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Information on EC 1.1.1.44 - phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating) and Organism(s) Homo sapiens and UniProt Accession P52209
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1.1.1.44 phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating)IUBMB Comments
The enzyme participates in the oxidative branch of the pentose phosphate pathway, whose main purpose is to produce NADPH and pentose for biosynthetic reactions. Highly specific for NADP+. cf. EC 1.1.1.343, phosphogluconate dehydrogenase (NAD+-dependent, decarboxylating).
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Word Map
- 1.1.1.44
- glucose-6-phosphate
- pentose
- acp
- gpi
-
malic
-
lipogenic
-
allozymes
-
pelteobagrus
-
monomorphic
- srebp-1
-
4.1.3.8
- fulvidraco
-
duffy
- physcion
- tropica
-
zymodemes
- medicine
- synthesis
- pharmacology
- biotechnology
- agriculture
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
6pgd, 6-pgd, 6-p-gluconate dehydrogenase, os6pgdh1, 6-phosphogluconate dehydrogenase (decarboxylating), 6-phospho-d-gluconate dehydrogenase, llpdh, 6-phosphogluconate dehydrogenase 1, 6-gpd, p6pgdh, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
6-phosphogluconate dehydrogenase
-
6-phospho-D-gluconate dehydrogenase
-
-
-
-
6-phosphogluconate dehydrogenase (decarboxylating)
-
-
-
-
6-phosphogluconic carboxylase
-
-
-
-
6-phosphogluconic dehydrogenase
-
-
-
-
GNTZII
-
-
-
-
phosphogluconic acid dehydrogenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-
SYSTEMATIC NAME
IUBMB Comments
6-phospho-D-gluconate:NADP+ 2-oxidoreductase (decarboxylating)
The enzyme participates in the oxidative branch of the pentose phosphate pathway, whose main purpose is to produce NADPH and pentose for biosynthetic reactions. Highly specific for NADP+. cf. EC 1.1.1.343, phosphogluconate dehydrogenase (NAD+-dependent, decarboxylating).
CAS REGISTRY NUMBER
COMMENTARY
9073-95-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
-
-
-
?
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
-
-
-
-
?
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
the enzyme catalyzes a step of the pentose phosphate pathway
-
-
?
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
-
-
-
-
?
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
-
-
286834, 286836, 286837, 286838, 286839, 286841, 286846, 286849, 286850, 286881, 286890, 286892, 286895, 286897, 286903
-
-
r
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
-
enzyme specific for the oxidative pentose phosphate pathway
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
-
-
-
?
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
-
-
-
-
?
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
the enzyme catalyzes a step of the pentose phosphate pathway
-
-
?
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
-
-
-
-
?
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
-
-
-
-
r
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
-
enzyme specific for the oxidative pentose phosphate pathway
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(5Z)-5-[[4-(3-fluorophenoxy)phenyl]methylidene]-2-imino-3-(2-methoxyphenyl)-1,3-thiazolidin-4-one
-
1-hydroxy-8-methoxy-anthraquinone
inhibition of the enzyme (6PGD) via chemical inhibitor 1-hydroxy-8-methoxy-anthraquinone results in an induction of senescence
2,6-dimethoxy-4-[5-phenyl-4-[4-(phenylsulfanyl)phenyl]-1H-imidazol-2-yl]phenol
-
5,6-bis(2H-1,3-benzodioxol-5-yl)-2-(3-methylphenyl)-4,7-diphenyl-3a,4,7,7a-tetrahydro-1H-4,7-methanoisoindole-1,3,8(2H)-trione
-
7-[[3-(benzyloxy)phenyl][(4-methylpyridin-2-yl)amino]methyl]quinolin-8-ol
-
(4S)-trans-4-ethylammonio-6-methyl-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
-
i.e. dorzolamide, competitive
5-(3,7,12-trioxo-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
-
weak inhibition
5-(3alpha,7alpha,12alpha-triacetoxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
-
competitive
5-(3alpha,7alpha,12alpha-trihydroxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
-
competitive
additional information
-
no inhibition by cefozin, decefin, streptomycin, combisid, and meronem
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-(3alpha-acetoxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
-
activates
5-(3alpha-hydroxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
-
activates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.14
(4S)-trans-4-ethylammonio-6-methyl-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
-
-
0.0042
