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

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
1.1.1.49
-
RECOMMENDED NAME
GeneOntology No.
glucose-6-phosphate dehydrogenase (NADP+)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-glucose 6-phosphate + NADP+ = 6-phospho-D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
-
-
-
-
D-glucose 6-phosphate + NADP+ = 6-phospho-D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
sequential mechanism
-
D-glucose 6-phosphate + NADP+ = 6-phospho-D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
reaction mechanism is important for regulation
-
D-glucose 6-phosphate + NADP+ = 6-phospho-D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
rapid equilibrium ordered bi bi kinetic
-
D-glucose 6-phosphate + NADP+ = 6-phospho-D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
physiological regulating function is discussed
-
D-glucose 6-phosphate + NADP+ = 6-phospho-D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
rapid-equilibrium random-order mechanism
-
D-glucose 6-phosphate + NADP+ = 6-phospho-D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
rapid equilibrium random bi bi kinetic mechanism
-
D-glucose 6-phosphate + NADP+ = 6-phospho-D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
ternary-complex mechanism
-
D-glucose 6-phosphate + NADP+ = 6-phospho-D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
the adult kidney cortex enzyme shows a ping pong bi bi kinetic mechanism, while the lamb kidney enzyme obeys an ordered bi bi mechanism, thus the kinetic mechanism alters due to aging
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidation
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
formaldehyde oxidation I
-
-
Glutathione metabolism
-
-
heterolactic fermentation
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
NAD/NADP-NADH/NADPH cytosolic interconversion (yeast)
-
-
Pentose phosphate pathway
-
-
pentose phosphate pathway
-
-
pentose phosphate pathway (oxidative branch)
-
-
superpathway of glycolysis and Entner-Doudoroff
-
-
SYSTEMATIC NAME
IUBMB Comments
D-glucose-6-phosphate:NADP+ 1-oxidoreductase
The enzyme catalyses a step of the pentose phosphate pathway. The enzyme is specific for NADP+. cf. EC 1.1.1.363, glucose-6-phosphate dehydrogenase [NAD(P)+].
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6-phosphoglucose dehydrogenase
-
-
-
-
D-glucose 6-phosphate dehydrogenase
-
-
-
-
D-glucose 6-phosphate: NADP+ oxidoreductase
-
-
D-glucose-6-phosphate: NADP+ oxidoreductase
-
-
D-glucose-6-phosphate:NADP oxidoreductase
-
-
D-glucose-6-phosphate:NADP oxidoreductase
Bacillus megaterium QM Bl551
-
-
-
Entner-Doudoroff enzyme
-
-
-
-
G-6-PD
-
-
G6PD
-
-
-
-
G6PD
-
-
G6PD
-
-
G6PD
G1EHI3
-
G6PD
P11413
-
G6PD
Meyerozyma guilliermondii FTI 20037
-
-
-
G6PD1
-
-
-
-
G6PD1
Q43727
-
G6PD1
Arabidopsis thaliana T87
Q43727
-
-
G6PD2
-
-
-
-
G6PD2
Q9FY99
-
G6PD2
Arabidopsis thaliana T87
Q9FY99
-
-
G6PD3
-
-
-
-
G6PD3
Q8L743
-
G6PD3
Arabidopsis thaliana T87
Q8L743
-
-
G6PD4
-
-
-
-
G6PD4
Q93ZW0
-
G6PD4
Arabidopsis thaliana T87
Q93ZW0
-
-
G6PD5
-
-
-
-
G6PD5
Q9LK23
-
G6PD5
Arabidopsis thaliana T87
Q9LK23
-
-
G6PD6
-
-
-
-
G6PD6
Q9FJI5
-
G6PD6
Arabidopsis thaliana T87
Q9FJI5
-
-
G6PDH
Q43727
-
G6PDH
Q93ZW0, Q9FJI5, Q9FY99, Q9LK23
-
G6PDH
Arabidopsis thaliana T87
Q43727, Q8L743, Q93ZW0, Q9FJI5, Q9FY99, Q9LK23
-
-
G6PDH
-
-
G6PDH
-
-
G6PDH
Pseudomonas fluorescens 13525
-
-
-
G6PDH
Saccharomyces cerevisiae W303-181
-
-
-
G6PDH
-
-
G6PDH
Trypanosoma brucei 427
-
-
-
G6PDH
Q1WBU6
-
G6PDH1
-
-
-
-
G6PDH1
Q43727
-
G6PDH2
-
-
-
-
G6PDH3
-
-
-
-
G6PDH4
-
-
-
-
G6PDH5
-
-
-
-
G6PDH6
-
-
-
-
Glc6PDH
-
-
glucose 6-phosphate dehydrogenase
-
-
glucose 6-phosphate dehydrogenase
-
-
glucose 6-phosphate dehydrogenase
-
-
glucose 6-phosphate dehydrogenase
-
-
glucose 6-phosphate dehydrogenase
-
-
glucose 6-phosphate dehydrogenase
-
-
glucose 6-phosphate dehydrogenase
Pseudomonas fluorescens 13525
-
-
-
glucose 6-phosphate dehydrogenase
-
-
glucose 6-phosphate dehydrogenase
-
-
glucose 6-phosphate dehydrogenase
Saccharomyces cerevisiae W303-181
-
-
-
glucose 6-phosphate dehydrogenase (NADP)
-
-
-
-
glucose-6-phosphate 1-dehydrogenase
-
-
-
-
glucose-6-phosphate dehydrogenase
-
-
-
-
glucose-6-phosphate dehydrogenase
-
-
glucose-6-phosphate dehydrogenase
-
-
glucose-6-phosphate dehydrogenase
-
-
glucose-6-phosphate dehydrogenase
-
-
glucose-6-phosphate dehydrogenase
-
-
glucose-6-phosphate dehydrogenase
-
-
glucose-6-phosphate dehydrogenase
-
-
glucose-6-phosphate dehydrogenase
-
-
glucose-6-phosphate dehydrogenase
Moniliella megachiliensis SN-G42
-
-
-
glucose-6-phosphate dehydrogenase
-
-
glucose-6-phosphate dehydrogenase
-
-
glucose-6-phosphate dehydrogenase
-
-
glucose-6-phosphate dehydrogenase
Pseudomonas aeruginosa P4
-
-
-
glucose-6-phosphate dehydrogenase
-
-
glucose-6-phosphate dehydrogenase
-
-
glucose-6-phosphate dehydrogenase
-
-
glucose-6-phosphate dehydrogenase
-
-
glucose-6-phosphate dehydrogenase
-
-
glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase
-
-
NADP-dependent glucose 6-phophate dehydrogenase
-
-
-
-
NADP-glucose-6-phosphate dehydrogenase
-
-
-
-
NADP-glucose-6-phosphate dehydrogenase
-
-
NADP-glucose-6-phosphate dehydrogenase
Bacillus megaterium QM Bl551
-
-
-
VEG11
-
-
-
-
Vegetative protein 11
-
-
-
-
Zwischenferment
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9001-40-5
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene gsdA
-
-
Manually annotated by BRENDA team
Arabidopsis thaliana T87
strain T87
UniProt
Manually annotated by BRENDA team
filamentous fungus isolated from infected tongue of a human patient
-
-
Manually annotated by BRENDA team
strain ATCC 19213
-
-
Manually annotated by BRENDA team
strain QM Bl551
-
-
Manually annotated by BRENDA team
Bacillus megaterium QM Bl551
strain QM Bl551
-
-
Manually annotated by BRENDA team
Chalcalburnus tarischii
1811
-
-
Manually annotated by BRENDA team
Chalcalburnus tarischii 1811
1811
-
-
Manually annotated by BRENDA team
; high-level glucose-6-phosphate dehydrogenase strain
-
-
Manually annotated by BRENDA team
Escherichia coli DF82
high-level glucose-6-phosphate dehydrogenase strain
-
-
Manually annotated by BRENDA team
Escherichia coli K-10
-
-
-
Manually annotated by BRENDA team
2 isoenzymes
-
-
Manually annotated by BRENDA team
2 isoforms: A(+) and A(-), where A(-) is a mutant derivative of A(+) with V68M exchange
-
-
Manually annotated by BRENDA team
asymptomatic patient with high in vitro glucose-6-phosphate dehydrogenase deficiency, carrying a inherited mutation at A55T
-
-
Manually annotated by BRENDA team
wild-type and 3 enzyme-deficient children, i.e. mutants 1,2, and 3
-
-
Manually annotated by BRENDA team
wild-type and deficient mutant
-
-
Manually annotated by BRENDA team
X-linked house-keeping enzyme
-
-
Manually annotated by BRENDA team
var. Alfeo, root plastidic isozyme
-
-
Manually annotated by BRENDA team
isolated from a sea water sample collected at the Terra Nova Bay, Ross Sea, Antarctica
-
-
Manually annotated by BRENDA team
strain FTI 20037
-
-
Manually annotated by BRENDA team
Meyerozyma guilliermondii FTI 20037
strain FTI 20037
-
-
Manually annotated by BRENDA team
strain SN-G42 and 124A
-
-
Manually annotated by BRENDA team
Moniliella megachiliensis SN-G42
strain SN-G42 and 124A
-
-
Manually annotated by BRENDA team
var. Samsun, resistant SNN cultivar and susceptible Xanthi cultivar
-
-
Manually annotated by BRENDA team
Penicillium duponti
-
-
-
Manually annotated by BRENDA team
L. cv. Lincoln
-
-
Manually annotated by BRENDA team
strain P4 (soil-isolate)
-
-
Manually annotated by BRENDA team
Pseudomonas aeruginosa P4
strain P4 (soil-isolate)
-
-
Manually annotated by BRENDA team
strain 13525
-
-
Manually annotated by BRENDA team
strain ATCC 13525
-
-
Manually annotated by BRENDA team
Pseudomonas fluorescens 13525
strain 13525
-
-
Manually annotated by BRENDA team
female Wistar rats
-
-
Manually annotated by BRENDA team
male sprague-dawley rats
-
-
Manually annotated by BRENDA team
male Wistar rats
-
-
Manually annotated by BRENDA team
male Wister strain albino rats
-
-
Manually annotated by BRENDA team
Sprague-Dawley rats
-
-
Manually annotated by BRENDA team
strain W303-181, constitutive enzyme
-
-
Manually annotated by BRENDA team
W303-181, having the plasmid YEpPGK-G6P (built by coupling the vector YEPLAC 181 with the promoter phosphoglycerate kinase 1)
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae W303-181
strain W303-181, constitutive enzyme
-
-
Manually annotated by BRENDA team
4 weeks-old plants, isozymes in plastid, P1 and P2, and cytosol
-
-
Manually annotated by BRENDA team
2 isoenzymes
-
-
Manually annotated by BRENDA team
gene g6pd
-
-
Manually annotated by BRENDA team
427 strain
-
-
Manually annotated by BRENDA team
Trypanosoma brucei 427
427 strain
-
-
Manually annotated by BRENDA team
strains Tulahuen 2 and Y
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
high glucose level of 25 mM leads to a decrease in G6PD activity and protein level in islets. Inhibition of G6PD with siRNA leads to increase in reactive oxygen species and apoptosis, decreased proliferation, and impaired insulin secretion. High glucose level decreases insulin secretion, which is improved by overexpressing G6PD
metabolism
-
rate-limiting enzyme of the pentose-phosphate pathway
metabolism
-
regulatory enzyme of the pentose phosphate pathway
physiological function
-
part of pentose phosphate pathway
physiological function
-
G6PD-deficient mice have smaller islets and impaired glucose tolerance compared with control mice, which suggests that G6PD deficiency per se leads to beta-cell dysfunction and death
physiological function
Moniliella megachiliensis SN-G42
-
part of pentose phosphate pathway
-
metabolism
-
the bifunctional glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase enzyme catalyzes the first and second steps in the parasite's pentose phosphate pathway, cf. EC 3.1.1.31
additional information
-
development and optimization of a specific colorimetric assay whereby the NADPH generated reduces the tetrazolium salt WST-1, i.e 2-(4-indophenyl)-3-(4-nitrophenyl)-5-(2,4-disulfophenyl-2H tetrazolium), to water-soluble yellow-colored formazan with 1-methoxy-5-methylphenazium methylsulfate as an electron carrier
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-deoxy-D-glucose 6-phosphate + NAD(P)+
2-deoxy-D-glucono-1,5-lactone 6-phosphate + NAD(P)H
show the reaction diagram
-
low activity
-
-
?
2-deoxy-D-glucose 6-phosphate + NADP+
2-deoxy-D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
-
-
-
?
2-deoxy-D-glucose 6-phosphate + NADP+
2-deoxy-D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
wild-type and mutant P409R, below 10% activity compared to D-glucose 6-phosphate
-
-
?
2-deoxy-D-glucose-6-phosphate + NADP+
2-deoxy-D-gluconate 6-phosphate + NADPH
show the reaction diagram
-
-
-
-
?
6-phosphonogluconate + NADPH
?
show the reaction diagram
-
isoenzyme II
-
-
?
D-galactose 6-phosphate + NAD(P)+
D-galactonate 6-phosphate + NADH
show the reaction diagram
-
-
-
-
?
D-galactose 6-phosphate + NAD(P)+
D-galactonate 6-phosphate + NADH
show the reaction diagram
-
-
-
-
?
D-glucose + NAD(P)+
D-gluconate + NAD(P)H
show the reaction diagram
-
activity only with dimethylsulfoxide added by 40% (v/v)
-
-
?
D-glucose 6-phosphate + deamino-NADP+
D-glucono-1,5-lactone 6-phosphate + deamino-NADPH
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + deamino-NADP+
?
show the reaction diagram
-
-
-
-
-
D-glucose 6-phosphate + deamino-NADP+
?
