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Information on EC 1.1.1.49 - glucose-6-phosphate dehydrogenase (NADP+) and Organism(s) Homo sapiens and UniProt Accession P11413

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IUBMB Comments
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)+] and EC 1.1.1.388, glucose-6-phosphate dehydrogenase (NAD+).
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This record set is specific for:
Homo sapiens
UNIPROT: P11413
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
g6pd, glucose-6-phosphate dehydrogenase, g6pdh, g-6-pd, glucose 6-phosphate dehydrogenase, g-6-pdh, g-6pd, zwf-1, glucose-6-phosphate 1-dehydrogenase, glc6pdh, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glucose 6-phosphate dehydrogenase
-
glucose-6-phosphate dehydrogenase
-
6-phosphoglucose dehydrogenase
-
-
-
-
D-glucose 6-phosphate dehydrogenase
-
-
-
-
Entner-Doudoroff enzyme
-
-
-
-
G6PD1
-
-
-
-
G6PD2
-
-
-
-
G6PD3
-
-
-
-
G6PD4
-
-
-
-
G6PD5
-
-
-
-
G6PD6
-
-
-
-
G6PDH
-
-
G6PDH1
-
-
-
-
G6PDH2
-
-
-
-
G6PDH3
-
-
-
-
G6PDH4
-
-
-
-
G6PDH5
-
-
-
-
G6PDH6
-
-
-
-
glucose 6-phosphate dehydrogenase
-
-
glucose 6-phosphate dehydrogenase (NADP)
-
-
-
-
glucose-6-phosphate 1-dehydrogenase
-
-
-
-
glucose-6-phosphate dehydrogenase
NADP-dependent glucose 6-phophate dehydrogenase
-
-
-
-
NADP-glucose-6-phosphate dehydrogenase
-
-
-
-
VEG11
-
-
-
-
Vegetative protein 11
-
-
-
-
Zwischenferment
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-glucose 6-phosphate + NADP+ = 6-phospho-D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
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)+] and EC 1.1.1.388, glucose-6-phosphate dehydrogenase (NAD+).
CAS REGISTRY NUMBER
COMMENTARY hide
9001-40-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
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+
?
show the reaction diagram
-
-
-
-
?
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-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 + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
show the reaction diagram
additional information
?
-
-
both isoenzymes show no activity with glucose and NAD+, isoenzyme I shows no activity with 6-phosphonogluconate
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + 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 + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
deamino-NADP+
-
-
NADP+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
activation
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
Sodium acetate
-
at 400 mM regains 58% activity on refolding
additional information
-
no metal ions necessary
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
brimonidine
competitive inhibition
Trypsin
after 2 h of trypsin digestion in the presence of 0.01 mM NADP+ the enzyme retains about 57% of its original activity
-
2,3-diphosphoglycerate
-
-
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
chymotrypsin
-
-
-
dehydroepiandrosterone
-
non-competitively inhibits
EDTA
-
slightly
epiandrosterone
-
non-competitively inhibits
glucose
-
high glucose level of 25 mM leads to a decrease in G6PD activity and protein level in islets
guanidinium hydrochloride
metamizol
-
inhibition of wild-type and mutant enzyme 3
NADP+
NADPH
netilmicin
-
inhibition of wild-type and mutant enzymes 1-3
palmitoyl-CoA
-
leads to dissociation of active tetramers to inactive dimers
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
Tl+
-
201Tl solution and radiation exposure has inhibitory effects on the enzyme activity both in vivo and in vitro
Zn2+
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
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
glycerol
-
marginally increases the refolding yield in the presence of Arg, and it is unable to replace Arg in promoting a high refolding yield
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
metamizol
-
activation of mutant enzymes 1 and 2
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
-
streptomycin
-
activation of mutant enzymes 1 and 2
trehalose
-
marginally increases the refolding yield in the presence of Arg, and it is unable to replace Arg in promoting a high refolding yield
additional information
-
temperature and protein concentration have positive influence on refolding. Refolding at 25°C 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 30°C, refolding is faster in the early stages than at 25°C, 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 25°C. Correct refolding is severely suppressed at 37°C, 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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0478 - 50.7
