z.; Sarlauskas, J.; Cenas, N.
Arch. Biochem. Biophys.
404
254-262
Catalysis of diaphorase reactions by Mycobacterium tuberculosis lipoamide dehydrogenase occurs at the EH4 level
2003
Argyrou, A.; Sun, G.; Palfey, B.A.; Blanchard, J.S.
Biochemistry
42
2218-2228
Characterization of a new member of the flavoprotein disulfide reductase family of enzymes from Mycobacterium tuberculosis
2004
Argyrou, A.; Vetting, M.W.; Blanchard, J.S.
J. Biol. Chem.
279
52694-52702
Pyranose 2-oxidase from Phanerochaete chrysosporium--expression in E. coli and biochemical characterization
2009
Pisanelli, I.; Kujawa, M.; Spadiut, O.; Kittl, R.; Halada, P.; Volc, J.; Mozuch, M.D.; Kersten, P.; Haltrich, D.; Peterbauer, C.
J. Biotechnol.
142
97-106
Antiplasmodial activity of quinones: roles of aziridinyl substituents and the inhibition of Plasmodium falciparum glutathione reductase
2010
Grellier, P.; Maroziene, A.; Nivinskas, H.; Sarlauskas, J.; Aliverti, A.; Cenas, N.
Arch. Biochem. Biophys.
494
32-39
Heterologous expression and biochemical characterization of novel pyranose 2-oxidases from the ascomycetes Aspergillus nidulans and Aspergillus oryzae
2012
Pisanelli, I.; Wuehrer, P.; Reyes-Dominguez, Y.; Spadiut, O.; Haltrich, D.; Peterbauer, C.
Appl. Microbiol. Biotechnol.
93
1157-1166
Reduction of quinones and nitroaromatic compounds by Escherichia coli nitroreductase A (NfsA) Characterization of kinetics and substrate specificity
2017
Valiauga, B.; Williams, E.M.; Ackerley, D.F.; Cenas, N.
Arch. Biochem. Biophys.
614
14-22