5-(3alpha,7alpha,12alpha-triacetoxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
-
-
0.0878
5-(3alpha,7alpha,12alpha-trihydroxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0013
(5Z)-5-[[4-(3-fluorophenoxy)phenyl]methylidene]-2-imino-3-(2-methoxyphenyl)-1,3-thiazolidin-4-one
Homo sapiens
25°C, pH 8.0
0.0035
11-(4-methoxyphenyl)-11H-benzo[b]indeno[1,2-e][1,4]thiazepin-12-ol
Homo sapiens
25°C, pH 8.0
0.0018
2,6-dimethoxy-4-[5-phenyl-4-[4-(phenylsulfanyl)phenyl]-1H-imidazol-2-yl]phenol
Homo sapiens
25°C, pH 8.0
0.0049
2-methyl-3-[2-(3-nitrophenyl)-2-oxoethyl]naphthalene-1,4-dione
Homo sapiens
25°C, pH 8.0
0.0021
4,4'-[1,4-phenylenebis(oxy-1H-benzimidazole-6,2-diyl)]dianiline
Homo sapiens
25°C, pH 8.0
0.0024
5,5'-methylenebis[2-(4-methoxyphenyl)-1H-benzimidazole]
Homo sapiens
25°C, pH 8.0
0.0027
5,6-bis(2H-1,3-benzodioxol-5-yl)-2-(3-methylphenyl)-4,7-diphenyl-3a,4,7,7a-tetrahydro-1H-4,7-methanoisoindole-1,3,8(2H)-trione
Homo sapiens
25°C, pH 8.0
0.0022
7-[[3-(benzyloxy)phenyl][(4-methylpyridin-2-yl)amino]methyl]quinolin-8-ol
Homo sapiens
25°C, pH 8.0
0.0043
N-[(4-chlorophenyl)(2-hydroxy-1-naphthyl)methyl]-2-phenylacetamide
Homo sapiens
25°C, pH 8.0
1.41
(4S)-trans-4-ethylammonio-6-methyl-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
Homo sapiens
-
-
0.00253
5-(3alpha,7alpha,12alpha-triacetoxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
Homo sapiens
-
-
0.0601
5-(3alpha,7alpha,12alpha-trihydroxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
Homo sapiens
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22.1
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
infected with the lentivirus expressing Flag tagged 6PGD (Flag-6PGD)
stably expressing epidermal growth factor receptor (EGFR), infected with the lentivirus expressing Flag tagged 6PGD (Flag-6PGD)
-
-
286834, 286836, 286837, 286838, 286839, 286841, 286849, 286850, 286881, 286890, 286892, 286895, 286897, 286903, 656386
-
-
-
antibodies to 6-phosphogluconate dehydrogenase, decarboxylating are present in serum samples of ASA-positive (antisperm antibodies) infertile men
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
malfunction
enzyme suppression causes a characteristic ER-dilation phenotype that is associated with increased extracellular matrix protein inside cells as well as decreased secretion
metabolism
physiological function
malfunction
-
enzyme suppression decreases lipogenesis and RNA biosynthesis and elevates reactive oxygen species levels in cancer cells, attenuating cell proliferation and tumor growth
metabolism
-
enzyme-mediated production of D-ribulose 5-phosphate inhibits adenine monophosphate-activated protein kinase activation by disrupting the active tumor suppressor liver kinase B1 complex, thereby activating acetyl-CoA carboxylase 1 and lipogenesis
physiological function
-
the enzyme is important for oxidative triphosphate and lipogenesis, as well as proliferative and tumor growth potential of cancer cells
drug target
abrogating 6-phosphogluconate dehydrogenase Y481 phosphorylation (pY481) dramatically attenuates epidermal growth factor receptor(EGF) promotes glioma cell proliferation, tumor growth and resistance to ionizing radiation. 6PGD pY481 is associated with Fyn expression, the malignancy and prognosis of human glioblastoma. Critical role of Fyn-dependent 6-phosphogluconate dehydrogenase (6PGD) phosphorylation in EGF-promoted tumor growth and radiation resistance
drug target
targeting 6-phosphogluconate dehydrogenase (6PGD) and NADPH production is sufficient to block growth of acute myeloid leukemia cell lines resistant to the chemotherapeutics daunorubicin and cytarabine. Stromal cell-mediated resistance to targeted inhibition of oncogenic FLT3 kinase activity by quizartinib is circumvented by 6PGD knockdown
drug target
the enzyme (6PGD) is a putative therapeutic drug target in breast cancer treatment. Targeting 6PGD not only reduces cell proliferation through cell cycle arrest and apoptosis induction but also activates p53 and decreases the stem cell-like characteristics of breast cancer cells. Inhibition of 6PGD alters the stem cell characteristics and mammosphere formation capabilities of MCF-7 cells, opening new avenues to prevent cancer recurrance after surgery or chemotherapy. Inhibition of 6PGD via chemical inhibitor 1-hydroxy-8-methoxy-anthraquinone results in an induction of senescence, which, together with the cell cycle arrest and apoptosis induction, might be orchestrated by p53 activation
drug target