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
-
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
ir
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
glucono-delta-lactone-6-phosphate
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
?, ir
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
Penicillium duponti
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
sigmoidal relationship in cofactor binding
-
-
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
isoform A(-) shows sigmoidal enzyme-substrate interaction, isoform A(+) shows hyperbolic enzyme-substrate interaction
D-glucose-delta-lactone 6-phosphate
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
hyperbolic cofactor binding
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
Schizosaccharomyces pombe NCYC 132S2-2
-
-
-
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
Pseudomonas sp. W5
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + NAD(P)+
D-glucono-1,5-lactone 6-phosphate + NAD(P)H
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NAD(P)+
D-glucono-1,5-lactone 6-phosphate + NAD(P)H
show the reaction diagram
-
key enzyme catalyzing the first step of the pentose phosphate pathway generating NADPH for anabolic metabolsim pathways and protection systems in the liver
-
-
?
D-glucose 6-phosphate + NAD+
D-glucono-1,5-lactone 6-phosphate + NADH + H+
show the reaction diagram
-
-
-
-
-
D-glucose 6-phosphate + NAD+
D-glucono-1,5-lactone 6-phosphate + NADH + H+
show the reaction diagram
-
-
-
-
-
D-glucose 6-phosphate + NAD+
D-glucono-1,5-lactone 6-phosphate + NADH + H+
show the reaction diagram
-
-
-
-
-
D-glucose 6-phosphate + NAD+
D-glucono-1,5-lactone 6-phosphate + NADH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NAD+
D-glucono-1,5-lactone 6-phosphate + NADH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
show the reaction diagram
-
NADP+-specific enzyme. In presence of NAD+ 410fold reduction in the performance of the enzyme
-
-
?
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
show the reaction diagram
Escherichia coli K-10, Escherichia coli DF82
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
Q43727
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
Q43727, Q8L743, Q93ZW0, Q9FJI5, Q9FY99, Q9LK23
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
Q8L743
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
catalyzes the first step of the pentose phosphate pathway, enzyme deficiency often causes hemolytic anaemia
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
differential regulation of isozymes, the cytosolic enzyme is regulated by sugar availability at transcriptional level, while the plastidic isozymes are regulated by redox mechanism
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
enzyme catalyzes the first step of the pentose phosphate pathway
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
involved in oxidative pentose phosphate pathway in roots, related to glutamate synthesis in the plastids
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
key enzyme catalyzing the first step in the pentose phosphate pathway
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
key enzyme catalyzing the first step of the hexose monophosphate shunt pathway
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
key enzyme of the pentose phosphate pathway
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
key regulatory enzyme of the pentose phosphate pathway, regulation mechanism study
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
wild-type and mutant P409R
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
first step in the pentose phosphate pathway
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
G6PDH is the rate-limiting step in the formation of NADPH via the triphosphate, and is responsible for the major supply of NADPH in the cell
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
inhibition by divalent metal ions, at low NADPH /NADP+ ratio, is another means of controlling the pentose phosphate pathway, the substrate specificity is extremely strict
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
Arabidopsis thaliana T87
Q43727, Q8L743, Q93ZW0, Q9FJI5, Q9FY99, Q9LK23
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
Meyerozyma guilliermondii FTI 20037
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
Pseudomonas fluorescens 13525
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
Trypanosoma brucei 427
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
show the reaction diagram
P11413
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
show the reaction diagram
Q1WBU6
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
show the reaction diagram
G1EHI3
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
show the reaction diagram
-
oxidative enzyme of pentose phosphate pathway
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
show the reaction diagram
-
random bi bi sequential mechanism in rapid equilibrium
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
show the reaction diagram
Pseudomonas aeruginosa P4
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-gluconate 6-phosphate + NADPH
show the reaction diagram
Q43727, Q8L743, Q93ZW0, Q9FJI5, Q9FY99, Q9LK23
-
-
-
?
D-glucose 6-phosphate + NADP+
D-gluconate 6-phosphate + NADPH
show the reaction diagram
Arabidopsis thaliana T87
Q43727, Q8L743, Q93ZW0, Q9FJI5, Q9FY99, Q9LK23
-
-
-
?
D-glucose 6-phosphate + NADP+
NADPH + ?
show the reaction diagram
-
assay at pH 7.4
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
-
first enzyme of the pentose phosphate pathway, one of the main sources of NADPH
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
-
oxidative pentose pathway
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
-
the enzyme is involved pentose biosynthesis
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
-
NADP+-specific enzyme. In presence of NAD+ 410fold reduction in the performance of the enzyme. Modeling of the sensitivity of reduced cofactor production by G6PDH as a function of the redox ratios of NAD/NADH (rRNAD) and NADP/NADPH (rRNADP). NADPH production sharply increases within the range of thermodynamically feasible values of rRNADP, but NADH production remains low within the range feasible for rRNAD
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
Escherichia coli K-10, Escherichia coli DF82
-
-
-
-
?
D-glucose 6-phosphate + NADP+ + H2O
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+ + H2O
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+ + H2O
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+ + H2O
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
the enzyme is responsible for the production of NADPH, which is required for biosynthetic reactions and protection of cells from free radicals
-
-
?
D-glucose 6-phosphate + NADP+ + H2O
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
Saccharomyces cerevisiae W303-181
-
-
-
-
?
D-glucose 6-phosphate + thio-NAD(P)+
D-glucono-1,5-lactone 6-phosphate + thio-NAD(P)H
show the reaction diagram
-
the thio-cofactors give increased activity compared to the non-thio-cofactors
-
-
?
deoxy-D-glucose 6-phosphate + NADP+
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
both isoenzymes show no activity with glucose and NAD+, isoenzyme I shows no activity with 6-phosphonogluconate
-
-
-
additional information
?
-
-
no activity with glucose, glucose 1-phosphate, 2-deoxyglucose 6-phosphate, fructose, fructose 6-phosphate, fructose 1,6-diphosphate, mannose, galactose 6-phosphate, NAD+
-
-
-
additional information
?
-
-
no activity with D-glucose, D-ribose, D-fructose-6-phosphate, D-ribose-5-phosphate
-
-
-
additional information
?
-
-
physiological regulation of NADP+-NADPH-ratio in the brain is dicussed
-
-
-
additional information
?
-
-
no activity with glucose and glucosamine 6-phosphate
-
-
-
additional information
?
-
-
glucose-6-phosphate dehydrogenase protects the parasite against reactive oxygen species
-
-
-
additional information
?
-
-
G6PD overexpressed in adipocytes in obese (including db/db, ob/ob and diet-induced obesity) mice, in adipocytes and stromal-vascular cells in diabetic db/db mice, and in adipocytes cultured under high-glucose conditions in vitro induces the expression of NADPH oxidase and leads to an increase in oxidative stress
-
-
-
additional information
?
-
-
G6PDH plays a critical role in maintaining cellular reduced glutathione levels under long-term salt stress in plants. NADPH, produced by G6PDH, not only acts as the reducing potential for the output of reduced glutathione, but is involved in the activity of plasma membrane NADPH oxidase under salt stress, which results in hydrogen peroxide accumulation
-
-
-
additional information
?
-
-
G6PDH plays a role in supplying NADPH for oil accumulation in developing seeds in which photosynthesis may be light limited
-
-
-
additional information
?
-
-
transgenic (previously susceptible) lines overexpressing G6PDH-encoding gene, displaying high NADPH tolerance engineered for cytosolic expression, show early oxidative bursts, callose deposition, and changes in metabolic parameter
-
-
-
additional information
?
-
-
no activity with other sugars, such as fructose-6-phosphate, glucose-1-phosphate, ribulose 5-phosphate, and ribose 5-phosphate
-
-
-
additional information
?
-
-
the following substances, 1 mM, are not substrates when substituted for D-glucose 6-phosphate: D-glucose 6-phosphate, D-fructose 1-phosphate, D-gluconate 6-phosphate, D-galactose 6-phosphate, D-ribose 5-phosphate, and D-glucose
-
-
-
additional information
?
-
-
the enzyme is a bifunctional enzyme glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase, the enzyme activity is analyzed for the reaction of glucose-6-phosphate dehydrogenase, EC 1.1.1.49, in a coupled assay with diaphorase activity, which uses NADPH to reduce resazurin to form the highly fluorescent molecule resorufin
-
-
-
additional information
?
-
Schizosaccharomyces pombe NCYC 132S2-2
-
no activity with D-glucose, D-ribose, D-fructose-6-phosphate, D-ribose-5-phosphate
-
-
-
additional information
?
-
Escherichia coli K-10, Escherichia coli DF82
-
the following substances, 1 mM, are not substrates when substituted for D-glucose 6-phosphate: D-glucose 6-phosphate, D-fructose 1-phosphate, D-gluconate 6-phosphate, D-galactose 6-phosphate, D-ribose 5-phosphate, and D-glucose
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
-
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
Penicillium duponti
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
sigmoidal relationship in cofactor binding
-
-
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
isoform A(-) shows sigmoidal enzyme-substrate interaction, isoform A(+) shows hyperbolic enzyme-substrate interaction
D-glucose-delta-lactone 6-phosphate
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
hyperbolic cofactor binding
-
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
Schizosaccharomyces pombe NCYC 132S2-2
-
-
-
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
Pseudomonas sp. W5
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + NAD(P)+
D-glucono-1,5-lactone 6-phosphate + NAD(P)H
show the reaction diagram
-
key enzyme catalyzing the first step of the pentose phosphate pathway generating NADPH for anabolic metabolsim pathways and protection systems in the liver
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
catalyzes the first step of the pentose phosphate pathway, enzyme deficiency often causes hemolytic anaemia
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
differential regulation of isozymes, the cytosolic enzyme is regulated by sugar availability at transcriptional level, while the plastidic isozymes are regulated by redox mechanism
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
enzyme catalyzes the first step of the pentose phosphate pathway
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
involved in oxidative pentose phosphate pathway in roots, related to glutamate synthesis in the plastids
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
key enzyme catalyzing the first step in the pentose phosphate pathway
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
key enzyme catalyzing the first step of the hexose monophosphate shunt pathway
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
key enzyme of the pentose phosphate pathway
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
key regulatory enzyme of the pentose phosphate pathway, regulation mechanism study
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
first step in the pentose phosphate pathway
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
G6PDH is the rate-limiting step in the formation of NADPH via the triphosphate, and is responsible for the major supply of NADPH in the cell
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
-
inhibition by divalent metal ions, at low NADPH /NADP+ ratio, is another means of controlling the pentose phosphate pathway
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
show the reaction diagram
Q1WBU6
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
show the reaction diagram
G1EHI3
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
show the reaction diagram
-
oxidative enzyme of pentose phosphate pathway
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
-
first enzyme of the pentose phosphate pathway, one of the main sources of NADPH
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
-
oxidative pentose pathway
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
-
the enzyme is involved pentose biosynthesis
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
Meyerozyma guilliermondii FTI 20037
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH
show the reaction diagram
Pseudomonas fluorescens 13525
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
Escherichia coli K-10, Escherichia coli DF82
-
-
-
-
?
D-glucose 6-phosphate + NADP+ + H2O
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
D-glucose 6-phosphate + NADP+ + H2O
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
-
the enzyme is responsible for the production of NADPH, which is required for biosynthetic reactions and protection of cells from free radicals
-
-
?
D-glucose 6-phosphate + NADP+ + H2O
D-gluconate 6-phosphate + NADPH + H+
show the reaction diagram
Saccharomyces cerevisiae W303-181
-
-
-
-
?
additional information
?
-
-
physiological regulation of NADP+-NADPH-ratio in the brain is dicussed
-
-
-
additional information
?
-
-
glucose-6-phosphate dehydrogenase protects the parasite against reactive oxygen species
-
-
-
additional information
?
