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
Advanced search results
Engineering
Engineering on EC 1.1.1.363 - glucose-6-phosphate dehydrogenase [NAD(P)+]
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D177N
D205C
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enzyme variant with cysteine close to the dimer interface, about 30% loss of specific activity compared to wild-type enzyme shows changes in activity and the efficacy of immobilization.
D374Q
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kcat/Km for D-glucose 6-phosphate is 7.7fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 7.3fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 12.2fold lower compared to kcat/KM of wild-type enzyme
D453C
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enzyme variant with cysteine far from the active center, no significant loss in specific activity compared to wild-type enzyme, in contrast to wild-type enzyme, the mutant enzyme is readily immobilited
H178N
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kcat/KM for D-glucose 6-phosphate (with cosubstrate NADP+) is fold lower than the value for the wild-type enzyme, kcat/KM for NADP+ is fold lower than the value for the wild-type enzyme, kcat/KM for D-glucose 6-phosphate (with cosubstrate NAD) is fold lower than the value for the wild-type enzyme, kcat/KM for D-glucose 6-phosphate (with cosubstrate NAD+) is fold lower than the value for the wild-type enzyme
H250N
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kcat/KM for D-glucose 6-phosphate (with cosubstrate NADP+) is fold lower than the value for the wild-type enzyme, kcat/KM for NADP+ is fold lower than the value for the wild-type enzyme, kcat/KM for D-glucose 6-phosphate (with cosubstrate NAD) is fold lower than the value for the wild-type enzyme, kcat/KM for D-glucose 6-phosphate (with cosubstrate NAD+) is fold lower than the value for the wild-type enzyme
K182Q
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kcat/Km for D-glucose 6-phosphate is 127fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 1.1fold higher compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 1.4fold lower compared to kcat/KM of wild-type enzyme
K182R
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kcat/Km for D-glucose 6-phosphate is 81fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 1.1fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 1.6fold lower compared to kcat/KM of wild-type enzyme
K21Q
kcat/Km for D-glucose 6-phosphate in the NADP+-dependent reaction is 76.2fold lower compared to wild-type value, kcat/Km for D-glucose 6-phosphate in the NAD+-dependent reaction is 28.5fold lower compared to wild-type value
K21R
kcat/Km for D-glucose 6-phosphate in the NADP+-dependent reaction is 1.9fold lower compared to wild-type value, kcat/Km for D-glucose 6-phosphate in the NAD+-dependent reaction is 1.4fold lower compared to wild-type value
K343Q
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kcat/Km for D-glucose 6-phosphate is 445fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 2.7fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 2.6fold lower compared to kcat/KM of wild-type enzyme
K343R
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kcat/Km for D-glucose 6-phosphate is 23fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 1.2fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 2fold lower compared to kcat/KM of wild-type enzyme
L218C
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enzyme variant with cysteine close to the active center, about 30% loss of specific activity compared to wild-type enzyme, the mutant enzyme shows almost complete immobilization but poor carrier activity
P149G
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kcat/Km for D-glucose 6-phosphate is 890fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 120fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 448fold lower compared to kcat/KM of wild-type enzyme
P149V
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kcat/Km for D-glucose 6-phosphate is 5933fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 1265fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 3843fold lower compared to kcat/KM of wild-type enzyme
Q47A
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kcat/Km for D-glucose 6-phosphate is 1.1fold higher compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 1.3fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 1.8fold lower compared to kcat/KM of wild-type enzyme
Q47E
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kcat/Km for D-glucose 6-phosphate is 1.3fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 6.4fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 1.7fold lower compared to kcat/KM of wild-type enzyme
R46A
R46C
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mutant glucose-6-phosphate dehydrogenases with coenzyme specificity that favors NAD+, whereas the wild-type enzyme prefers NADP+ as coenzyme
R46E
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kcat/Km for D-glucose 6-phosphate is 4.8fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 1406fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 6.7fold lower compared to kcat/KM of wild-type enzyme
R46Q
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the enzyme's Km and Ki values for NADP+ are greatly increased (2-3 orders of magnitude)
T14A
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kcat/Km for D-glucose 6-phosphate is 1.8fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 5.7fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 12.8fold lower compared to kcat/KM of wild-type enzyme
T14S
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kcat/Km for D-glucose 6-phosphate is 1.1fold higher compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 1.6fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 1.5fold lower compared to kcat/KM of wild-type enzyme
Y179F
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kcat/Km for D-glucose 6-phosphate is 4.9fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 2.2fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 1.7fold lower compared to kcat/KM of wild-type enzyme
Y415F
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kcat/Km for D-glucose 6-phosphate is 1.2fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 1.4fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 1.6fold lower compared to kcat/KM of wild-type enzyme
absence of a negatively charged aspartate at 177 accounts for the decrease in catalytic activity at pH 7.8
D177N
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kcat/KM for D-glucose 6-phosphate (with cosubstrate NADP+) is fold lower than the value for the wild-type enzyme, kcat/KM for NADP+ is fold lower than the value for the wild-type enzyme, kcat/KM for D-glucose 6-phosphate (with cosubstrate NAD) is fold lower than the value for the wild-type enzyme, kcat/KM for D-glucose 6-phosphate (with cosubstrate NAD+) is fold lower than the value for the wild-type enzyme
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mutant glucose-6-phosphate dehydrogenases with coenzyme specificity that favors NAD+, whereas the wild-type enzyme prefers NADP+ as coenzyme
R46A
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the enzyme's Km and Ki values for NADP+ are greatly increased (2-3 orders of magnitude)