the enzyme is critically involved in the development of anaplastic thyroid carcinoma resistance to oxorubicin. Inhibiting 6-phosphogluconate dehydrogenase reverses doxorubicin resistance in anaplastic thyroid cancer via inhibiting NADPH-dependent metabolic reprogramming
drug target
the enzyme might serve as promising therapeutic target for the treatment of cancers in which the enzyme (6PGD) is aberrantly overexpressed
metabolism
6-phosphogluconate dehydrogenase links cytosolic carbohydrate metabolism to protein secretion via modulation of glutathione levels
metabolism
inhibition of the enzyme (6PGD) in MCF-7 cells reduces cell proliferation and shows a significant decrease in glucose consumption and an increase in glutamine consumption, resulting in an important alteration in the metabolism of these cells
metabolism
no difference in reactive oxygen species production levels is observed after inhibition of the enzyme (6PGD), indicating that 6PGD, in contrast to glucose 6-phosphate dehydrogenase, is not involved in redox balance
metabolism
upon epidermal growth factor receptor (EGFR) activation, the enzyme (6PGD) is phosphorylated at tyrosine 481 by Src family kinase Fyn. This phosphorylation enhances 6PGD activity by increasing its binding affinity to NADP+ and therefore activates the pentose phosphate pathway for NADPH and ribose-5-phosphate, which consequently detoxifies intracellular reactive oxygen species (ROS) and accelerates DNA synthesis
physiological function
acute myeloid leukemia cells require 6-phosphogluconate dehydrogenase for cell growth and NADPH-dependent metabolic reprogramming
physiological function
the enzyme involved in carbohydrate metabolism, is required for endoplasmic reticulum structural integrity and protein secretion
physiological function
the enzyme is commonly upregulated and plays important roles in many human cancers
physiological function
the enzyme is involved in the oxidative branch of the pentose phosphate pathway
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). 6PGD_HUMAN
483
0
53140
Swiss-Prot
Secretory Pathway (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
104000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
dimer
homodimer
monomers act independently to each other. Each monomer consists of large alpha-helical domain while small beta-alpha-beta domain, forming a six stranded beta-sheet
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
Y481 phosphorylation is essential for epidermal growth factor receptor (EGFR) activation-enhanced 6PGD activity
additional information
hyperactivation is mediated through post-transcriptional and post-translational modifications by YTH domain family 2 (YTHDF2), Nrf2 (nuclear factor erythroid 2-related factor 2), EGFR (epidermal growth factor receptor) and via direct structural interactions with ME1 (malic enzyme 1)
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 50% glycerol, under long-term storage conditions, the enzyme is stable for at least one month
4°C, stable for 5 h, loses 20% of its activity after 24%, no activity after 3 days
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
725.4fold from erythrocytes by ammonium sulfate precipitation, 2',5'-ADP-resin affinity chromatography, and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
6PGDH cDNA encodes a protein with 94% sequence identity with the sheep liver enzyme
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
overexpressed in number of cancer types. Upregulated expression of the enzyme (6PGD) provides metabolic as well as defensive advantage to cancer cells, thus, promoting their proliferative and metastatic potential. Enhanced 6PGD expression also performs key role in development of chemoresistance as well as radiation resistance in cancer
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
with a deficiency of 6-phosphogluconate dehydrogenase some reticulocytosis occurs
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pearse, B.M.F.; Harris, J.I.
6-Phosphogluconate dehydrogenase from Bacillus stearothermophilus
FEBS Lett.
38
49-52
1973
Geobacillus stearothermophilus, Cyberlindnera jadinii, Homo sapiens, Geobacillus stearothermophilus NCA 1503
Veronese, F.M.; Boccu, E.; Fontana, A.; Benassi, C.A.; Scoffone, E.
Isolation and some properties of 6-phosphogluconate dehydrogenase from Bacillus stearothermophilus
Biochim. Biophys. Acta
334
31-44
1974
Geobacillus stearothermophilus, Cyberlindnera jadinii, Homo sapiens, Neurospora crassa, Rattus norvegicus, Geobacillus stearothermophilus NCA 1503
-
Pearse, B.M.F.; Rosemeyer, M.A.