-
-
the enzyme is a bifunctional enzyme glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase, the enzyme activity is analyzed for the reaction of glucose-6-phosphate dehydrogenase, EC 1.1.1.49, in a coupled assay with diaphorase activity, which uses NADPH to reduce resazurin to form the highly fluorescent molecule resorufin
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
deamino-NADP+
-
-
deamino-NADP+
-
not as effective as NADP+
NAD+
-
-
NAD+
-
dual coenzyme specificity for NAD+ and NADP+, G6PDH-1; dual coenzyme specificity for NAD+ and NADP+, G6PDH-2
NAD+
-
NADP+-specific enzyme. In presence of NAD+ 410fold reduction in the performance of the enzyme
NAD+
-
NAD+ can replace NADP+, with 10 mM NAD+ giving 25% of the rate in the usual assay with NADP+
NADP+
Penicillium duponti
-
-
NADP+
-
absolute specificity
NADP+
-
high preference for
NADP+
-
absolute specificity
NADP+
-
isoform A(-) has a higher affinity for NADP+
NADP+
-
absolute specificity
NADP+
-
high preference for
NADP+
-
absolute specificity
NADP+
-
binding by mutant P409R is reduced
NADP+
-
preferred cofactor, 20.4fold higher activity at 40C and 5.7fold at 70C than with NAD+
NADP+
-
highly preferred cofactor, 1000fold higher activity than with NAD+
NADP+
-
-
NADP+
-
specific for, no activity with NAD+
NADP+
-
dual coenzyme specificity for NAD+ and NADP+, G6PDH-1; dual coenzyme specificity for NAD+ and NADP+, G6PDH-2
NADP+
-
the enzyme contains 1 mol NADP+ per subunit. Apoenzyme, devoid of bound NADP+, is still fully active
NADP+
-
-
NADP+
-
NADP+ has major positive influence on refolding. NADP+ is essential for the folding intermediate to adopt native structure. Without added NADP+, the recovery yield is only about 10%. As the concentration of NADP+ increases, more enzyme activity can be regained in a concentration dependent manner
NADP+
-
G6PD activity is regulated by the intracellular NADP+ levels and the NADPH/NADP+ ratio
NADP+
Q1WBU6
-
NADP+
-
NADP+-specific enzyme. In presence of NAD+ 410fold reduction in the performance of the enzyme. Modeling of the sensitivity of reduced cofactor production by G6PDH as a function of the redox ratios of NAD/NADH (rRNAD) and NADP/NADPH (rRNADP). NADPH production sharply increases within the range of thermodynamically feasible values of rRNADP, but NADH production remains low within the range feasible for rRNAD
NADP+
-
almost specific for NADP+ as coenzyme. In presence of 2 and 3 mM NAD+ the velocity is about 2% compared to NADP+
NADP+
-
-
NADP+
G1EHI3
the enzyme has two NADP+ binding sites, one is the structural NADP+ and the second is the catalytic NADP+. The structural NADP+ domain adopt a classic beta-alpha-beta dinucleotide fold with the fingerprint sequence GASGDLA at the tight turn following the first beta-strand
NADPH
Penicillium duponti
-
-
NADPH
-
-
thio-NAD+
-
-
thio-NADP+
-
best cofactor
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ag+
-
1 mM, 1.6fold activation, G6PDH-2
Ca2+
-
activation
Ca2+
-
activation
Ca2+
-
1 mM, 1.4fold activation
Cd2+
-
1 mM, 1.3fold activation, G6PDH-2
Cd2+
-
enzyme is stimulated in presence of 3 mg and 5 mg of Cd on the first day of experiment in gill, liver and kidney tissues. The stimulation effect of the 5 mg/l dose of Cd on G6PD and 6PGD enzyme activities is significantly diminished after seven days. The G6PDenzyme activity levels are stimulated by approximately 60% in gills, 68% in liver, and 67% in kidneys
Mg2+
-
activation
Mg2+
-
required
Mg2+
-
required
Mg2+
-
activation
Mg2+
-
activation
Mg2+
-
activation
Mg2+
-
required, can substitute for Mn2+
Mg2+
-
is markedly stimulated by (but not absolutely dependent upon) Mg2+
Mg2+
-
required
Mg2+
-
1 mM, 1.6fold activation
Mg2+
-
activates, no absolute requirement. In the presence of saturating concentrations of spermidine or other polycations, Mg2+ ions have no further stimulatory effect
Mg2+
-
required
Mg2+
G1EHI3
required
Mg2+
-
required
Mn2+
-
activation
Mn2+
-
required, can substitute for Mg2+
Na2HPO4
-
at 400 mM regains 22% activity on refolding
Na2SO4
-
at 400 mM regains 23% activity on refolding
NaCl
-
at 400 mM regains 63% activity on refolding
NaClO4
-
at 400 mM regains 2.3% activity on refolding
NaSCN
-
at 400 mM regains 1.4% activity on refolding
nitrate
-
activates plastidic isozymes by 10fold by direct action on the enzyme
nitrite
-
activates plastidic isozymes by 10fold by direct action on the enzyme
Sodium acetate
-
at 400 mM regains 58% activity on refolding
sulfate
-
activates plastidic isozymes by 10fold by direct action on the enzyme
Mn2+
-
is markedly stimulated by (but not absolutely dependent upon) Mn2+
additional information
-
no metal ions necessary
additional information
-
high ionic strength inactivates the enzyme
additional information
-
no effect on cytosolic isozyme by H2O2, FeCl3, NH4Cl, NaNO2, NaNO3, sulfate or endothall, okadaic acid and NaF
additional information
-
no essential requirement for divalent cations
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R,3R)-2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-3,4-dihydro-2H-chromen-3-yl 3,4,5-trihydroxybenzoate
-
-
(2R,3R)-5,7-dihydroxy-2-(3,4,5-trihydroxyphenyl)-3,4-dihydro-2H-chromen-3-yl 3,4,5-trihydroxybenzoate
-
-
(2S,3R)-2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-3,4-dihydro-2H-chromen-3-yl 3,4,5-trihydroxybenzoate
-
-
(2S,3R)-5,7-dihydroxy-2-(3,4,5-trihydroxyphenyl)-3,4-dihydro-2H-chromen-3-yl 3,4,5-trihydroxybenzoate
-
-
(4Z)-4-(3-bromobenzylidene)-1-(4-methylphenyl)pyrazolidine-3,5-dione
-
-
(5Z)-1-(4-bromophenyl)-5-[[5-(2-nitrophenyl)furan-2-yl]methylidene]pyrimidine-2,4,6(1H,3H,5H)-trione
-
-
(5Z)-1-(4-ethoxyphenyl)-5-[[5-(2-nitrophenyl)furan-2-yl]methylidene]pyrimidine-2,4,6(1H,3H,5H)-trione
-
-
(5Z)-5-[[5-(2-methyl-4-nitrophenyl)furan-2-yl]methylidene]-1-(3-methylphenyl)pyrimidine-2,4,6(1H,3H,5H)-trione
-
reversible, non-competitive inhibition versus NADP+, mixed-type versus D-glucose 6-phosphate
2'-phosphoadenosine 5'-diphosphoribose
-
-
2,3-diphosphoglycerate
-
-
2-[(5Z)-5-(4-hydroxy-3-methoxybenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]-3-phenylpropanoate
-
-
2-[(E)-(4-nitrocyclohexa-2,4-dien-1-yl)(2-phenylhydrazinylidene)methyl]benzene-1,4-diol
-
non-competitive inhibition versus NADP+, non-competitive or mixed-type versus D-glucose 6-phosphate
2-[4-(4-chlorophenyl)-1,3-thiazol-2-yl]-5-methyl-4-(3,4,5-trimethoxybenzyl)-2,4-dihydro-3H-pyrazol-3-one
-
irreversible, non-competitive inhibition versus NADP+, mixed-type versus D-glucose 6-phosphate
3-(3,4-dichlorophenyl)-1,1'-dimethyl urea
-
cytosolic isozyme, inhibition by uncoupling of photosynthetic electron transport
3-(4-hydroxyphenyl)-2-(pyridin-3-yl)quinazolin-4(3H)-one
-
irreversible, non-competitive inhibition versus NADP+, mixed-type versus D-glucose 6-phosphate
3-(5-bromopyridin-2-yl)-2-(pyridin-3-yl)quinazolin-4(3H)-one
-
irreversible, non-competitive inhibition versus NADP+, mixed-type versus D-glucose 6-phosphate
3-(5-[(E)-[2-(5-nitropyridin-2-yl)hydrazinylidene]methyl]furan-2-yl)benzoic acid
-
-
4-fluoro-N-(4-hydroxynaphthalen-1-yl)benzenesulfonamide
-
-
4-methyl-3-(propan-2-yloxy)-6H-benzo[c]chromen-6-one
-
non-competitive inhibition versus NADP+, mixed-type versus D-glucose 6-phosphate
5-(3alpha,7alpha,12alpha-triacetoxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
-
weak inhibition
5-(3alpha,7alpha,12alpha-trihydroxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
-
weak inhibition
5-[[5-(4-methoxy-2-nitrophenyl)furan-2-yl]methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
reversible, competitive inhibition versus NADP+, mixed-type versus D-glucose 6-phosphate
-
5alpha-androstan-16-alpha-bromo-3beta-ol-17-one
-
in vitro cell viability assays shows a LD50 of 20 microM for Trypanosoma cruzi epimastigotes
5alpha-Androstan-3beta-ol-17-one
-
uncompetitive inhibitor
5alpha-androsten-16-alpha-bromo-3beta-ol-17-one
-
potent inhibitor, in vitro cell viability assays shows a LD50 of 12 microM for Trypanosoma cruzi epimastigotes
6-amino-NAD+
-
irreversibly inhibits G6PD
6-amino-NADP+
-
irreversibly inhibits G6PD
6-phosphogluconate
-
-
adenosine 5' [beta,gamma-amido] triphosphate
-
-
-
adenosine 5' [beta-thio] diphosphate
-
-
-
adenosine 5' [gamma-thio] triphosphate
-
-
ADP
-
-
ADP
-
15% inhibition at 2 mM
amikacin
-
in vitro, noncompetitive
ammonia
-
inhibition in vitro and in vivo at sublethal concentration of 0.0022-0.0055 mM, IC50: 0.0187 mM
amoxicillin
Chalcalburnus tarischii
-
-
AMP
-
only 2'-AMP
AMP
-
5% inhibition at 2 mM
ATP
-
-
ATP
-
15% inhibition at 2.5 mM, 24% inhibition at 10 mM
ATP
-
weak, noncompetitive inhibition
ATP
-
2.0 mM, 65% inhibition, G6PDH-2; G6PDH-1
ATP
-
10 mM, 50-75% inhibition, assay without MgCl2
ATP
-
31% inhibition at 5 mM, non-competitive inhibition with respect to D-glucose 6-phosphate
beta-naphthoquinone-4-sulfonic acid
-
1 mM, 68% inhibition, G6PDH-1; 1 mM, 81% inhibition, G6PDH-2
Blue dextran
-
-
-
Cd2+
-
1 mM, 53% inhibition, G6PDH-1
Cd2+
-
1 mM, 83% inhibition
Cd2+
-
noncompetitive inhibition
ceftriaxone
-
strongly inhibits
Chymotrypsin
-
-
-
Ciprofloxacin
Chalcalburnus tarischii
-
-
Co2+
-
competitive, 60% inhibition at 0.01 mM
Co2+
-
1 mM, 56% inhibition
Cu2+
-
1 mM, 24% inhibition, G6PDH-1; 1 mM, 78% inhibition, G6PDH-2
Cu2+
-
1 mM, complete inhibition
Cu2+
-
noncompetitive inhibition
cumene hydroperoxide
-
1% residual activity after treatment with 17 mM cumene hydroperoxide at 50C and pH 7 for 2 h
cycloheximide
-
-
cypermethrin
-
inhibits G6PD in vitro
D-glucose 6-phosphate
-
-
dehydroandrosterone
-
uncompetitive inhibitor
dehydroepiandrosterone
-
uncompetitively inhibits bloodstream form cells
dehydroepiandrosterone
-
non-competitively inhibits
deltamethrin
-
inhibits G6PD both in vivo and in vitro, significantly inhibits activity after the 48th hour. Among pesticides, it is the most effective one, which is widely used both at homes and in agricultural fields. Deltamethrin inhibits the enzyme at very low doses, particularly in in vivo conditions, indicating that fish in natural and cultural environments are susceptible to this pesticide and that deltamethrin contaminations can be cause high mortality in fish population, which may lead to the increase in food insufficiency for increasing populations and cause disruption of ecological balance. Thus, usage of deltamethrin must be well controlled
DTT
-
1 mM, 2 h, 20% loss of activity in the first 15 min and then the enzyme activity remains steady throughout the incubation
EDTA
-
slightly
EDTA
-
5 mM, 85% inhibition, G6PDH-1; 5 mM, 97% inhibition, G6PDH-2
epiandrosterone
-
uncompetitively inhibits bloodstream form cells
epiandrosterone
-
non-competitively inhibits
Estrogen
-
-
Fe2+
-
strong competitive inhibition
fructose 6-phosphate
-
-
gentamicin sulfate
-
in vitro, noncompetitive
glucosamine 6-phosphate
-
parabolic inhibition
glucosamine 6-phosphate
-
competitive G6PDH inhibitor
glucose
-
at concentration above 10 mM
glucose
-
high glucose level of 25 mM leads to a decrease in G6PD activity and protein level in islets
glyceraldehyde 3-phosphate
-
-
glyoxylate
-
-
guanidinium hydrochloride
-
denatures
guanidinium hydrochloride
-
in the presence of 4 M, after 2 hours all secondary structure is lost
guanosine hydrochloride
-
the enzyme shows a sharp loss in activity above 0.75 M, but is activated by low concentrations of 0.2 M of GdmCl
-
Hg2+
-
1 mM, 47% inhibition, G6PDH-2; 1 mM, 84% inhibition, G6PDH-1
Hg2+
-
1 mM, complete inhibition
Hg2+
-
noncompetitive inhibition
hydrogen peroxide
-
inhibitory at 0.25%, at pH 7
Isocitrate
-
-
KMnO4
Chalcalburnus tarischii
-
-
lidocaine
-
strongly inhibits
marcaine
-
noncompetitive
meloksikam
-
strongly inhibits
metamizol
-
inhibition of wild-type and mutant enzyme 3
metamizol
-
competitive
metamizol
-
strongly inhibits
MgSO4
-
competitive
N-(4-hydroxynaphthalen-1-yl)-2,5-dimethylbenzenesulfonamide
-
-
-
NADH
-
noncompetitive
NADH
-
allosteric inhibition, inhibition is not reversed by NAD+, AMP, or spermidine
NADP+
-
at high concentration, dead-end ternary complexes are formed
NADP+
-
at concentrations above 0.3 mM
NADP+
-
-
NADP+
-
substrate inhibition
NADPH
-
-
NADPH
-
-
NADPH
-
liver enzyme is more sensitive to inhibition than kidney enzyme
NADPH
-
inhibition patterns of substrates and product
NADPH
-
NADPH binding is important for physiological regulation of pentose phosphate pathway
NADPH
-
competitive
NADPH
-
competitive
NADPH
-
has a regulatory role in pentaose phosphate pathway
NADPH
-
slight inhibition
NADPH
-
product inhibition
NADPH
Q8L743
-
NADPH
-
product inhibition with NADP+ or D-glucose 6-phosphate as the varying substrate
NADPH
-
when NADP+ is the varied substrate, NADPH NADPH is a competitive inhibitor both in the presence and absence of Mg2+, linear competitive inhibition. When glucose 6-phosphate is the varied substrate NADPH causes linear noncompetitive inhibition
NADPH
-
competitive inhibition with respect to NADP+ and D-glucose 6-phosphate
netilmicin
-
