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1.1.1.49: glucose-6-phosphate dehydrogenase (NADP+)

This is an abbreviated version!
For detailed information about glucose-6-phosphate dehydrogenase (NADP+), go to the full flat file.

Word Map on EC 1.1.1.49

Reaction

D-glucose 6-phosphate
+
NADP+
=
6-phospho-D-glucono-1,5-lactone
 +
NADPH
 +
H+

Synonyms

6-phosphoglucose dehydrogenase, beta-D-glucose-6-phosphate; NADP oxidoreductase, beta-D-glucose-6-phosphate;NADP oxido-reductase, D-glucose 6-phosphate dehydrogenase, D-glucose 6-phosphate: NADP+ oxidoreductase, D-glucose-6-phosphate: NADP+ oxidoreductase, D-glucose-6-phosphate:NADP oxidoreductase, Entner-Doudoroff enzyme, G-6-PD, G-6-PDH, G-6PD, G6PD, G6PD1, G6PD2, G6PD3, G6PD4, G6PD5, G6PD6, G6PDH, G6PDH-1, G6PDH-2, G6PDH1, G6PDH2, G6PDH3, G6PDH4, G6PDH5, G6PDH6, Glc6PDH, glucose 6-phosphate dehydrogenase, glucose 6-phosphate dehydrogenase (NADP), glucose-6-phosphate 1-dehydrogenase, glucose-6-phosphate dehydrogenase, glucose-6-phosphate dehydrogenase Zwf, glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase, GPD, KlZWF1, NADP-dependent glucose 6-phophate dehydrogenase, NADP-glucose-6-phosphate dehydrogenase, P2-G6PDH, PF14_0511, PfGluPho, plastidial glucose 6-phosphate dehydrogenase, VEG11, Vegetative protein 11, Zwf, zwf-1, Zwf-2, Zwf1p, Zwischenferment