D-glucose 6-phosphate
0.0072 - 6.46
NADP+
0.374
2-deoxy-D-glucose 6-phosphate
-
pH 8.0, 25°C, recombinant mutant R454C, with NADP+
0.864
6-phosphonogluconate
-
isoenzyme II
0.031 - 0.047
D-galactose 6-phosphate
0.00953 - 0.5
D-glucose 6-phosphate
0.0156
deamino-NADP+
-
pH 8.0, 25°C, recombinant mutant R454C, with D-glucose 6-phosphate
0.00238 - 0.21
NADP+
0.014 - 0.015
NADPH
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
207 - 251
D-glucose 6-phosphate
207 - 251
NADP+
22.4
2-deoxy-D-glucose 6-phosphate
-
pH 8.0, 25°C, recombinant mutant R454C, with NADP+
43
2-deoxyglucose 6-phosphate
-
-
157
D-galactose 6-phosphate
-
-
20 - 571
D-glucose 6-phosphate
98
deamino-NADP+
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5200
D-glucose 6-phosphate
at pH 8.0 and 37°C
34300
NADP+
at pH 8.0 and 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.048
brimonidine
pH and temperature not specified in the publication
additional information
additional information
-
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0299
brimonidine
Homo sapiens
pH and temperature not specified in the publication
0.0000036
Tl+
Homo sapiens
-
201Tl solution, pH 8.5, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0443
crude extract, at pH 8.0 and 37°C
0.2282
purified enzyme, at pH 8.0 and 37°C
130
-
purified recombinant mutant R393H
135
-
purified recombinant mutant R393E
166
-
purified recombinant mutant R393V
176
-
purified recombinant mutant R393L
178
-
purified recombinant mutant R393G
181
-
purified recombinant mutant R393I
210
-
purified isoenzyme I
222.8
-
recombinant from Escherichia coli
27.5
-
purified wild-type enzyme
52
-
purified isoenzyme II
8.35
-
pH 8.5, 25°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.3
-
isoform A(+)
8.5
-
mutant enzymes 1 and 3
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
40
-
mutant enzymes 1 and 3
45
-
mutant enzyme 2
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
G6PD deficiency is associated with premature senescence of human fibroblasts
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
G6PD_HUMAN
515
0
59257
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10000
dimeric apoenzyme, gel filtration
100000
-
gel filtration, refolded protein
200000
-
gel filtration, native enzyme
210000
-
-
220000
-
isoenzymes I and II, gel filtration
53000
-
4 * 53000, SDS-PAGE
57000
-
4 * 57000, SDS-PAGE
59000
-
? * 59000, SDS-PAGE, native and recombinant from Escherichia coli
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
tetramer
additional information
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
A44T
-
asymptomatic patient with high in vitro glucose-6-phosphate dehydrogenase deficiency, carrying a inherited mutation at A55T
G488S
-
clinical mutant G6PDFukaya, mutation in the vicinity of the structural NADP+ site, elevated Kd values of the structural NADP+, is denatured by guanidinium hydrochloride and refolded by rapid dilution in the presence of L-Arg, NADP+ and dithiothreitol at 25°C, displays decreased thermostability and high susceptibility to chymotrypsin digestion as compared to the wild-type
G488V
-
clinical mutant G6PDCampinas, mutation in the vicinity of the structural NADP+ site, elevated Kd values of the structural NADP+, is denatured by guanidinium hydrochloride and refolded by rapid dilution in the presence of L-Arg, NADP+ and dithiothreitol at 25°C, displays decreased thermostability and high susceptibility to chymotrypsin digestion as compared to the wild-type
P409R
-
natural occurring point mutation, reconstructed by site-directed mutagenesis, the gene g6pd is highly polymorphic with over 130 mutations identified, reduced activity drastically altered kinetics, and altered tertiary structure, disturbing the binding of NADP+, compared to the wild-type enzyme, reduced thermal stbility
P489S
-
missense mutation associated with severe enzyme deficiency
R393E
-
site-directed mutagenesis, the mutation affects a residue in the dimer interface close to the structural NADP+ site, the mutant activity is slightly reduced compared to the activity of the wild-type enzyme
R393G
R393H
R393I
-
site-directed mutagenesis, the mutation affects a residue in the dimer interface close to the structural NADP+ site, the mutant activity is similar to the activity of the wild-type enzyme
R393L
-
site-directed mutagenesis, the mutation affects a residue in the dimer interface close to the structural NADP+ site, the mutant activity is similar to the activity of the wild-type enzyme