inhibition of wild-type and mutant enzymes 1-3
Nicotine
-
inhibits the enzyme from lung, testis, kidney, stomach, and brain, in concert with vitamin E the enzyme from testis brain and liver is inhibited, tissue-specific inhibition of 12.5-48%, overview, nicotine has no effect on enzyme from muscle, heart, and liver
nidazole
Chalcalburnus tarischii
-
-
oleic acid
-
G6PDH-1 is more susceptible to oleic acid than G6PDH-2
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
can be reversed 100% by dithiothreitol, partially by glutathione
p-chloromercuribenzoate
-
-
palmitoyl-CoA
-
-
palmitoyl-CoA
-
non-competitive
palmitoyl-CoA
-
leads to dissociation of active tetramers to inactive dimers
Pb2+
-
noncompetitive inhibition
penicillin G potassium
-
in vitro, noncompetitive
pental sodium
-
noncompetitive
peracetic acid
-
1% residual activity after treatment with 4 mM peracetic acid at 25C and pH 7 for 15 min
phosphoenol pyruvate
-
25% inhibition at 10 mM
phosphoenolpyruvate
-
-
phosphoenolpyruvate
-
13% inhibition at 2.5 mM, 31% inhibition at 10 mM
phosphoenolpyruvate
-
-
prilocaine
-
strongly inhibits
progesterone
-
-
propoxur
-
inhibits G6PD in vitro
pyridoxal 5'-phosphate
-
-
quartz
-
24 h incubation with quartz particles (80 microg/cm(2)) inhibits G6PD activity by 70%. Inhibition is fully prevented by glutathione. Silica exerts on G6PD an oxidative damage
-
Ribulose 1,5-diphosphate
-
-
RNAi
-
mediates reduction of the G6PDH level in bloodstream form cells
-
RNAi
-
suppression of endogenous cytosolic G6PDH isoforms result in highly uniform defense responses and also enhanced drought tolerance and flowering
-
sodium ceftizoxime
-
inhibition of wild-type and mutant enzymes 1-3
sodium cefuroxime
-
inhibition of wild-type and mutant enzymes 1-3
streptomycin
-
inhibition of wild-type and mutant enzyme 3
sulfanilacetamide
Chalcalburnus tarischii
-
-
sulfanilamide
Chalcalburnus tarischii
-
-
suramin
-
77% inhibition at 0.05 mM
tert-butyl hydroperoxide
-
1% residual activity after treatment with 290 mM tert-butyl hydroperoxide at 50C and pH 7 for 3 h
Thioredoxin f
-
from chloroplasts
-
Tl+
-
201Tl solution and radiation exposure has inhibitory effects on the enzyme activity both in vivo and in vitro
Urea
-
inhibition in vitro and in vivo at sublethal concentration of 0.02-0.05 mM, IC50: 0.0238 mM
Vancomycin
-
competitive
Vancomycin
Chalcalburnus tarischii
-
-
vitamin E
-
in concert with nicotine the enzyme from testis brain and liver is inhibited, while the enzyme from muscle and stomach is activated, overview
Zn2+
-
competitive, 40% inhibition at 0.01 mM
Zn2+
-
1 mM, 83% inhibition, G6PDH-2; 1 mM, 94% inhibition, G6PDH-1
Zn2+
-
noncompetitive inhibition
Mn2+
-
1 mM, 56% inhibition
additional information
-
the cytosolic isoyzme is not affected by osmotic change, phosphate sequestration, or ocidative stress
-
additional information
-
effects of streptomycin sulfate and tetracyclin antibiotics
-
additional information
-
product and dead-end inhibition studies, overview, no inhibition by AMP
-
additional information
-
not inhibited by ATP, phosphate, or Mg2+
-
additional information
-
is not inhibited by dehydroepiandrosterone and epiandrosterone
-
additional information
-
hyperaldosteronism downregulates G6PD and whereby decreases GSH levels and conversely increases oxidative stress, which evokes endothelial-derived NO and impairs vascular function
-
additional information
-
inhibition of G6PD protects rat hearts from ischemia-reperfusion injury induced by oxidative stress
-
additional information
Q43727
Trx f1 regulates G6PDH1 activity as efficiently as Trx m1 or m4. Trx x is a very poor regulator of G6PDH activity. Trx y1 is inefficient as inhibitor but it shows high efficiency in activation. Upon illumination, a strong and fast reductive inhibition of G6PDH1 activity dependent on the presence of all the components of the Fd/Trx system
-
additional information
Q43727, Q8L743, Q93ZW0, Q9FJI5, Q9FY99, Q9LK23
during 7 days of phosphate starvation, G6PD5 is continuously expressed throughout phosphate-starvation; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced
-
additional information
-
fluoride-containing bioactive glasses as used in tissue engineering as well as bone repair, inhibit the pentose phosphate oxidative pathway and the glucose 6-phosphate dehydrogenase activity. The effects are ascribable to the fluoride content/release of glass powders, they are mimicked by NaF solutions and are prevented by radical scavengers dimethyl sulfoxide and tempol, by superoxide dismutase, and by glutathione, but not by apocynin
-
additional information
-
non-radioactive Tl+, Fe3+ and Cu2+ do not influence the enzyme in vitro
-
additional information
-
NADH: no inhibition at up to 0.5 mM
-
additional information
-
high-throughput screening for small-molecule inhibitors of the enzyme from Plasmodium falciparum, inhibitor evaluation, structure-activity relationship analysis, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-(3alpha,12alpha-dihydroxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
-
weak activation
5-(3alpha,acetoxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
-
activates
6-Aminohexanoic acid
-
marginally increases the refolding yield in the presence of Arg, and it is unable to replace Arg in promoting a high refolding yield
acetazolamide
-
activates
anhydrotetracyclin
Q43727
induces expression of mature G6PDH1
-
artesunate
-
induces a 25fold increase in glucose-6-phosphate dehydrogenase activity while there is no significant reduction in the red blood cell count. Critical role for glucose-6-phosphate dehydrogenase in the prevention of oxidative stress and lysis of red blood cells in artesunate-treated rats
butanol
-
marginally increases the refolding yield in the presence of Arg, and it is unable to replace Arg in promoting a high refolding yield
cyclophilin A
-
facilitates refolding, the yield, at about 82%, is about 12% higher than without cyclophilin A. Even with 0.0004 mM cyclophilin A in the standard refolding buffer, maximal recovery takes about 7 days
-
dithiothreitol
-
dithiothreitol has major positive influence on refolding
glucosamine 6-phosphate
-
-
glycerol
-
marginally increases the refolding yield in the presence of Arg, and it is unable to replace Arg in promoting a high refolding yield
guanosine hydrochloride
-
the enzyme shows a sharp loss in activity above 0.75 M, but is activated by low concentrations of 0.2 M of GdmCl
-
H2O2
-
H2O2, produced under salt stress, induces increased G6PDH activity and the enzymes of glutathione cycle, which concomitantly results in an increased reduced glutathione contents
Insulin
-
stimulates, in pregnant women with types 1 diabetes insulin effect on the enzyme activity is lower than in the control. In the group of pregnant women with type 2 diabetes and gestational diabetes the effect of insulin is decreased as compared to control
-
insulin-like growth factor 1
-
stimulates, in pregnant women with types 1 diabetes effect of insulin-like growth factor 1 is absent. In the group of pregnant women with type 2 diabetes and gestational diabetes the effect of insulin-like growth factor 1 is decreased as compared to control
-
L-Arg
-
L-Arg has major positive influence on refolding. L-Arg is the key player in the refolding of human G6PD, preventing the aggregation of folding intermediate
N-ethylmaleimide
-
blocking the SH group leads to activation of rBmG6PD activity
paraquat
-
activates plastidic isozymes by 10fold by direct action on the enzyme, no activation of the cytosolic isozyme
PEG 3350
-
marginally increases the refolding yield in the presence of Arg, and it is unable to replace Arg in promoting a high refolding yield
-
relaxin
-
stimulates, in pregnant women with types 1 diabetes effect of relaxin is absent. In the group of pregnant women with type 2 diabetes and gestational diabetes the effect of relaxin is somewhat higher as compared to control
-
S-methyl 1,2,3-benzothiadiazole-7-carbothioate
-
treatment of fruits
spermidine
-
activation constant: 0.2 mM
streptomycin
-
activation of mutant enzymes 1 and 2
Sucrose
-
in wild-type seedlings G6PD5 and G6PD6 show small (1.7- and 2fold, respectively) but significant induction by sucrose
trehalose
-
marginally increases the refolding yield in the presence of Arg, and it is unable to replace Arg in promoting a high refolding yield
vitamin E
-
in concert with nicotine the enzyme from testis brain and liver is inhibited, while the enzyme from muscle and stomach is activated by 36% and 20%, respectively, overview
metamizol
-
activation of mutant enzymes 1 and 2
additional information
-
light and metabolizable sugars induce the cytosolic isozyme by increased de novo protein synthesis, while the plastidic isozymes are unaffected
-
additional information
-
temperature and protein concentration have positive influence on refolding. Refolding at 25C is relatively slow, taking about one week to reach the maximum activity. Final refolding yield at pH 7.5 is about 69%, similar to 71% at pH 8.0, and only slightly higher than 65% at pH 8.5. At 30C, refolding is faster in the early stages than at 25C, but the highest activities, achieved after 4-5 days, are 49% at pH 7.5, 53% at pH 8.0, and 48% at pH 8.5, respectively, considerably lower than at 25C. Correct refolding is severely suppressed at 37C, with the highest recovery yield at 13%. Recovery yields are 54%, 70%, 56%, and 33% for protein concentrations at 5 microg/ml, 10 microg/ml, 20 microg/ml and 50 microg/ml, respectively
-
additional information
Q43727
oxidative activation is strictly dependent on plastidial thioredoxins that show differential efficiencies. Trx f1 regulates G6PDH1 activity as efficiently as Trx m1 or m4. Trx x is a very poor regulator of G6PDH activity. Trx y1 is inefficient as inhibitor but it shows high efficiency in activation. G6PDH activity can be recovered by transferring from light to dark, reversibility of inactivation certifying redox modulation of the enzyme. In the dark, reactivation can be enhanced by the addition of oxidants, such as oxidized dithiothreitol and H2O2
-
additional information
-
after pathogen infection with Phytophthora nicotianae, G6PDH activity rises 2 to 3fold in leaves of a resistant, but not of a susceptible, tobacco cultivar
-
additional information
Q43727, Q8L743, Q93ZW0, Q9FJI5, Q9FY99, Q9LK23
activity of G6PDH increases rapidly just after the inoculation of 10-day-old cells into fresh medium; activity of G6PDH increases rapidly just after the inoculation of 10-day-old cells into fresh medium; activity of G6PDH increases rapidly just after the inoculation of 10-day-old cells into fresh medium; activity of G6PDH increases rapidly just after the inoculation of 10-day-old cells into fresh medium; activity of G6PDH increases rapidly just after the inoculation of 10-day-old cells into fresh medium; activity of G6PDH increases rapidly just after the inoculation of 10-day-old cells into fresh medium
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.374
2-deoxy-D-glucose 6-phosphate
-
pH 8.0, 25C, recombinant mutant R454C, with NADP+
24
2-deoxy-D-glucose 6-phosphate
-
pH 7.4, 37C, with NADP+
35
2-deoxy-D-glucose 6-phosphate
-
pH 7.4, 80C, recombinant enzyme
0.279
6-phosphonogluconate
-
isoenzyme II
0.864
6-phosphonogluconate
-
isoenzyme II
0.031
D-galactose 6-phosphate
-
isoenzyme II
0.046 - 0.047
D-galactose 6-phosphate
-
isoenzyme I
0.051
D-galactose 6-phosphate
-
isoenzyme II
0.0021
D-glucose 6-phosphate
-
nephridic enzyme
0.0033
D-glucose 6-phosphate
-
hepatic enzyme
0.00953
D-glucose 6-phosphate
-
pH 8.0, 25C, recombinant mutant R454C, with NADP+
0.00971
D-glucose 6-phosphate
-
pH 8.0, 25C, recombinant mutant R454H, with NADP+
0.014
D-glucose 6-phosphate
-
25C, pH 7.8
0.0145
D-glucose 6-phosphate
-
pH 7.5, temperature not specified in the publication
0.019
D-glucose 6-phosphate
-
pH 7.8, 85C, recombinant enzyme
0.024
D-glucose 6-phosphate
-
-
0.026
D-glucose 6-phosphate
-
pH 8.5, 30C
0.036
D-glucose 6-phosphate
-
pH 8.0, 25C
0.037
D-glucose 6-phosphate
-
-
0.04
D-glucose 6-phosphate
-
-
0.04
D-glucose 6-phosphate
-
-
0.04
D-glucose 6-phosphate
-
22C, liver extralesional parenchyma
0.041
D-glucose 6-phosphate
-
pH 7.4, 37C
0.042
D-glucose 6-phosphate
-
cosubstrate NADP+
0.048
D-glucose 6-phosphate
-
pH 8.0, 25, mutant 2
0.0488
D-glucose 6-phosphate
-
pH 8.0, 25C, recombinant mutant R454C, with deamino-NADP+
0.0491
D-glucose 6-phosphate
-
clinical mutant G488S
0.05
D-glucose 6-phosphate
-
pH 8.0, 25C
0.052
D-glucose 6-phosphate
-
pH 8.0, 25C, recombinant wild-type enzyme
0.052
D-glucose 6-phosphate
-
pH 8.0, 25C, recombinant wild-type enzyme, with NADP+
0.052
D-glucose 6-phosphate
-
native G6PD
0.0538
D-glucose 6-phosphate
-
clinical mutant G488V
0.0547
D-glucose 6-phosphate
-
refolded G6PD
0.056
D-glucose 6-phosphate
-
isoenzyme II
0.0578
D-glucose 6-phosphate
-
-
0.061
D-glucose 6-phosphate
-
isoenzyme I
0.063
