1.1.1.47: glucose 1-dehydrogenase [NAD(P)+] This is an abbreviated version! For detailed information about glucose 1-dehydrogenase [NAD(P)+], go to the full flat file .
Reaction
D-glucose +
NAD(P)+ =
D-glucono-1,5-lactone +
NAD(P)H +
H+
Synonyms alkali-resistant glucose 1-dehydrogenase, beta-D-glucose:NAD(P)+ 1-oxido-reductase, beta-D-glucose:NAD(P)+ 1-oxidoreductase, BmGlcDH-III, BmGlcDH-IV, bzgdh, D-glucose dehydrogenase (NAD(P)), EC 1.1.5.2, GDH, gdh-2, GDHB, general stress protein 74, GlcDH, GlcDH-I, GlcDH-II, GlcDH-IWG3, glucose 1-dehydrogenase, glucose 1-dehydrogenase 3, glucose 1-dehydrogenase B, glucose 1-dehydrogenase III, glucose 1-dehydrogenase IV, glucose dehydrogenase, glucose1-dehydrogenase, GluDH, GSP74, hexose phosphate dehydrogenase, hexose-6-phosphate dehydrogenase, LsGDH, More, NAD(P)-dependent glucose 1-dehydrogenase, NAD(P)-dependent glucose dehydrogenase, NAD(P)-dependent glucose-1-dehydrogenase, NAD-GDH, nicotinamide adenine dinucleotide (NAD)-linked glucose dehydrogenase, SsGDH, SSO3204
ECTree
Cofactor
Cofactor on EC 1.1.1.47 - glucose 1-dehydrogenase [NAD(P)+]
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FAD
the catalytic alpha-subunit contains a FAD binding motif at the N-terminal region
additional information
dual cofactor specificity due to presence of Asn215, His217, and the GXGXXA motif
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NAD+
-
-
NAD+
-
completely inactive with NAD+
NAD+
-
NAD+ is more effective as cofactor than NADP+ on all substrates tested
NAD+
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although they can utilize both NAD+ and NADP+: GlcDH-III and GlcDH-IV prefer NAD+, and GlcDH-I and GlcDH-II prefer NADP+
NAD+
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the enzyme is specific for NADP+ and completely inactive with NAD+
NAD+
catalytic efficiency for the reaction with beta-D-glucose and NADP+ (kcat/Km) is 7.8 fold higher compared to catalytic efficiency for the reaction with beta-D-glucose and NAD+
NAD+
kcat/Km of glucose in reaction with NAD+ is about 8fold lower compared to kcat/Km of glucose in the reaction with NADP+
NAD+
the enzyme prefers NAD+ rather than NADP+
NADH
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NADP+
-
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NADP+
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NAD+ is more effective as cofactor than NADP+ on all substrates tested
NADP+
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although they can utilize both NAD+ and NADP+: GlcDH-III and GlcDH-IV prefer NAD+, and GlcDH-I and GlcDH-II prefer NADP+
NADP+
-
the enzyme is specific for NADP+ and completely inactive with NAD+
NADP+
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enzyme is specific for NADP+ and completely inactive with NAD+
NADP+
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about 3times more active with NADP+ than with NAD+
NADP+
GlcDH prefers NADP+ to NAD+ as the cofactor
NADP+
catalytic efficiency for the reaction with beta-D-glucose and NADP+ (kcat/Km) is 7.8 fold higher compared to catalytic efficiency for the reaction with beta-D-glucose and NAD+
NADP+
kcat/Km of glucose in reaction with NADP+ is about 8fold higher compared to kcat/Km of glucose in the reaction with NAD+
NADP+
the enzyme prefers NAD+ rather than NADP+
NADPH
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