R393V
-
site-directed mutagenesis, the mutation affects a residue in the dimer interface close to the structural NADP+ site, the mutant activity is reduced compared to the activity of the wild-type enzyme
R454C
-
site-directed mutagenesis, the mutant strain overexpresses the clinical enzyme mutants, i.e. Union clone, C1360T, the mutation abolishes a salt bridge between Arg454 and Asp 286, and leads to 10% decreased kcat and activity, Km values for both G6P and NADP+ are decreased approximately 5fold, the mutant shows decreased thermostability
R454H
-
site-directed mutagenesis, the mutant strain overexpresses the clinical enzyme mutants, i.e. Andalus clone, G1361A, the mutation abolishes a salt bridge between Arg454 and Asp 286, and leads to 10% decreased kcat and activity, Km values for both G6P and NADP+ are decreased approximately 5fold, the mutant shows decreased thermostability
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
inactivation at 4°C is partially reversed at room temperature, especially with added NADP+
47
the half-life temperature is 47°C
45
-
60 min, the wild-type enzyme is completely stable, the mutant P409R shows 86% reduced thermal stability compared to the wild-type enzyme
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
isoform A(-) is less stable during purification than A(+) due to V68M mutation that makes it suceptible to oxidation of sulfhydryl group
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, storage in saline-adenine-glucose-mannitol, 6 weeks, the enzyme activity decreases significantly to 18%
-10°C, 10 mM Tris-HCl, pH 7.4, 5 mM 2-mercaptoethanol, 2 mM EDTA, 40% glycerol (v/v), weeks
-
4°C, several months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HiTrap QXL column chromatography
two varients G6PD(Plymouth) (G163D) and G6PD(Mahidol) (G163S)
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
-
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
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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
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
-
wild-type and clinical mutants expressed in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
TAp73 protein stimulates the expression of glucose-6-phophate dehydrogenase. Enzyme expression is elevated in various tumors, correlating with the upregulation of TAp73
high glucose level inhibits G6PD expression
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cohen, P.; Rosemeyer, M.A.
Glucose-6-phosphate dehydrogenase from human erythrocytes
Methods Enzymol.
41
208-214
1975
Homo sapiens
Manually annotated by BRENDA team
Schraven, E.; Gruber, C.
Organ- und speziesspezifische Eigenschaften von Glucose-6-phosphatdehydrogenase und deren Beeinflussung durch Molsidomin
Arzneimittelforschung
38
36-39
1988
Canis lupus familiaris, Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Bautista, J.M.; Mason, P.J.; Luzzatto, L.
Purification and properties of human glucose-6-phosphate dehydrogenase made in E. coli
Biochim. Biophys. Acta
1119
74-80
1992
Homo sapiens
Manually annotated by BRENDA team
Adediran, S.A.
Kinetic and thermodynamic properties of two electrophoretically similar genetic variants of human erythrocyte glucose-6-phosphate dehydrogenase
Biochimie
78
165-170
1996
Homo sapiens
Manually annotated by BRENDA team
Ozer, N.; Aksoy, Y.; Ogus, I.H.
Kinetic properties of human placental glucose-6-phosphate dehydrogenase
Int. J. Biochem. Cell Biol.
33
221-226
2001
Homo sapiens
Manually annotated by BRENDA team
Cho, S.W.; Joshi, J.G.
Characterization of glucose-6-phosphate dehydrogenase isozymes from human and pig brain
Neuroscience
38
819-828
1990
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Grabowska, D.; Jablonska-Skwiecinska, E.; Plochocka, D.; Chelstowska, A.; Lewandowska, I.; Witos, I.; Majewska, Z.; Rokicka-Milewska, R.; Burzynska, B.
A novel mutation in the glucose-6-phosphate dehydrogenase gene in a subject with chronic nonspherocytic hemolytic anemia--characterization of enzyme using yeast expression system and molecular modeling
Blood Cells Mol. Dis.
32
124-130
2004
Homo sapiens
Manually annotated by BRENDA team
Oezmen, I.; Ciftci, M.; Kufrevioglu, O.I.; Curuk, M.A.
Investigation of glucose 6-phosphate dehydrogenase (G6PD) kinetics for normal and G6PD-deficient persons and the effects of some drugs
J. Enzyme Inhib. Med. Chem.
19
45-50
2004
Homo sapiens
Manually annotated by BRENDA team
Wang, X.; Lam, V.M.; Engel, P.C.