D-glucose 6-phosphate
-
70C, recombinant enzyme, with NADP+
0.067
D-glucose 6-phosphate
-
pH 8.0, 25C, recombinant mutant R393G
0.069
D-glucose 6-phosphate
-
recombinant from E. coli
0.07
D-glucose 6-phosphate
-
pH 7.4, 37C
0.07
D-glucose 6-phosphate
-
pH 8.0, temperature not specified in the publication
0.072
D-glucose 6-phosphate
-
-
0.0745
D-glucose 6-phosphate
-
-
0.075
D-glucose 6-phosphate
-
pH 7.5
0.077
D-glucose 6-phosphate
-
pH 8.0, 37C, native wild-type enzyme
0.083
D-glucose 6-phosphate
-
pH 8.0, 37C, recombinant wild-type enzyme
0.083
D-glucose 6-phosphate
-
pH 8.0, 25, mutant 3
0.092
D-glucose 6-phosphate
-
-
0.1
D-glucose 6-phosphate
-
25C, pH 8.0, wild-type strain K-10
0.1073
D-glucose 6-phosphate
-
pH 7.6, 25C
0.122
D-glucose 6-phosphate
-
pH 7.4, 37C, with NADP+ or deamino-NADP+
0.138
D-glucose 6-phosphate
-
-
0.145
D-glucose 6-phosphate
-
25C, pH 8.0, high-level glucose-6-phosphate dehydrogenase strain DF82
0.15
D-glucose 6-phosphate
-
pH 7.4, 80C, recombinant enzyme
0.15
D-glucose 6-phosphate
-
pH 8.0, 25, mutant 1
0.153
D-glucose 6-phosphate
-
-
0.167
D-glucose 6-phosphate
-
isoenzyme I
0.174
D-glucose 6-phosphate
-
25C, pH 8.0, cofactor: NADP+
0.18
D-glucose 6-phosphate
-
isoenzyme II
0.19
D-glucose 6-phosphate
-
pH 8.0, 25C, recombinant mutant R393H
0.2
D-glucose 6-phosphate
-
22C, normal liver parenchyma
0.206
D-glucose 6-phosphate
-
pH 7.6, temperature not specified in the publication
0.23
D-glucose 6-phosphate
-
-
0.24
D-glucose 6-phosphate
-
G6PDH activity extracted from source leaves of wild-type tobacco SNN cultivars
0.25
D-glucose 6-phosphate
-
G6PDH activity extracted from source leaves of wild-type tobacco Xanthi cultivars
0.286
D-glucose 6-phosphate
-
pH 8.0, 37C, recombinant mutant P409R
0.44
D-glucose 6-phosphate
-
pH 8.0, 25C
0.5
D-glucose 6-phosphate
-
pH 8.0, 25, wild-type enzyme
0.57
D-glucose 6-phosphate
Q8L743
-
0.96
D-glucose 6-phosphate
-
25C
1.25
D-glucose 6-phosphate
-
25C, pH 8.0, cofactor: NAD+
1.9
D-glucose 6-phosphate
-
22C, liver (pre)neoplastic lesions
44.4
D-glucose 6-phosphate
-
25C, pH 8.0, mutant enzyme G163D
45.8
D-glucose 6-phosphate
-
25C, pH 8.0, wild-type enzyme
50.7
D-glucose 6-phosphate
-
25C, pH 8.0, mutant enzyme G163S
0.0156
deamino-NADP+
-
pH 8.0, 25C, recombinant mutant R454C, with D-glucose 6-phosphate
0.047
NAD+
-
-
1.67
NAD+
-
25C, pH 8.0
5.09
NAD+
-
25C, pH 8.0
12
NAD+
-
pH 7.4, 80C, recombinant enzyme
0.000012
NADP+
-
pH 8.0, 25C
0.0003
NADP+
-
nephridic enzyme
0.001
NADP+
-
hepatic enzyme
0.0013
NADP+
-
25C, pH 7.8
0.0016
NADP+
-
-
0.00238
NADP+
-
pH 8.0, 25C, recombinant mutant R454H, with D-glucose 6-phosphate
0.00276
NADP+
-
pH 8.0, 25C, recombinant mutant R454C, with D-glucose 6-phosphate
0.0053
NADP+
-
-
0.0056
NADP+
-
-
0.006 - 0.008
NADP+
-
isoenzymes I and II, with glucose 6-phosphate
0.006
NADP+
-
pH 7.5
0.00694
NADP+
-
refolded G6PD
0.00707
NADP+
-
pH 8.0, 25C, recombinant wild-type enzyme, with D-glucose 6-phosphate
0.00707
NADP+
-
native G6PD
0.0071
NADP+
-
pH 8.0, 25C, recombinant wild-type enzyme
0.0075
NADP+
-
25C, pH 8.0
0.00839
NADP+
-
pH 8.0, 25C, recombinant mutant R454C, with deoxy-D-glucose 6-phosphate
0.0086
NADP+
-
pH 7.5, temperature not specified in the publication
0.009
NADP+
-
25C
0.0093
NADP+
-
pH 8.0, 25C, recombinant mutant R393G
0.0094
NADP+
-
-
0.01
NADP+
-
pH 7.4, 37C, with D-glucose 6-phosphate or 2-deoxy-D-glucose 6-phosphate
0.0107
NADP+
-
clinical mutant G488V
0.0118
NADP+
-
clinical mutant G488S
0.012
NADP+
-
-
0.012
NADP+
-
recombinant from E. coli
0.0121
NADP+
-
-
0.013
NADP+
-
-
0.0147
NADP+
-
pH 7.4, 37C
0.015
NADP+
-
25C, pH 8.0, high-level glucose-6-phosphate dehydrogenase strain DF82
0.015
NADP+
-
pH 8.0, temperature not specified in the publication
0.016
NADP+
-
25C, pH 8.0, wild-type strain K-10
0.0165
NADP+
-
pH 8.0, 25C, recombinant mutant R393H
0.017
NADP+
-
0.0025 mM glucose 6-phosphate
0.017
NADP+
-
pH 8.0, 25C
0.02
NADP+
-
with D-glucose 6-phosphate or D-galactose 6-phosphate
0.0225
NADP+
-
pH 7.6, temperature not specified in the publication
0.023
NADP+
-
pH 7.4, 37C
0.024
NADP+
Q8L743
-
0.025
NADP+
-
isoenzyme II, with 6-phosphonogluconate 0.1 mM
0.026
NADP+
-
-
0.03
NADP+
-
-
0.03
NADP+
-
with 2-deoxyglucose 6-phosphate, KM decreases to 10 mM with increasing substrate concentration from 0.3 to 1.5 mM
0.03
NADP+
-
pH 7.4, 80C, recombinant enzyme
0.041
NADP+
-
G6PDH activity extracted from source leaves of wild-type tobacco SNN cultivars; G6PDH activity extracted from source leaves of wild-type tobacco Xanthi cultivars
0.067
NADP+
-
-
0.07
NADP+
-
pH 8.0, 25, mutant enzyme 2
0.077
NADP+
-
pH 8.0, 25C
0.08
NADP+
-
pH 7.8, 85C, recombinant enzyme
0.085
NADP+
-
pH 8.0, 25, mutant enzyme 3
0.116
NADP+
-
pH 8.5, 30C
0.13
NADP+
-
pH 8.0, 25, mutant enzyme 1
0.21
NADP+
-
pH 8.0, 25, wild-type enzyme
4.67
NADP+
-
25C, pH 8.0, wild-type enzyme
4.8
NADP+
-
25C, pH 8.0, mutant enzyme G163D
6.46
NADP+
-
25C, pH 8.0, mutant enzyme G163S
0.014
NADPH
-
recombinant from E. coli
0.015
NADPH
-
-
0.02
NADPH
-
-
0.023
NADPH
-
isoenzyme II, with 6-phosphonogluconate 0.1 mM
1.5
thio-NAD+
-
pH 7.4, 80C, recombinant enzyme
0.06
thio-NADP+
-
pH 7.4, 80C, recombinant enzyme
2 - 3
deamino-NADP+
-
pH 7.4, 37C, with D-glucose 6-phosphate
additional information
additional information
-
-
-
additional information
additional information
Penicillium duponti
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetics and thermodynamics, rapid equilibrium random bi bi kinetic model
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
thermodynamics, steady-state kinetics
-
additional information
additional information
-
steady-state kinetics of wild-type and mutant enzymes
-
additional information
additional information
-
ping pong bi bi kinetic mechanism
-
additional information
additional information
-
steady-state kinetics of wild-type and mutant enzymes
-
additional information
additional information
-
kinetics, kinetic mechanism analysis, ternary-complex mechanism, overview
-
additional information
additional information
-
hyperbolic kinetics versus D-glucose 6-phosphate
-
additional information
additional information
-
the initial velocity plots of the enzyme follow the Michaelis-Menten equation in the absence of NADH. In its presence, however, the velocity versus substrate plots for NADP+ become sigmoidal but remain hyperbolic for glucose 6-phosphate as the variable substrate. Inhibition against both of the substrates of the enzyme by NADH is noncompetitive. The inhibition curves for NADH are also sigmoidal, suggesting a multisite binding of the inhibitor on the enzyme surface
-
additional information
additional information
-
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
22.4
2-deoxy-D-glucose 6-phosphate
-
pH 8.0, 25C, recombinant mutant R454C, with NADP+
1800
2-deoxy-D-glucose 6-phosphate
-
pH 7.4, 80C, recombinant enzyme
43
2-deoxyglucose 6-phosphate
-
-
157
D-galactose 6-phosphate
-
-
16.4
D-glucose 6-phosphate
-
-
20 - 50
D-glucose 6-phosphate
-
pH 8.0, 25C, recombinant mutant R454C, with deamino-NADP+
22.2
D-glucose 6-phosphate
-
-
28.6
D-glucose 6-phosphate
-
pH 8.0, 25C, recombinant mutant R454C, with NADP+
34
D-glucose 6-phosphate
-
25C
39.9
D-glucose 6-phosphate
-
pH 8.0, 25C, recombinant mutant R454H, with NADP+
57.1
D-glucose 6-phosphate
-
pH 7.6, temperature not specified in the publication
83
D-glucose 6-phosphate
-
pH 7.5
87.7
D-glucose 6-phosphate
-
pH 8.0, 25C, recombinant mutant R454C, with deamino-NADP+
192
D-glucose 6-phosphate
-
pH 8.0, 25C, recombinant mutant R393H
207
D-glucose 6-phosphate
-
25C, pH 8.0, mutant enzyme G163S
212
D-glucose 6-phosphate
-
clinical mutant G488V
232
D-glucose 6-phosphate
-
pH 8.0, 25C, recombinant mutant R393G
249
D-glucose 6-phosphate
-
25C, pH 8.0, mutant enzyme G163D
251
D-glucose 6-phosphate
-
25C, pH 8.0, wild-type enzyme
254
D-glucose 6-phosphate
-
clinical mutant G488S
275
D-glucose 6-phosphate
-
pH 8.0, 25C, recombinant wild-type enzyme
275
D-glucose 6-phosphate
-
pH 8.0, 25C, recombinant wild-type enzyme, with NADP+
275
D-glucose 6-phosphate
-
native G6PD
279
D-glucose 6-phosphate
-
refolded G6PD
571
D-glucose 6-phosphate
-
-
3500
D-glucose 6-phosphate
-
pH 7.4, 80C, recombinant enzyme
98
deamino-NADP+
-
-
288
NAD+
-
25C, pH 8.0
1100
NAD+
-
pH 7.4, 80C, recombinant enzyme
34
NADP+
-
25C
174
NADP+
-
25C, pH 8.0
207
NADP+
-
25C, pH 8.0, mutant enzyme G163S
249
NADP+
-
25C, pH 8.0, mutant enzyme G163D
251
NADP+
-
25C, pH 8.0, wild-type enzyme
3500
NADP+
-
pH 7.4, 80C, recombinant enzyme
2100
thio-NAD+
-
pH 7.4, 80C, recombinant enzyme
8000
thio-NADP+
-
pH 7.4, 80C, recombinant enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
56
NAD+
-
25C, pH 8.0
7
23200
NADP+
-
25C, pH 8.0
10
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0048
5alpha-Androstan-3beta-ol-17-one
-
substrate D-glucose 6-phosphate, pH 7.6, temperature not specified in the publication; substrate NADP+, pH 7.6, temperature not specified in the publication
0.0136
6-phosphogluconate
-
Kis, variable substrate D-glucose 6-phosphate
0.00226
ammonia
-
-
643.5
amoxicillin
Chalcalburnus tarischii
-
25C, pH 8.5
6.5
ATP
-
pH 8.0, 25C
16.61
ATP
-
pH 8.0, 25C
2.034
Cd2+
-
pH 6.0, 25C
2.26
Ciprofloxacin
Chalcalburnus tarischii
-
25C, pH 8.5
0.0047
Co2+
-
pH 7.5
1.721
Cu2+
-
pH 6.0, 25C
2.63
cypermethrin
-
-
0.1053
D-glucose 6-phosphate
-
pH 7.6, temperature not specified in the publication
0.0215
dehydroandrosterone
-
substrate D-glucose 6-phosphate, pH 7.6, temperature not specified in the publication
0.0223
dehydroandrosterone
-
substrate NADP+, pH 7.6, temperature not specified in the publication
0.0011
dehydroepiandrosterone
-
in the presence of NADP+
0.0017
dehydroepiandrosterone
-
in the presence of D-glucose 6-phosphate
1.84
deltamethrin
-
-
0.00046
epiandrosterone
-
in the presence of NADP+
0.00049
epiandrosterone
-
in the presence of D-glucose 6-phosphate
0.197
Fe2+
-
pH 6.0, 25C
0.308
gentamicin sulfate
-
pH 8.0, 25C
13.8
glucosamine 6-phosphate
-
Kis, variable substrate: NADP+
35.1
glucosamine 6-phosphate
-
Kii, variable substrate: NADP+
0.542
Hg2+
-
pH 6.0, 25C
0.0002
KMnO4
Chalcalburnus tarischii
-
25C, pH 8.5
0.0446
marcaine
-
-
0.392
metamizol
-
-
0.112
NADH
-
pH 8.0, 25C
0.023
NADP+
-
pH 7.5
0.00195
NADPH
-
Kis, variable substrate NADP+
0.01
NADPH
-
pH 8.0, temperature not specified in the publication, varied substrate: NADP+
0.012
NADPH
-
pH 7.4, 37C
0.02
NADPH
-
pH 7.5, versus NADP+
0.025
NADPH
-
versus D-glucose 6-phosphate, pH 8.0, 25C
0.0378
NADPH
-
Kis, variable substrate D-glucose 6-phosphate
0.038
NADPH
-
25C, pH 8.0, competitive inhibition constant
0.04
NADPH
-
pH 8.0, temperature not specified in the publication, varied substrate: glucose 6-phosphate, slope inhibition constant
0.04
NADPH
-
versus NADP+, pH 8.0, 25C
0.041 - 0.043
NADPH
-
pH 7.5, versus D-glucose 6-phosphate
0.05
NADPH
-
G6PDH activity extracted from source leaves of wild-type tobacco Xanthi cultivars
0.051
NADPH
-
G6PDH activity extracted from source leaves of wild-type tobacco SNN cultivars
0.059
NADPH
-
25C
0.06
NADPH
Q8L743
-
0.11
NADPH
-
pH 7.4, 80C, recombinant enzyme
0.161
NADPH
-
pH 8.0, 25C
0.18
NADPH
-
pH 8.0, temperature not specified in the publication, varied substrate: glucose 6-phosphate, intercept inhibition constant
0.279
NADPH
-
Kii, variable substrate D-glucose 6-phosphate
2.09
NADPH
-
25C, pH 8.0, non-competitive inhibition constant
1.178
nidazole
Chalcalburnus tarischii
-
25C, pH 8.5
0.213
Pb2+
-
pH 6.0, 25C
0.748
penicillin G potassium
-
pH 8.0, 25C
0.748
pental sodium
-
-
16.55
propoxur
-
-
0.032
sulfanilacetamide
Chalcalburnus tarischii
-
25C, pH 8.5
0.037
sulfanilamide
Chalcalburnus tarischii
-
25C, pH 8.5
0.00186
Urea
-
-
1.466
Vancomycin
-
-
1.88
Vancomycin
Chalcalburnus tarischii
-
25C, pH 8.5
0.0066
Zn2+
-
pH 7.5
2.77
Zn2+
-
pH 6.0, 25C
12.12
MgSO4
-
-
additional information
additional information
-
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00018
(2R,3R)-2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-3,4-dihydro-2H-chromen-3-yl 3,4,5-trihydroxybenzoate
-
-
0.00025
(2R,3R)-5,7-dihydroxy-2-(3,4,5-trihydroxyphenyl)-3,4-dihydro-2H-chromen-3-yl 3,4,5-trihydroxybenzoate
-
-
0.00024
(2S,3R)-2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-3,4-dihydro-2H-chromen-3-yl 3,4,5-trihydroxybenzoate
-
-
0.00023
(2S,3R)-5,7-dihydroxy-2-(3,4,5-trihydroxyphenyl)-3,4-dihydro-2H-chromen-3-yl 3,4,5-trihydroxybenzoate
-
-
0.0018
2-[(E)-(4-nitrocyclohexa-2,4-dien-1-yl)(2-phenylhydrazinylidene)methyl]benzene-1,4-diol
-
pH 7.5, temperature not specified in the publication
0.0039
4-fluoro-N-(4-hydroxynaphthalen-1-yl)benzenesulfonamide
-
pH 7.5, temperature not specified in the publication
0.00097
4-methyl-3-(propan-2-yloxy)-6H-benzo[c]chromen-6-one
-
pH 7.5, temperature not specified in the publication
0.000216
5alpha-androstan-16-alpha-bromo-3beta-ol-17-one
-
pH 7.6, temperature not specified in the publication
0.025
5alpha-Androstan-3beta-ol-17-one
-
pH 7.6, temperature not specified in the publication
