Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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

Reaction

D-glucose 6-phosphate
+
NAD(P)+
=
6-phospho-D-glucono-1,5-lactone
+
NAD(P)H
+
H+

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

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.363 glucose-6-phosphate dehydrogenase [NAD(P)+]

Engineering

Engineering on EC 1.1.1.363 - glucose-6-phosphate dehydrogenase [NAD(P)+]

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D177N
D205C
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
R46C
-
mutant glucose-6-phosphate dehydrogenases with coenzyme specificity that favors NAD+, whereas the wild-type enzyme prefers NADP+ as coenzyme
R46E
-
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
-
the enzyme's Km and Ki values for NADP+ are greatly increased (2-3 orders of magnitude)
T14A
-
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
-
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
-
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
-
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