Human 6-phosphogluconate dehydrogenase. Purification of the erythrocyte enzyme and the influence of ions and NADPH on its activity
Eur. J. Biochem.
42
213-223
1974
Ovis aries, Homo sapiens
Pearse, B.M.F.; Rosemeyer, M.A.
The molecular weight and subunit structure of human erythrocyte 6-phosphogluconate dehydrogenase
Eur. J. Biochem.
42
225-235
1974
Cyberlindnera jadinii, Drosophila sp. (in: flies), Ovis aries, Homo sapiens, Rattus norvegicus
King, J.
6-Phosphogluconat-dehydrogenase
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
1
668-672
1974
Saccharomyces cerevisiae, Homo sapiens
-
Pearse, B.M.F.; Rosemeyer, M.A.
6-Phosphogluconate from human erythrocytes
Methods Enzymol.
41
220-226
1975
Homo sapiens
Bridges, R.B.; Palumbo, M.P.; Wittenberger, C.L.
Purification and properties of an NADP-specific 6-phosphogluconate dehydrogenase from Streptococcus faecalis
J. Biol. Chem.
250
6093-6100
1975
Cyberlindnera jadinii, Enterococcus faecalis, Homo sapiens, Neurospora crassa, Rattus norvegicus
Betts, S.A.; Mayer, R.J.
Purification and properties of 6-phosphogluconate dehydrogenase from rabbit mammary gland
Biochem. J.
151
263-270
1975
Cyberlindnera jadinii, Oryctolagus cuniculus, Escherichia coli, Ovis aries, Homo sapiens, Rattus norvegicus
Toews, M.L.; Kanji, M.I.; Carper, R.W.
6-Phosphogluconate dehydrogenase. Purification and kinetics
J. Biol. Chem.
251
7127-7131
1976
Cyberlindnera jadinii, Ovis aries, Homo sapiens, Rattus norvegicus, Sus scrofa
Dallocchio, F.; Matteuzzi, M.; Bellini, T.
Half-site reactivity in 6-phosphogluconate dehydrogenase from human erythrocytes
Biochem. J.
227
305-310
1985
Cyberlindnera jadinii, Ovis aries, Homo sapiens
Hanau, S.; Dallocchio, F.; Rippa, M.
NADPH activates a decarboxylation reaction catalyzed by lamb liver 6-phosphogluconate dehydrogenase
Biochim. Biophys. Acta
1122
273-277
1992
Cyberlindnera jadinii, Ovis aries, Homo sapiens
Berdis, A.J.; Cook, P.F.
Overall kinetic mechanism of 6-phosphogluconate dehydrogenase from Candida utilis
Biochemistry
32
2036-2040
1993
Leuconostoc mesenteroides, Cyberlindnera jadinii, Haemophilus influenzae, Ovis aries, Homo sapiens, Rattus norvegicus
Corpas, F.J.; Garcia-Salguero, L.; Barroso, J.B.; Aranda, F.; Lupianez, J.A.
Kinetic properties of hexose-monophosphate dehydrogenases. II. Isolation and partial purification of 6-phosphogluconate dehydrogenase from rat liver and kidney cortex
Mol. Cell. Biochem.
144
97-104
1995
Cyberlindnera jadinii, Gallus sp., Homo sapiens, Rattus norvegicus, Rattus norvegicus Wistar
Ganea, E.; Harding, J.J.
Inhibition of 6-phosphogluconate dehydrogenase by carbamylation and protection by alpha-crystallin, a chaperone-like protein
Biochem. Biophys. Res. Commun.
222
626-631
1996
Homo sapiens
Rippa, M.; Giovannini, P.P.; Barrett, M.P.; Dallocchio, F.; Hanau, S.
6-Phosphogluconate dehydrogenase: The mechanism of action investigated by a comparison of the enzyme from different species
Biochim. Biophys. Acta
1429
83-92
1998
Cyberlindnera jadinii, Ovis aries, Homo sapiens, Trypanosoma brucei
Akyuez, M.; Erat, M.; Ciftci, M.; Guemuestekin, K.; Bakan, N.
Effects of some antibiotics on human erythrocyte 6-phosphogluconate dehydrogenase: an in vitro and in vivo study
J. Enzyme Inhib. Med. Chem.
19
361-365
2004
Homo sapiens, Rattus norvegicus
Adem, S.; Ciftci, M.
Effects of some drugs on human erythrocyte 6-phosphogluconate dehydrogenase: an in vitro study
J. Enzyme Inhib. Med. Chem.
22
751-754
2007
Homo sapiens
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
Domagala, A.; Pulido, S.; Kurpisz, M.; Herr, J.C.