0.000086
5alpha-androsten-16-alpha-bromo-3beta-ol-17-one
-
pH 7.6, temperature not specified in the publication
0.0187
ammonia
-
inhibition in vitro and in vivo at sublethal concentration of 0.0022-0.0055 mM, IC50: 0.0187 mM
1007
amoxicillin
Chalcalburnus tarischii
-
25C, pH 8.5
1.97
Cd2+
-
pH 6.0, 25C
0.33
ceftriaxone
-
-
7.69
Ciprofloxacin
Chalcalburnus tarischii
-
25C, pH 8.5
1.19
Cu2+
-
pH 6.0, 25C
0.63
cypermethrin
-
-
0.0056
dehydroandrosterone
-
pH 7.6, temperature not specified in the publication
12
deltamethrin
-
-
0.39
Fe2+
-
pH 6.0, 25C
0.87
Hg2+
-
pH 6.0, 25C
0.001
KMnO4
Chalcalburnus tarischii
-
25C, pH 8.5
1.54
lidocaine
-
-
0.0012
meloksikam
-
-
0.57
metamizol
-
-
0.0053
N-(4-hydroxynaphthalen-1-yl)-2,5-dimethylbenzenesulfonamide
-
pH 7.5, temperature not specified in the publication
-
1.15
nidazole
Chalcalburnus tarischii
-
25C, pH 8.5
0.78
Pb2+
-
pH 6.0, 25C
28.17
prilocaine
-
-
1.02
propoxur
-
-
0.075
sulfanilacetamide
Chalcalburnus tarischii
-
25C, pH 8.5
0.119
sulfanilamide
Chalcalburnus tarischii
-
25C, pH 8.5
0.0000036
Tl+
-
201Tl solution, pH 8.5, 25C
0.0238
Urea
-
inhibition in vitro and in vivo at sublethal concentration of 0.02-0.05 mM, IC50: 0.0238 mM
1.18
Vancomycin
Chalcalburnus tarischii
-
25C, pH 8.5
2.16
Zn2+
-
pH 6.0, 25C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.007 - 0.009
-
cellular extract
0.025
-
cells grown on a phosphate-deficient medium TRP
0.045
-
cells grown on a phosphate-deficient medium TRP
0.077
-
nephridic enzyme
0.09
-
cells grown on a phosphate-sufficient minimal medium M9
0.098
-
cells grown on a phosphate-sufficient minimal medium M9
0.327
-
hepatic enzyme
0.346
-
crude extract, pH 8.0, 25C
0.64
-
crude enzyme in optimized culture
1.83
-
purified enzyme
2.15
-
partially purified enzyme
2.15
-
purified enzyme
4.64
-
purified enzyme
5.7
-
pH 8.0, temperature not specified in the publication
8.35
-
pH 8.5, 25C
11.23
Q43727
purified G6PDH1 upon reduction by reduced DTT
14
-
purified enzyme
15.43
-
purified enzyme
16.24
-
purified enzyme
16.7
-
purified enzyme
20.3
Q43727
purified G6PDH1
22.2
-
untreated fruits
27.5
-
purified wild-type enzyme
27.69
-
purified kidney cortex enzyme
32
-
purified enzyme, pH and temperature not specified in the publication
33.8
-
25C, pH 7.8, substrates: D-glucose 6-phosphate and NADP+
36.25
-
purified enzyme, pH 6.0, 25C
36.3
-
fruits treated with benzo-thiadiaziole-7-carbothioic acid S-methyl ester
44.16
-
purified enzyme
50
-
purified isoenzyme I
52
-
purified isoenzyme II
53.8
-
purified enzyme
54.1
-
purified enzyme
67.6
-
39C, pH 7.8, substrates: D-glucose 6-phosphate and NADP+
76
-
purified recombinant enzyme, development of a coupled continuous thermostable assay method, determination at 85C
100
-
25C, pH 8.0, high-level glucose-6-phosphate dehydrogenase strain DF82
104
-
25C, pH 8.0, wild-type strain K-10
130
-
purified enzyme
130
-
purified recombinant mutant R393H
135
-
purified recombinant mutant R393E
139.5
Q43727
purified G6PDH1 upon oxidation by diamide
166
-
purified recombinant mutant R393V
176
-
purified recombinant mutant R393L
178
-
purified recombinant mutant R393G
180
-
purified recombinant wild-type enzyme
181
-
purified recombinant mutant R393I
201
-
purified isoenzyme II
210
-
purified isoenzyme I
220
-
purified enzyme
222.8
-
recombinant from Escherichia coli
289.6
G1EHI3
purified recombinant His-tagged enzyme, pH 7.5, 25C
480
-
purified enzyme
745
-
purified enzyme
790
-
purified enzyme
1033
-
cofactor: NADP+, G6PDH-2
1077
-
cofactor: NAD+, G6PDH-2
2890
-
cofactor: NADP+, G6PDH-1
3078
-
cofactor: NAD+, G6PDH-1
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
steady state kinetics
additional information
-
isoform A(-) shows about ten times lower specific activity than isoform A(+)
additional information
-
detection by ultrastructural enzyme-cytochemistry
additional information
-
quantification by in situ hydridization and immunohistochemistry
additional information
-
assay under nitrogen atmosphere
additional information
-
in-gel staining of purified native enzyme
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5
-
in 0.05 M sodium citrate buffer
6.7 - 7.8
-
-
7.2
-
assay at
7.4 - 8.2
-
-
7.4
-
-
7.4
-
assay at
7.5
-
assay at
7.5
-
assay at
7.5
G1EHI3
assay at
7.5
-
assay at
8 - 8.2
-
-
8 - 9
-
-
8 - 9
Penicillium duponti
-
-
8
-
recombinant enzyme
8
-
assay at
8
-
wild-type enzyme
8
-
assay at
8
-
assay at
8
-
assay at
8
-
G6PDH-1; G6PDH-2
8
-
assay at
8
-
assay at
8.3
-
isoform A(+)
8.5 - 9.5
-
-
8.5
-
mutant enzymes 1 and 3
9
-
isoform A(-)
9
-
mutant enzyme 2
10
-
in 0.5 M glycine-KOH buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
-
pH profile
5.9 - 9
-
50% of maximal activity at pH 5.9 and pH 9.0
6 - 8.5
-
recombinant enzyme
6 - 9
-
-
6.2 - 9.8
-
pH 6.2: about 50% of maximal activity, pH 9.8: about 50% of maximal activity
6.5 - 10
-
-
7.4 - 8.2
-
-
7.5 - 9.5
-
about 50% of maximal activity at pH 7.5 and pH 9.5
additional information
-
high pH value inactivates the enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
-
assay at room temperature
22
-
assay at room temperature
25
-
assay at
25
-
assay at
25
Penicillium duponti
-
assay at
25
-
assay at
25
-
assay at
25
-
assay at
25
-
assay at
25
-
assay at
25
-
assay at
25
G1EHI3
assay at
25
-
assay at
28
-
assay at
30
-
assay at
30
-
assay at
30
-
G6PDH-1; G6PDH-2
37
-
assay at
37
-
assay at
37
-
wild-type enzyme
40
-
mutant enzymes 1 and 3
45
-
mutant enzyme 2
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 60
-
temperature profile
70 - 90
-
over 60% of maximal activity at 70C and 90C, recombinant enzyme
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.85
-
isoelectric focusing, pH-gradient: 3.5-7.0, three isoforms with pI: 5.5, 5.3 and 4.85
5.3
-
isoelectric focusing, pH-gradient: 3.5-7.0, three isoforms with pI: 5.5, 5.3 and 4.85
5.5
-
isoelectric focusing, pH-gradient: 3.5-7.0, three isoforms with pI: 5.5, 5.3 and 4.85
5.7
-
isoelectric focusing, pH-range 3-10, G6PDH-2
6.4
-
isoelectric focusing, pH-range 3-10, G6PDH-1
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
G6PD is more than 2fold higher in pulmonary arteries compared with coronary arteries
Manually annotated by BRENDA team
-
negative correlation between locomotion of rats in the open field and activity of G-6-PDH in the sensorimotor cortex, especially in efferent layer V neurons and neurons of the caudate nucleus and nucleus accumbens, which attests to different capacity of the brain in Wistar rats with high and low open-field locomotion to regeneration of phosphopyridine nucleotides (NADP(+)) and production of pentoses via the pentose phosphate shunt. No correlation between enzyme activity in the hippocampus and locomotion
Manually annotated by BRENDA team
-
glucose-6-phosphate dehydrogenase plays a central role in modulating reduced glutathione levels in reed callus under salt stress
Manually annotated by BRENDA team
-
KlZWF1 is constitutively expressed. Its deletion leads to increased sensitivity to hydrogen peroxide on glucose. The Klzwf1DELTA strain has a reduced biomass yield on fermentative carbon sources as well as on lactate and glycerol
Manually annotated by BRENDA team
-
the highest glucose 6-phosphate dehydrogenase activity occurrs when the glucose solution is fed into the fermenter through the decreasing linear mode
Manually annotated by BRENDA team
-
of vile ducts and blood vessel walls in portal tracts
Manually annotated by BRENDA team
-
G6PD deficiency is associated with premature senescence of human fibroblasts
Manually annotated by BRENDA team
-
enzyme is stimulated in presence of 3 mg and 5 mg of Cd on the first day of experiment in gill, liver and kidney tissues. The stimulation effect of the 5 mg/l dose of Cd on G6PD and 6PGD enzyme activities is significantly diminished after seven days. The G6PD enzyme activity levels are stimulated by approximately 60% in gills
Manually annotated by BRENDA team
-
primary hepatocyte
Manually annotated by BRENDA team
-
enzyme activity of G6PD enzyme is significantly stimulated after three days in liver and kidney tissues at a dose of 1 mg/l Cdand is stimulated on the first day of experiment in gill, liver and kidney tissues at doses of 3 and 5 mg/l Cd. The stimulation effect of the 5 mg/l dose of Cd on G6PD and 6PGD enzyme activities is significantly diminished after seven days. The G6PDenzyme activity levels are stimulated by approximately 67% in kidney
Manually annotated by BRENDA team
-
resident liver macrophage, from sinusoidal lumen
Manually annotated by BRENDA team
Chalcalburnus tarischii
-
-
Manually annotated by BRENDA team
-
daily rhythm of G6PDH activity follows a seasonal pattern
Manually annotated by BRENDA team
-
enzyme activity of G6PD enzyme is significantly stimulated after three days in liver and kidney tissues at a dose of 1 mg/l Cd and is stimulated on the first day of experiment in gill, liver and kidney tissues at doses of 3 and 5 mg/l Cd. The stimulation effect of the 5 mg/l dose of Cd on G6PD and 6PGD enzyme activities is significantly diminished after seven days. The G6PDenzyme activity levels are stimulated by approximately 68% in liver
Manually annotated by BRENDA team
Chalcalburnus tarischii 1811
-
-
-
Manually annotated by BRENDA team
-
G6PD is more than 2fold higher in rat lungs than in rat hearts
Manually annotated by BRENDA team
-
in patients with type 1 diabetes G6PDH activity does not differ from control group, but enzyme activity is sharply decreased in pregnant women with type 2 diabetes and gestational diabetes
Manually annotated by BRENDA team
-
pregnant women, G6PD translocates to microtubule-organizing centers
Manually annotated by BRENDA team
-
high glucose level of 25 mM leads to a decrease in G6PD activity and protein level in islets
Manually annotated by BRENDA team
-
extralesional and wild-type, the lesions show a 20fold higher, and extralesional parenchyma a 2fold higher, virtual flux at physiological substrate concentrations compared to normal parenchyma
Manually annotated by BRENDA team
-
glucose-6-phosphate dehydrogenase plays a pivotal role in nitric oxide-involved defense against oxidative stress under salt stress in red kidney bean roots
Manually annotated by BRENDA team
-
murine thymic lymphoma cells
Manually annotated by BRENDA team
additional information
-
distribution pattern
Manually annotated by BRENDA team
additional information
-
fermentation on rice straw hemicellulosic hydrolysate, evaluation and optimization of enzyme production, modeling, overview
Manually annotated by BRENDA team
additional information
-
different patterns of glucose-6-phosphate dehydrogenase activities are observed among strains Tulahuen S and Y along the growth curve and when cells are challenged with H2O2
Manually annotated by BRENDA team
additional information
-
G6PDH-2 is detected throughout the growth phase, the enzyme is detected throughout the growth phase. The substantial increase in G6PDH-1 observed at stationary phase or as the results of external oxidative stress indicates that this enzyme is inducible under stressful environmental conditions
Manually annotated by BRENDA team
additional information
-
G6PD activity is higher in healthy small rather than large follicles, with similar glutathione concentration in both cases. Activity of G6PD decreases in atretic small follicles, but not in large ones. Specific activity of G6PD and glutathione concentrations in the atretic follicular fluid are lower than those in granulosa cells (10- and 5times respectively) in all kind of follicles. The higher G6PD activity in the small follicles may be related to granulosa cell proliferation, follicular growth, and a lower sensitivity to oxidative stress when compared with large follicles. Lower G6PD activity in large follicles indicating a higher susceptibility to oxidative stress associates to apoptosis progression in follicle atresia
Manually annotated by BRENDA team
additional information
-
cultivated at 10C under continuous illumination
Manually annotated by BRENDA team
additional information
Meyerozyma guilliermondii FTI 20037
-
fermentation on rice straw hemicellulosic hydrolysate, evaluation and optimization of enzyme production, modeling, overview
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
cytosolic G6PDH seems to be a crucial factor for the outcome of plant defense responses
Manually annotated by BRENDA team
-
liver, lungs and heart
Manually annotated by BRENDA team
Arabidopsis thaliana T87
-
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae W303-181
-
-
-
Manually annotated by BRENDA team
-
liver, lungs and heart
-
Manually annotated by BRENDA team
-
isozyme, not in chloroplast
Manually annotated by BRENDA team
-
plastidic isozymes P1 and P2 are regulated by redox regulation
Manually annotated by BRENDA team
Arabidopsis thaliana T87
-
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae W303-181
-
-
-
-
Manually annotated by BRENDA team