Functional properties of two mutants of human glucose 6-phosphate dehydrogenase, R393G and R393H, corresponding to the clinical variants G6PD Wisconsin and Nashville
Biochim. Biophys. Acta
1762
767-774
2006
Homo sapiens
Manually annotated by BRENDA team
Merritt, J.; Butz, J.A.; Ogunnaike, B.A.; Edwards, J.S.
Parallel analysis of mutant human glucose 6-phosphate dehydrogenase in yeast using PCR colonies
Biotechnol. Bioeng.
92
519-531
2005
Homo sapiens
Manually annotated by BRENDA team
Wang, X.T.; Lam, V.M.; Engel, P.C.
Marked decrease in specific activity contributes to disease phenotype in two human glucose 6-phosphate dehydrogenase mutants, G6PD(Union) and G6PD(Andalus)
Hum. Mutat.
26
284
2005
Homo sapiens
Manually annotated by BRENDA team
Minucci, A.; Concolino, P.; Antenucci, M.; Santonocito, C.; Ameglio, F.; Zuppi, C.; Giardina, B.; Capoluongo, E.
Description of a novel missense mutation of glucose-6-phosphate dehydrogenase gene associated with asymptomatic high enzyme deficiency
Clin. Biochem.
40
856-858
2007
Homo sapiens
Manually annotated by BRENDA team
Minucci, A.; Concolino, P.; Vendittelli, F.; Giardina, B.; Zuppi, C.; Capoluongo, E.
Glucose-6-phosphate dehydrogenase Buenos Aires: a novel de novo missense mutation associated with severe enzyme deficiency
Clin. Biochem.
41
742-745
2008
Homo sapiens
Manually annotated by BRENDA team
Bulbul, M.; Erat, M.
Investigation of the effects of some sulfonamide derivatives on the activities of glucose-6-phosphate dehydrogenase, 6-phospho gluconate dehydrogenase and glutathione reductase from human erythrocytes
J. Enzyme Inhib. Med. Chem.
23
418-423
2008
Homo sapiens
Manually annotated by BRENDA team
Huang, Y.; Choi, M.Y.; Au, S.W.; Au, D.M.; Lam, V.M.; Engel, P.C.
Purification and detailed study of two clinically different human glucose 6-phosphate dehydrogenase variants, G6PD(Plymouth) and G6PD(Mahidol): Evidence for defective protein folding as the basis of disease
Mol. Genet. Metab.
93
44-53
2008
Homo sapiens (P11413), Homo sapiens
Manually annotated by BRENDA team
Wang, X.T.; Chan, T.F.; Lam, V.M.; Engel, P.C.
What is the role of the second, "structural" NADP+ binding site in human glucose 6-phosphate dehydrogenase?
Protein Sci.
17
1403-1411
2008
Homo sapiens (P11413), Homo sapiens
Manually annotated by BRENDA team
Ho, H.Y.; Cheng, M.L.; Chiu, D.T.
Glucose-6-phosphate dehydrogenase - from oxidative stress to cellular functions and degenerative diseases
Redox Rep.
12
109-118
2007
Homo sapiens
Manually annotated by BRENDA team
Kuznetsova, L.; Chistyakova, O.
The regulation of glucose-6-phosphate dehydrogenase and glycogen synthase activities by peptides of insulin superfamily in myometrium of pregnant women and its impairments in different types of diabetes mellitus
Biochemistry (Moscow)
3
311-316
2009
Homo sapiens
-
Manually annotated by BRENDA team
Wang, X.T.; Engel, P.C.
Clinical mutants of human glucose 6-phosphate dehydrogenase: impairment of NADP(+) binding affects both folding and stability
Biochim. Biophys. Acta
1792
804-809
2009
Homo sapiens
Manually annotated by BRENDA team
Wang, X.; Engel, P.
An optimised system for refolding of human glucose 6-phosphate dehydrogenase
BMC Biotechnol.
9
19
2009
Homo sapiens
Manually annotated by BRENDA team
Gupte, S.A.
Glucose-6-phosphate dehydrogenase: a novel therapeutic target in cardiovascular diseases
Curr. Opin. Investig. Drugs
9
993-1000
2008
Bos taurus, Saccharomyces cerevisiae, Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Minucci, A.; Giardina, B.; Zuppi, C.; Capoluongo, E.
Glucose-6-phosphate dehydrogenase laboratory assay: How, when, and why?
