1.1.1.363: glucose-6-phosphate dehydrogenase [NAD(P)+]
This is an abbreviated version!
For detailed information about glucose-6-phosphate dehydrogenase [NAD(P)+], go to the full flat file.
Word Map on EC 1.1.1.363
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1.1.1.363
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citrate
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mesenteroides
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leuconostoc
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clarias
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batrachus
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4-hydroxy-2-nonenal
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freshwater
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multicatalytic
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catfish
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hne
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hne-treated
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lipogenic
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8-anilino-1-naphthalenesulfonic
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actinomycin
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pentose
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disease-related
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teleost
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synthesis
- 1.1.1.363
- citrate
- mesenteroides
-
leuconostoc
-
clarias
- batrachus
- 4-hydroxy-2-nonenal
-
freshwater
-
multicatalytic
- catfish
- hne
-
hne-treated
-
lipogenic
-
8-anilino-1-naphthalenesulfonic
- actinomycin
- pentose
-
disease-related
-
teleost
- synthesis
Reaction
Synonyms
G6-PDH, G6PD, G6PDH, G6PDH-1, Glc6PD, Glu-6-PDH, glucose 6-phosphate dehydrogenase, glucose-6-phosphate dehydrogenase, glucose-6-phosphate dehydrogenase Zwf, NADP+- and NAD+-dependent G6PDH, PputG6PDH-1, zwf-1
ECTree
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Cofactor
Cofactor on EC 1.1.1.363 - glucose-6-phosphate dehydrogenase [NAD(P)+]
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NAD+
kcat/Km of NADP+ is 9.3fold higher compared to kcat/Km of D-glucose 6-phosphate in NAD+-dependent reaction, kcat/Km of D-glucose 6-phosphate in the NADP+-dependent reaction is 3.5fold higher compared to kcat/Km of D-glucose 6-phosphate in NAD+-dependent reaction. kcat/Km of D-glucose 6-phosphate in the NADP+-dependent reaction is 3.5fold higher compared to kcat/Km of D-glucose 6-phosphate in NAD+-dependent reaction
NAD+
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the maximum quenching of protein fluorescence is 50% for NAD+. The dissociation constant for NAD+ is 2.5 mM
NAD+
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the mechanism with NAD+ is more complex compared to the reaction with D-glucose 6-phosphate and NADP+
NAD+
the NAD+/enzyme complex is half-open. It is suggested that if NAD+ approaches the open form of the enzyme, and this approach generates a conformation change, initially to the half-open form. The concomitant movement of the coenzyme sheet allows Gln47 to approach the adenine ribose 20-hydroxyl and moves away the side chain of Arg46
NADP+
binds to the furthest open form of the enzyme. Of the residues within the coenzyme domain, only Arg46 moves, interacting with the 20-phosphate and adenine. NAD+ is less well defined in the binding site
NADP+
kcat/Km of NADP+ is 9.3fold higher compared to kcat/Km of D-glucose 6-phosphate in NAD+-dependent reaction, kcat/Km of D-glucose 6-phosphate in the NADP+-dependent reaction is 3.5fold higher compared to kcat/Km of D-glucose 6-phosphate in NAD+-dependent reaction. kcat/Km of D-glucose 6-phosphate in the NADP+-dependent reaction is 3.5fold higher compared to kcat/Km of D-glucose 6-phosphate in NAD+-dependent reaction
NADP+
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ordered, sequential mechanism for this reaction in which NADP+ is bound first to the enzyme and NADPH released last
NADP+
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the maximum quenching of protein fluorescence is 5% for NADP+. The dissociation constant for NADP+ is 0.003 mM
NADP+
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wild-type enzyme prefers NADP+ as coenzyme. Arg46 plays a key role in NADP+-binding
NADP+
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NAD+-reducing activity is higher than NADP+-reducing activity