additional information
-
the levels of transcripts are low at day 0 and increase markedly at day 1, then gradually decrease
-
Manually annotated by BRENDA team
additional information
Arabidopsis thaliana T87
-
the levels of transcripts are low at day 0 and increase markedly at day 1, then gradually decrease
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10000
-
dimeric apoenzyme, gel filtration
689915
50000
-
about, native PAGE
657284
57500
-
about, recombinant enzyme, native PAGE
654181
73200
-
gel filtration
656419
75000
-
gel filtration
655712
77600
-
gel filtration
657147
95000
-
gel filtration, recombinant enzyme
655612
100000
-
gel filtration, refolded protein
696962
103000 - 110000
-
gel filtration
286976, 286977
103000 - 110000
-
gel electrophoresis
286978
103000 - 110000
-
gel filtration
286983
105000
-
gel filtration
674379
107000
-
-
730067
110000
-
G6PDH-2, gel filtration
688308
112000
-
gel filtration
287006
114000
-
dimer dimerization to MW 209000 in presence of NADP+, gel filtration
286996
117000
-
gel filtration
287015
118000 - 120000
-
three principal forms with MW of 120000 Da, 240000 Da and 345000 Da, gel electrophoresis
286986
118000 - 120000
-
gel filtration
286987
118000 - 120000
-
sucrose density gradient centrifugation
286992
120000
-
gel filtration
656382
121000
-
gel filtration
287014
126000
Penicillium duponti
-
gel filtration
286982
130000
-
G6PDH-1, gel filtration
688308
134000
-
gel filtration
689323
138000
-
gel filtration
286999
144000
-
gel filtration
723699
150000
-
gel filtration
286819
158000
-
gel filtration
287012
160000
-
gel filtration
287005
180000
-
gel filtration
286995
180000
-
gel filtration
287005
200000
-
gel filtration
287001
200000
-
gel filtration, native enzyme
696962
206000
-
gel electrophoresis
286978
210000
-
-
286984
220000
-
Entner-Doudoroff enzyme, gel chromatography
286985, 286993
220000
-
isoenzymes I and II, gel filtration
287017
238700
-
ultracentrifugation
286980
240000
-
three principal forms with MW of 120000 Da, 240000 Da and 345000 Da, gel electrophoresis
286986
240000
-
gel filtration
286988
240000
-
-
286991
240000
-
gel filtration
286998
265000
-
Zwischenferment, gel chromatography
286985, 286993
274000
-
-
722212
300000
-
recombinant His-tagged enzyme, gel filtration
723340
345000
-
three principal forms with MW of 120000 Da, 240000 Da and 345000 Da, gel electrophoresis
286986
additional information
-
native PAGE
655736
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 52000, SDS-PAGE
?
G1EHI3
x * 63000, SDS-PAGE
?
-
? * 59000, SDS-PAGE, native and recombinant from Escherichia coli
?
-
? * 55000 + ? * 53000, SDS-PAGE
?
-
? * 50000 SDS-PAGE
?
-
? * 60000 + ? * 57000, SDS-PAGE
?
-
? * 56000, SDS-PAGE
?
-
59000-60000, wild-type and mutant enzymes, SDS-PAGE
?
-
x * 53100, SDS-PAGE
?
-
x * 59500, calculated from sequence
?
-
x * 48500, SDS-PAGE
?
Escherichia coli K-10, Escherichia coli DF82
-
x * 52000, SDS-PAGE
-
dimer
-
2 * 55000, SDS-PAGE
dimer
-
2 * 62000, SDS-PAGE
dimer
-
2 * 62000, SDS-PAGE
dimer
-
2 * 57000, SDS-PAGE
dimer
-
2 * 57000, SDS-PAGE
dimer
-
2 * 52000, SDS-PAGE
dimer
-
2 * 54000, SDS-PAGE
dimer
-
2 * 68000, SDS-PAGE
dimer
-
2 * 52500, SDS-PAGE
dimer
-
2 * 61000
dimer
-
2 * 58000, SDS gel electrophoresis
dimer
-
2 * 61000, SDS gel electrophoresis
dimer
-
2 * 55300, SDS-PAGE
dimer
-
2 * 66880, SDS-PAGE
dimer
-
2 x 60000, alpha2, recombinant enzyme, SDS-PAGE
dimer
-
2 * 60000, G6PDH-2, SDS-PAGE
dimer
-
gel filtration, the refolded protein intermediates shift from dominant monomer to dimer, the gradual emergence of dimer correlating well with the regain of enzyme activity
dimer
Schizosaccharomyces pombe NCYC 132S2-2
-
2 * 57000, SDS-PAGE
-
homotetramer
-
4 * 68400, SDS-PAGE
monomer
-
1 x 48000, SDS-PAGE
monomer
-
1 x 57500, recombinant enzyme, SDS-PAGE
monomer
-
1 x 73180, SDS-PAGE
monomer
-
1 x 74400, SDS-PAGE
tetramer
-
-
tetramer
-
gel filtration
tetramer
-
4 * 60000, SDS-PAGE
tetramer
-
4 * 60000, SDS-PAGE
tetramer
-
4 * 60000, SDS-PAGE
tetramer
-
4 * 57000, SDS-PAGE
tetramer
-
4 * 57000, SDS-PAGE
tetramer
-
4 * 31000, SDS-PAGE
tetramer
-
4 * 48000, SDS-PAGE
tetramer
-
4 * 52000, SDS-PAGE
tetramer
-
4 * 52000, SDS-PAGE
tetramer
-
4 * 53000, SDS-PAGE
tetramer
-
4 * 65000, Zwischenferment, 4 * 55000, Entner-Doudoroff enzyme
tetramer
-
4 * 35200, G6PDH-1, SDS-PAGE
tetramer
-
partial dimerization of the G6PDH tetramer on ethanol
tetramer
-
4 * 75000, recombinant His-tagged enzyme, SDS-PAGE
monomer
-
1 x 79300, SDS-PAGE
additional information
-
presence of SH-reagents, high enzyme and Mg2+ or Mn2+ concentrations, low pH and ionic strength favour oligomeric, active forms of the enzyme, while the opposite conditions favour inactive monomers
additional information
G1EHI3
structure modeling
additional information
-
low pH value and low ionic strength cause aggregation of the enzyme in active oligomeric forms, e.g. as tetramer or hexamer
additional information
-
modeling of subunit interface reveals the importance of cysteine residues for oligomeric integrity
additional information
-
molecular modeling of the tertiary structure of wild-type and mutant enzymes
additional information
-
rBmG6PD is composed of 37% alpha-helices and 26% beta-sheets
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N-terminally truncated enzyme mutant DELTA37N, sitting drop vapour diffusion method, from 20 mMTris-HCl, pH 8.0, and 5 mM D-glucose 6-phosphate, mixing of 0.002 ml reservoir solution, containing 6% PEG 400, 1.6 M ammonium sulfate, 0.1 M HEPES pH 7.5 without D-glucose 6-phosphate and 4% PEG 400, 1.8 M ammonium sulfate, 0.1 M Na HEPES pH 7.5, with D-glucose 6-phosphate, with 0.002 ml of protein solution, containing 20 mg/ml and 33 mg/ml protein, respectively, followed by equilibration against 0.09 ml of reservoir solution, 4 days, X-ray diffraction structure determination and analysis at 2.85-3.35 A resolution, molecular replacement
Q1WBU6
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 10
-
stable
286988
5.4 - 7
Penicillium duponti
-
highest stability
286982
6 - 10.5
-
stable at 5C for 48 h
286987
6 - 10.5
-
stable at 5C for 48 h
286993
6
-
optimally stable at
657147
6.5 - 10
-
Entner-Doudoroff enzyme stable
286985, 286993
6.5 - 10
-
stable, purified enzyme
673156
8 - 10.5
-
the enzyme displays a peak of activity at pH 10 in glycine-KOH buffer and is half-maximally active in this buffer at pH 8 and at pH 10.5
677998
8.5
-
stable
656382
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 30
-
activity is increased 2-3fold by heating at 25C (either at pH 10 in 0.5 M glycine KOH buffer or at pH 5 in 0.05 M sodium citrate buffer) prior to assay, the stimulation is reversed by chilling to 0C but is not reversed at temperatures between 20C and 30C
677998
4
-
inactivation at 4C is partially reversed at room temperature, especially with added NADP+
689915
5
-
48 h
286987
25
-
half-life: 15 min
286998
30
-
1 month
287001
37
-
pH 7.2, 24 h: wild-type enzyme loses 42% of its initial activity, mutant enzyme G163S loses 73% of its initial activity, mutant enzyme G163D loses 94% of its initial activity. Stability of all three enzymes is enhanced by addition of NADP+
689022
37
-
the stripped enzyme, much less stable than holoenzyme, inactivates irreversibly within 2 d
689915
45
-
60 min, the wild-type enzyme is completely stable, the mutant P409R shows 86% reduced thermal stability compared to the wild-type enzyme
655123
47
-
50 min, the enzyme is completely inactivated either in the cell free extract or in the concentrated fraction. The thermodynamic parameters of G6PD thermal inactivation suggests the occurrence of two inactivation events both related to breaking of bonds responsible for the active dimer integrity: one, prevailing at low temperature, likely led to the formation of a less active dimer, while the other, prevailing at high temperature, is responsible for the formation of a totally inactive dimer or monomer
686448
50
-
purified recombinant His-tagged enzyme, inactivation
723340
55
-
completely inactivated in 15 min
286988
55
-
purified enzyme, rapid and irreversible inactivation, half life: 3.2 min, in presence of substrate D-glucose 6-phosphate 7.5 min
674379
70
-
120 min, no loss in activity
655612
70
-
30 min, G6PDH-1 retains 40% of its activity; 30 min, G6PDH-2 retains 35% of its activity
688308
80
-
120 min, 20% loss in activity
655612
80
-
very sensitive to moist heat at 80C
678997
90
-
half-life: 24 h
655518
95 - 100
-
120 min, almost complete loss in activity
655612
100
-
half-life: 12 h
655518
additional information
-
mutant enzymes are more thermostable than the wild-type enzyme
656387
additional information
-
at physiological temperatures the mutant enzymes looses only 10% of their activity after 20 min in the presence of 0.01 mM NADP+
673944
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
EDTA stabilizes
-
thioglycolate stabilizes
-
unfolding equilibrium of rBmG6PD with GdmCl/urea shows the triphasic unfolding pattern along with the highly stable intermediate obtained by GdmCl
-
isoform A(-) is less stable during purification than A(+) due to V68M mutation that makes it suceptible to oxidation of sulfhydryl group
-
NADP+ stabilizes, while the enzyme is rapidly inactivated in presence of substrate glucose 6-phosphate
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimethylsulfoxide
-
substrate glucose and 40% DMSO (v/v): 10% remaining enzyme activity in HEPES buffer, 20% remaining enzyme activity in phosphate buffer
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 100 mM Tris-HCl buffer, pH 7.9, several months
Q43727
5C, pH 6.0-10.5, stable for 48 h
-
4C, purified 650fold, several weeks
-
-20C, 0.05 M Tris-Cl buffer containing 1 mM glucose 6-phosphate, pH 7.5, stable for over 2 months
-
30C, Bacillus stearothermophilus enzyme maintains more than 80% of activity after 1 month
-
-10C, 10 mM Tris-HCl, pH 7.4, 5 mM 2-mercaptoethanol, 2 mM EDTA, 40% glycerol (v/v), weeks
-
4C, several months
-
-20C or -40C, impure state, more than 1 week
Penicillium duponti
-
4C, several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli, to homogeneity by heat precipitation, and nickel affinity chromatography
-
by affinity chromatography, to homogeneity
Q43727
native enzyme 230fold to homogeneity by ammonium sulfate fractionation, affinity chromatography, and gel filtration
-
recombinant His-tagged enzyme from Escherichia coli strain C41 by nickel affinity chromatography
-
recombinant His-tagged enzyme 95.5fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
G1EHI3
2000fold by 2times 2',5'-ADP affinity chromatography and gel filtration
-
-
Chalcalburnus tarischii
-
74fold by ammonium sulfate precipitation and DEAE ion exchange chromatography
-
G6PDH-1; G6PDH-2
-
approximately 100-fold purification; approximately 450fold purification
-
by affinity chromatography, at 4C, 5343fold with a yield of 52%
-
both isoforms A(-) and A(+)
-
isoenzymes I and II
-
native and recombinant from Escherichia coli
-
native wild-type from blood leukocyte, and recombinant wild-type and mutant P409R from Saccharomyces cerevisiae, by 2',5'-ADP affinity chromatography
-
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by 2',5'-ADP affinity chromatography
-
recombinant wild-type and mutant enzymes from G6PD-deficient Escherichia coli strain DF213
-
two varients G6PD(Plymouth) (G163D) and G6PD(Mahidol) (G163S)
-
wild-type and clinical mutants purified to homogeneity
-
wild-type enzyme, 4.1fold from blood by ammonium sulfate precipitation, dialysis, and 2',5'-ADP affinity chromatography
-
rapid partial purifiation from root plastids, 17.7fold
-
native enzyme 90fold by anion exchange and affinity chromatography
-
to homogeneity by a single nickel affinity chromatographic step
-
rapid procedure, 1.58fold by ammonium sulfate precipitation and ADP resin chromatography
-
by ammonium sulfate precipitation and affinity chromatography, 1691fold, with a yield of 63%
-
native enzyme 1010fold from liver by 2',5'-ADP affinity chromatography
-
native enzyme 1600fold from erythrocytes by ammonium sulfate fractionation, and 2',5'-ADP affinity chromatography to homogeneity
-
native enzyme 2488fold from hemolysate by ammonium sulfate, dialysis, and 2',5'-ADP affinity chromatography
-
1189fold by ammonium sulfate precipitation and 2',5'-ADP affinity chromatography
-
native enzyme 1384fold from kidney cortex by ultracentrifugation, 2',5'-ADP affinity and anion exchange chromatography
-
-
Penicillium duponti
-
58fold from leaves by ammonium sulfate precipitation and DEAE ion exchange chromatography
-
by homogenate precipitation, ammonium sulfate precipitation and ion exchange chromatography, at 4C, 124.8fold, with a yield of 57.6%
-
native enzyme by blue native PAGE to homogeneity, method optimization, overview
-
978fold from small intestine, by ammonium sulfate precipitation, dialysis, and DEAE ion exchange and 2',5'-ADP affinity chromatography
-