IUBMB Life
61
27-34
2009
Homo sapiens
Manually annotated by BRENDA team
Hue, N.T.; Charlieu, J.P.; Chau, T.T.; Day, N.; Farrar, J.J.; Hien, T.T.; Dunstan, S.J.
Glucose-6-phosphate dehydrogenase (G6PD) mutations and haemoglobinuria syndrome in the Vietnamese population
Malar. J.
8
152
2009
Homo sapiens (P11413), Homo sapiens
Manually annotated by BRENDA team
Bergandi, L.; Aina, V.; Garetto, S.; Malavasi, G.; Aldieri, E.; Laurenti, E.; Matera, L.; Morterra, C.; Ghigo, D.
Fluoride-containing bioactive glasses inhibit pentose phosphate oxidative pathway and glucose 6-phosphate dehydrogenase activity in human osteoblasts
Chem. Biol. Interact.
183
405-415
2010
Homo sapiens
Manually annotated by BRENDA team
Zhang, Z.; Liew, C.W.; Handy, D.E.; Zhang, Y.; Leopold, J.A.; Hu, J.; Guo, L.; Kulkarni, R.N.; Loscalzo, J.; Stanton, R.C.
High glucose inhibits glucose-6-phosphate dehydrogenase, leading to increased oxidative stress and beta-cell apoptosis
FASEB J.
24
1497-1505
2010
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Sahin, A.; Senturk, M.; Ciftci, M.; Varoglu, E.; Kufrevioglu, O.I.
The effects of chemical and radioactive properties of Tl-201 on human erythrocyte glucose 6-phosphate dehydrogenase activity
Nucl. Med. Biol.
37
389-394
2010
Homo sapiens
Manually annotated by BRENDA team
Savchenko, A.A.
Evaluation of NADP-dependent dehydrogenase activities in neutrophilic granulocytes by the bioluminescent method
Bull. Exp. Biol. Med.
159
692-695
2015
Homo sapiens (P11413)
Manually annotated by BRENDA team
Jiang, P.; Du, W.; Yang, X.
A critical role of glucose-6-phosphate dehydrogenase in TAp73-mediated cell proliferation
Cell Cycle
12
3720-3726
2013
Homo sapiens (P11413), Homo sapiens
Manually annotated by BRENDA team
Lin, H.R.; Wu, C.C.; Wu, Y.H.; Hsu, C.W.; Cheng, M.L.; Chiu, D.T.
Proteome-wide dysregulation by glucose-6-phosphate dehydrogenase (G6PD) reveals a novel protective role for G6PD in aflatoxin B1-mediated cytotoxicity
J. Proteome Res.
12
3434-3448
2013
Homo sapiens (P11413)
Manually annotated by BRENDA team
Boonyuen, U.; Chamchoy, K.; Swangsri, T.; Saralamba, N.; Day, N.P.; Imwong, M.
Detailed functional analysis of two clinical glucose-6-phosphate dehydrogenase (G6PD) variants, G6PDViangchan and G6PDViangchan+Mahidol: Decreased stability and catalytic efficiency contribute to the clinical phenotype
Mol. Genet. Metab.
118
84-91
2016
Homo sapiens (P11413), Homo sapiens
Manually annotated by BRENDA team
Peters, A.L.; van Bruggen, R.; de Korte, D.; Van Noorden, C.J.; Vlaar, A.P.
Glucose-6-phosphate dehydrogenase activity decreases during storage of leukoreduced red blood cells
Transfusion
56
427-432
2016
Homo sapiens (P11413)
Manually annotated by BRENDA team
Wu, Y.H.; Chiu, D.T.; Lin, H.R.; Tang, H.Y.; Cheng, M.L.; Ho, H.Y.
Glucose-6-phosphate dehydrogenase enhances antiviral response through downregulation of NADPH sensor HSCARG and upregulation of NF-kappaB signaling
Viruses
7
6689-6706
2015
Homo sapiens (P11413)
Manually annotated by BRENDA team
Caliskan, B.; Oeztuerk Kesebir, A.; Demir, Y.; Akyol Salman, I.
The effect of brimonidine and proparacaine on metabolic enzymes Glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, and glutathione reductase
Biotechnol. Appl. Biochem.
69
281-288
2022
Homo sapiens (P11413), Homo sapiens
Manually annotated by BRENDA team