ECTree

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

Engineering

Engineering on EC 1.1.1.49 - glucose-6-phosphate dehydrogenase (NADP+)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K18A
-
the mutant with reduced catalytic efficiency shows 35fold preference for NADP+ over NAD+ as compared to the wild type enzyme (386fold)
K18A/R50A
-
the mutant shows almost no activity
K18T
-
the mutant with reduced catalytic efficiency sshows 35fold preference for NADP+ over NAD+ as compared to the wild type enzyme (386fold)
R50A
-
the mutant with reduced catalytic efficiency shows 50fold preference for NADP+ over NAD+ as compared to the wild type enzyme (386fold)
A44T
-
asymptomatic patient with high in vitro glucose-6-phosphate dehydrogenase deficiency, carrying a inherited mutation at A55T
G163D
mutant is markedly less stable than wild-type G6PD in both thermostability and urea-induced inactivation tests. According to unfolding and refolding experiments, the mutant is impaired in its folding properties. KM-values and turnover numbers are similar to wild-type values
G163S
mutant markedly less stable than wild-type G6PD in both thermostability and urea-induced inactivation tests. According to unfolding and refolding experiments, the mutant is impaired in its folding properties. KM-values and turnover numbers are similar to wild-type values
G488S
-
clinical mutant G6PDFukaya, mutation in the vicinity of the structural NADP+ site, elevated Kd values of the structural NADP+, is denatured by guanidinium hydrochloride and refolded by rapid dilution in the presence of L-Arg, NADP+ and dithiothreitol at 25°C, displays decreased thermostability and high susceptibility to chymotrypsin digestion as compared to the wild-type
G488V
-
clinical mutant G6PDCampinas, mutation in the vicinity of the structural NADP+ site, elevated Kd values of the structural NADP+, is denatured by guanidinium hydrochloride and refolded by rapid dilution in the presence of L-Arg, NADP+ and dithiothreitol at 25°C, displays decreased thermostability and high susceptibility to chymotrypsin digestion as compared to the wild-type
P409R
-
natural occurring point mutation, reconstructed by site-directed mutagenesis, the gene g6pd is highly polymorphic with over 130 mutations identified, reduced activity drastically altered kinetics, and altered tertiary structure, disturbing the binding of NADP+, compared to the wild-type enzyme, reduced thermal stbility
P489S
-
missense mutation associated with severe enzyme deficiency
R393E
-
site-directed mutagenesis, the mutation affects a residue in the dimer interface close to the structural NADP+ site, the mutant activity is slightly reduced compared to the activity of the wild-type enzyme
R393G
R393H
R393I
-
site-directed mutagenesis, the mutation affects a residue in the dimer interface close to the structural NADP+ site, the mutant activity is similar to the activity of the wild-type enzyme
R393L
-
site-directed mutagenesis, the mutation affects a residue in the dimer interface close to the structural NADP+ site, the mutant activity is similar to the activity of the wild-type enzyme
R393V
-
site-directed mutagenesis, the mutation affects a residue in the dimer interface close to the structural NADP+ site, the mutant activity is reduced compared to the activity of the wild-type enzyme
R454C
-
site-directed mutagenesis, the mutant strain overexpresses the clinical enzyme mutants, i.e. Union clone, C1360T, the mutation abolishes a salt bridge between Arg454 and Asp 286, and leads to 10% decreased kcat and activity, Km values for both G6P and NADP+ are decreased approximately 5fold, the mutant shows decreased thermostability
R454H
-
site-directed mutagenesis, the mutant strain overexpresses the clinical enzyme mutants, i.e. Andalus clone, G1361A, the mutation abolishes a salt bridge between Arg454 and Asp 286, and leads to 10% decreased kcat and activity, Km values for both G6P and NADP+ are decreased approximately 5fold, the mutant shows decreased thermostability
K83A
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
K84A
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
L80G
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
R408A
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
A117S/F277I/Q324H/M381I/V443I/S470I
-
t1/2 for the mutant enzyme at 60°C is 95fold higher than the t1/2 value for the wild-type enzyme
A117S/Q324H/M381I/V443I/S470I
-
t1/2 for the mutant enzyme at 60°C is 75fold higher than the t1/2 value for the wild-type enzyme
A117S/Q324H/V443I/S470I
-
t1/2 for the mutant enzyme at 60°C is 13.5fold higher than the t1/2 value for the wild-type enzyme
L99I/A117S/G225S/F277I/Q324H/M381I/V443I/S470I/A476V
-
t1/2 for the mutant enzyme at 60°C is 124 fold higher than the t1/2 value for the wild-type enzyme. 3.4 °C increase in melting temperature (Tm), and a 5 °C increase in optimal temperature (Topt), without compromising the specific activity. The thermostable mutant is conducted to generate hydrogen from maltodextrin via in vitro synthetic biosystems, gaining a more than 8fold improvement of productivity rate with 76% of theoretical yield at 60°C
A117S/F277I/Q324H/M381I/V443I/S470I
-
t1/2 for the mutant enzyme at 60°C is 95fold higher than the t1/2 value for the wild-type enzyme
-
A117S/Q324H/M381I/V443I/S470I
-
t1/2 for the mutant enzyme at 60°C is 75fold higher than the t1/2 value for the wild-type enzyme
-
A117S/Q324H/V443I/S470I
-
t1/2 for the mutant enzyme at 60°C is 13.5fold higher than the t1/2 value for the wild-type enzyme
-
L99I/A117S/G225S/F277I/Q324H/M381I/V443I/S470I/A476V
-
t1/2 for the mutant enzyme at 60°C is 124 fold higher than the t1/2 value for the wild-type enzyme. 3.4 °C increase in melting temperature (Tm), and a 5 °C increase in optimal temperature (Topt), without compromising the specific activity. The thermostable mutant is conducted to generate hydrogen from maltodextrin via in vitro synthetic biosystems, gaining a more than 8fold improvement of productivity rate with 76% of theoretical yield at 60°C
-
additional information