native enzyme 531fold from kidney, co-purification with 6-phosphogluconate dehydrogenase and glutathione reductase in one chromatographic step by 2',5'-ADP affinity chromatography by using different elution buffers, method development and optimization, overview
-
partial from liver and kidney
-
partial purification of the enzyme from different tissues by ammonium sulfate fractionation and dialysis
-
continuous counter-current purification of glucose-6-phosphate dehydrogenase from Saccharomyces cerevisiae cells by liquid-liquid extraction using reverse micelles. A biocompatible reverse micellar system consisting of 0.05 M soybean lecithin (zwitterionic surfactants) in isooctane with hexanol is employed to study the influence of different flow-rates on G6PD purification. The results show that the reverse micellar system is able to remove proteins (impurities) from the cell-free. The enzyme recovery yield varies from 32% to 115% and G6PD purification factor from 1.0 to 2.2, under flow-rates ranging from 1.6:1.6 mL/min to 6.0:6.0 ml/min for both phases (micellar and aqueous phases). The steady hold-up values demonstrate that the mass transfer capability of this extraction apparatus is practically constant. The continuous counter-current purification system employed proves to be useful for purifying glucose-6-phosphate dehydrogenase and for maintaining the enzyme activity
-
glucose-6-phosphate dehydrogenase from commercial Saccharomyces cerevisiae was concentrated by reverse micelles liquid-liquid extraction using soybean lecithin. Five successive cycles of extraction ensured a G6PD purification factor of 5.4. The kinetic and thermodynamic properties either of the concentrated fraction or the cell free extract are investigated. While the Michaelis constant for glucose-6-phosphate is almost independent of the presence of cell debris, the maximum initial activity is about 16% higher in its absence. The extraction seems to slightly improve both the enzyme activity and stability
-
isoenzymes I and II
-
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
to homogeneity by a single nickel affinity chromatographic step
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli as His-tagged enzyme
-
expressed in Escherichia coli DH5alpha strain from the pASK-G6PDH1 plasmid
Q43727
into vector pET16b and expressed in a G6PDH-deficient Escherichia coli strain. Overexpression in the cytosol of the susceptible tobacco cultivar Xanthi
Q8L743
transient expression of the G6PD5 and G6PD6 fused to a GFP gene, cloned into the SpeI site of pCAMBIA1302. T-DNA insertion lines transformed with cosmid clones containing the regions of G6PD5 and G6PD6 isolated from a genomic cosmid (pBIC20) library
-
recombinant expression of His-tagged enzyme in Escherichia coli strain C41
-
DNA and amino acid sequence determination and analysis, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
G1EHI3
expression in Escherichia coli
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
expression of wild-type and mutant enzymes in the G6PD-deficient Escherichia coli strain DF213
-
gene g6pd is localized in the Xq28 region, DNA sequence determination and analysis and expression of wild-type and mutant P409R in Saccharomyces cerevisiae, functional complementation of the yeast enzyme deficient mutant strain ZWF1 by the wild-type and mutant P409R
-
study of functional complementation of the yeast deletion mutant strain zwf1 by human wild-type and mutant enzymes, construction of a human enzyme mutant library containing all possible single nucleotide missense mutations in the eight-residue glucose 6-phosphate binding peptide of the enzyme
-
the two variants G6PD(Plymouth) (G163D) and G6PD(Mahidol) (G163S) are constructed by site-directed mutagenesis and expressed in G6PD-deficient Escherichia coli DF 213 cells
-
wild-type and clinical mutants expressed in Escherichia coli
-
N-terminally His-tagged recombinant G6PDH expressed in Escherichia coli BL21 transformed with recombinant pET28 plasmid
-
overexpression in WEHI7.2 cells
-
cytosolic isozyme, DNA sequence determination, expression in Escherichia coli
-
DNA and amino acid sequence determination and analysis, functional expression in Escherichia coli strain BL21 as His-tagged enzyme
-
gene gpd, expression in Escherichia coli strain BL21(DE3) as His-tagged enzyme
-
N-terminally His-tagged recombinant G6PDH expressed in Escherichia coli BL21 transformed with recombinant pET28 plasmid
-
expression in Escherichia coli, His-tagged protein
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
high glucose level inhibits G6PD expression
-
the AMPK signaling pathway as well as the inhibitory p38 MAPK pathway are cooperating to inhibit G6PD expression. Arachidonic acid activates AMP-activated protein kinase in primary rat hepatocytes, and this effect is p38 MAPK-dependent. Activation of AMP-activated protein kinase mimics the inhibition by arachidonic acid of the insulin-mediated induction of G6PD. Overexpression of dominant-negative AMP-activated protein kinase abolishes the effect of arachidonic acid on G6PD expression
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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 25C, 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
-
naturally occuring mutation corresponding to the clinical variants G6PD Wisconsin, 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
R393G
-
clinical mutant G6PDWisconsin, 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 25C, displays thermostability as the wild-type and low susceptibility to chymotrypsin digestion
R393H
-
naturally occuring mutation corresponding to the clinical variants G6PD Nashville, 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
R393H
-
clinical mutant G6PDNashville, 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 25C, displays decreased thermostability and high susceptibility to chymotrypsin digestion as compared to the wild-type
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
additional information
-
activities of the cytosolic isoforms G6PD5 and G6PD6 are reciprocally increased in single mutants with no increase of their respective transcript levels. Seeds of the double mutant but not of the single mutants have higher oil content and increased weight compared to those of the wild-type, with no alteration in the carbon to nitrogen ratio or fatty acid composition. Total G6PDH activity is reduced only in the double mutant
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 25C, displays decreased thermostability and high susceptibility to chymotrypsin digestion as compared to the wild-type
additional information
-
G6PD mutations are thought to cause haemolytic anaemia by compromising enzyme stability, phenotypes
additional information
-
study of functional complementation of the yeast deletion mutant strain zwf1 by human wild-type and mutant enzymes, construction of a human enzyme mutant library containing all possible single nucleotide missense mutations in the eight-residue glucose 6-phosphate binding peptide of the enzyme, all mutations of residues Asp200, His201, Lys205 lead to inactive enzymes, some mutations of residues Ile199, Leu203, Arg198, Tyr202, Gly204 result in active, some in inactive enzymes, overview
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
additional information
-
stable overexpression in WEHI7.2 murine thymic lymphoma cells models glucose deprivation and sensitizes lymphoma cells to dexamethasone-induced apoptosis, overview, G6PDH-overexpressing WEHI7.2 cells are more sensitive to oxidative stress and glucocorticoids
additional information
-
construction of a genetically modified yeast using DNA recombination technique and the PGK1 promoter, optimization of pH, temperature, dissolved oxygen, and composition of the culture medium, to achieve a high enzyme production rate, growth through a batch fermentation process, overview
additional information
Saccharomyces cerevisiae W303-181
-
construction of a genetically modified yeast using DNA recombination technique and the PGK1 promoter, optimization of pH, temperature, dissolved oxygen, and composition of the culture medium, to achieve a high enzyme production rate, growth through a batch fermentation process, overview
-
additional information
Q1WBU6
generation of a N-terminally truncated version of the enzyme glucose-6-phosphate dehydrogenase from Trypanosoma cruzi lacking the first 37 residues, mutant DELTA37N
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
inactivated by potassium myristate
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
G6PD deficiency due to its polymorphism causes neonatal jaundice, acute hemolysis in malaria, favism, severe chronic non-spherocytic hemolytic anemia, and lipid dysregulation. G6PD deficiency may be responsible for the high incidence of coronary artery disease among African-Americans and reduces mortality due to ischemic heart disease and cerebrovascular disease in Sardinian males. In Mediterranean and Sardinian G6PD-deficient individuals, G6PD deficiency may confer a partial protection against atherosclerosis, leading to a reduced risk of cardiovascular diseases in G6PD-deficient individuals. G6PD appears to be an attractive therapeutic target for diabetes-induced cardiomyopathy, ischemic cardiomyopathy, pulmonary hypertension, angiotensin II-induced hypertension, vascular smooth muscle hypertrophy and coronary disease in humans
medicine
-
G6PD deficiency is the commonest clinically significant enzymopathy in humans. More than 400 million people worldwide are affected by this condition which may determine favism, drug-induced acute hemolytic anemia, severe chronic nonspherocytic haemolytic anemia, neonatal jaundice and hemolytic anemia associated with viral or microbiological infections. The highest prevalence of G6PD deficiency mainly regards tropical Africa, the Middle East, tropical and subtropical Asia, Papua New Guinea, and various Mediterranean regions, for example Sardinia island. G6PD deficiency may represent a selective advantage due to the increased resistance to severe Plasmodium falciparum infection of the affected individuals. G6PD/pyruvate kinase ratio is more reliable than the G6PD activity alone, for the identification of G6PD heterozygotes, especially in patients with microcytic anemia. G6PD/6PDG ratio is an absolute measure of G6PD deficiency of female carriers
medicine
-
in Vietnam the blackwater fever syndrome is associated with malaria infection, quinine ingestion and G6PD deficiency. G6PD deficiency is a major risk factor for haemoglobinuria in ethnic Vietnamese Kinh and within the G6PD deficient population G6PD Viangchan is significantly associated with haemoglobinuria
medicine
-
refolding protocol can be applied to produce high recovery yield of folded protein with unaltered properties, paving the way for future studies on clinical G6PD mutants with folding defects and providing a useful model system to study the folding process of oligomeric proteins
industry
-
production of abundant intermediates for industrially erythritol production
industry
Moniliella megachiliensis SN-G42
-
production of abundant intermediates for industrially erythritol production
-
drug development
-
the enzyme is a target for anti-parasite drug development
drug development
-
Trypanosoma brucei G6PDH is a valid drug target for human steroids. Inhibition of G6PDH by dehydroepiandrosterone derivatives may lead to the development of a new class of anti-trypanosomatid compounds
drug development
Trypanosoma brucei 427
-
Trypanosoma brucei G6PDH is a valid drug target for human steroids. Inhibition of G6PDH by dehydroepiandrosterone derivatives may lead to the development of a new class of anti-trypanosomatid compounds
-
additional information
Q8L743
because isoenzyme replacement of G6PDH in the cytosol of tobacco is beneficial under various kinds of cues, this strategy may be a tool to enhance stress tolerance in general
additional information
-
loss of cytosolic G6PDH activity affects the metabolism of developing seeds by increasing carbon substrates for synthesis of storage compounds rather than by decreasing the NADPH supply specifically for fatty acid synthesis
medicine
-
fluoride-containing bioactive glasses as used in tissue engineering as well as bone repair, inhibit the pentose phosphate oxidative pathway and the glucose 6-phosphate dehydrogenase activity. The effects are ascribable to the fluoride content/release of glass powders, they are mimicked by NaF solutions and are prevented by radical scavengers dimethyl sulfoxide and tempol, by superoxide dismutase, and by glutathione, but not by apocynin
additional information
-
evaluation and optimization of enzyme production in Candida guilliermondii, modeling, overview
additional information
Meyerozyma guilliermondii FTI 20037
-
evaluation and optimization of enzyme production in Candida guilliermondii, modeling, overview
-