Application of proteomic methods for identificaiton of sperm immunogenic antigens
Mol. Hum. Reprod.
13
437-444
2007
Homo sapiens
Lin, R.; Elf, S.; Shan, C.; Kang, H.B.; Ji, Q.; Zhou, L.; Hitosugi, T.; Zhang, L.; Zhang, S.; Seo, J.H.; Xie, J.; Tucker, M.; Gu, T.L.; Sudderth, J.; Jiang, L.; Mitsche, M.; DeBerardinis, R.J.; Wu, S.; Li, Y.; Mao, H.; Chen, P.R.; Wang, D.; Chen, G.Z.; Hurwitz, S.J.; Lonial, S.; Arellano, M.L.; Khoury, H.J.; Khuri, F.R.
6-Phosphogluconate dehydrogenase links oxidative PPP, lipogenesis and tumour growth by inhibiting LKB1-AMPK signalling
Nat. Cell Biol.
17
1484-1496
2015
Homo sapiens
Chan, B.; Sukhatme, V.P.
One-step purification of soluble recombinant human 6-phosphogluconate dehydrogenase from Escherichia coli
Protein Expr. Purif.
92
62-66
2013
Homo sapiens (P52209), Homo sapiens
Rodrigues, J.; Branco, V.; Lu, J.; Holmgren, A.; Carvalho, C.
Toxicological effects of thiomersal and ethylmercury: Inhibition of the thioredoxin system and NADP+-dependent dehydrogenases of the pentose phosphate pathway
Toxicol. Appl. Pharmacol.
286
216-223
2015
Homo sapiens
Ma, L.; Cheng, Q.
Inhibiting 6-phosphogluconate dehydrogenase reverses doxorubicin resistance in anaplastic thyroid cancer via inhibiting NADPH-dependent metabolic reprogramming
Biochem. Biophys. Res. Commun.
498
912-917
2018
Homo sapiens (P52209)
Sarfraz, I.; Rasul, A.; Hussain, G.; Shah, M.A.; Zahoor, A.F.; Asrar, M.; Selamoglu, Z.; Ji, X.Y.; Adem, S.; Sarker, S.D.
6-Phosphogluconate dehydrogenase fuels multiple aspects of cancer cells From cancer initiation to metastasis and chemoresistance
Biofactors
46
550-562
2020
Homo sapiens (P52209)
Polat, I.H.; Tarrado-Castellarnau, M.; Bharat, R.; Perarnau, J.; Benito, A.; Cortes, R.; Sabatier, P.; Cascante, M.
Oxidative pentose phosphate pathway enzyme 6-phosphogluconate dehydrogenase plays a key role in breast cancer metabolism
Biology
10
85
2021
Homo sapiens (P52209)
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 (P52209), Homo sapiens
Li, H.; Ericsson, M.; Rabasha, B.; Budnik, B.; Chan, S.H.; Freinkman, E.; Lewis, C.A.; Doench, J.G.; Wagner, B.K.; Garraway, L.A.; Schreiber, S.L.
6-Phosphogluconate dehydrogenase links cytosolic carbohydrate metabolism to protein secretion via modulation of glutathione levels
Cell Chem. Biol.
26
1306-1314
2019
Homo sapiens (P52209)
Haeussler, K.; Fritz-Wolf, K.; Reichmann, M.; Rahlfs, S.; Becker, K.
Characterization of Plasmodium falciparum 6-phosphogluconate dehydrogenase as an antimalarial drug target
J. Mol. Biol.
430
4049-4067
2018
Homo sapiens (P52209), Plasmodium falciparum (Q8IKT2), Plasmodium falciparum
Liu, R.; Li, W.; Tao, B.; Wang, X.; Yang, Z.; Zhang, Y.; Wang, C.; Liu, R.; Gao, H.; Liang, J.; Yang, W.
Tyrosine phosphorylation activates 6-phosphogluconate dehydrogenase and promotes tumor growth and radiation resistance
Nat. Commun.
10
991
2019
Homo sapiens (P52209), Homo sapiens
Bhanot, H.; Weisberg, E.L.; Reddy, M.M.; Nonami, A.; Neuberg, D.; Stone, R.M.; Podar, K.; Salgia, R.; Griffin, J.D.; Sattler, M.
Acute myeloid leukemia cells require 6-phosphogluconate dehydrogenase for cell growth and NADPH-dependent metabolic reprogramming
Oncotarget
8
67639-67650
2017
Homo sapiens (P52209)
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