Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
three-dimensional structure homology modeling of wild-type 6PGDH from Moorella thermoacetica and mutants based on the structure of human enzyme 6PGDH, PDB ID 2JKV
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
blockade of 6-phosphogluconate dehydrogenase reprograms CD8+ T cell metabolism to support superior effector function with higher tumoricidal activity. This metabolic checkpoint represents a key therapeutic target for cancer immunotherapies
drug target
Plasmodium falciparum 6-phosphogluconate dehydrogenase is an antimalarial drug target
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 an attractive antimalarial drug target due to its central role in metabolism
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
evolution
phylogenetic analysis of cyanobacterial 6-phosphogluconate dehydrogenases (6PGDH) reveals that an amino acid residue at position 42 in Sy6PGDH is highly conserved for each order of cyanobacteria, but Synechocystis 6PGDH (Sy6PGDH) is phylogenetically unique. In Sy6PGDH, a single amino acid substitution at position 42 from serine to threonine enhances the affinity for NADP+ and alters the mode of inhibition by NADPH
evolution
phylogenetic analysis of cyanobacterial 6PGDHs reveales that the amino acid residue at position 42 in Sy6PGDH is highly conserved
malfunction
-
enzyme suppression decreases lipogenesis and RNA biosynthesis and elevates reactive oxygen species levels in cancer cells, attenuating cell proliferation and tumor growth
malfunction
-
mutations of the chloroplast-localized enzyme cause a rough endosperm seed phenotype with reduced embryo oil and endosperm starch and altered carbon flux into starch
malfunction
blockade of 6-phosphogluconate dehydrogenase generates CD8+ effector T cells with enhanced anti-tumor function
malfunction
disruption of glucose-6-phosphate dehydrogenase (ZWF1), 6-phosphogluconate dehydrogenase GND1 and 6-phosphogluconate dehydrogenase GND2 genes can decrease the ability of yeast cells to reproduction in the exponential phase of culture
malfunction
enzyme suppression causes a characteristic ER-dilation phenotype that is associated with increased extracellular matrix protein inside cells as well as decreased secretion
malfunction
-
disruption of glucose-6-phosphate dehydrogenase (ZWF1), 6-phosphogluconate dehydrogenase GND1 and 6-phosphogluconate dehydrogenase GND2 genes can decrease the ability of yeast cells to reproduction in the exponential phase of culture
-
metabolism
pentose phosphate pathway
metabolism
-
phosphogluconate pathway, bacterial 6-phosphogluconate dehydrogenase is a constitutive enzyme, bacterial enzyme is active in young, non-inoculated mesquite seedlings growing under hydroponic conditions, external gluconate has no effect on the activity of 6-phosphogluconate dehydrogenase
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
metabolism
6-phosphogluconate dehydrogenase (Gcd1) and gluconate kinase (Idn1) act together to shunt glucose into the pentose phosphate pathway, creating an alternative route for directing glucose into the pentose phosphate pathway that bypasses hexokinase and the rate-limiting enzyme glucose-6-phosphate dehydrogenase
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
key enzyme catalyzing the third step in the reaction involving the oxidative phase of the pentose phosphate pathway
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
the enzyme catalyzes a step of the pentose phosphate pathway
metabolism
the enzyme catalyzes a step of the pentose phosphate pathway
metabolism
the enzyme is involved in the oxidative pentose phosphate pathway
metabolism
the enzyme plays a key role in breast cancer metabolism
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
metabolism
-
phosphogluconate pathway, bacterial 6-phosphogluconate dehydrogenase is a constitutive enzyme, bacterial enzyme is active in young, non-inoculated mesquite seedlings growing under hydroponic conditions, external gluconate has no effect on the activity of 6-phosphogluconate dehydrogenase
-
metabolism
-
6-phosphogluconate dehydrogenase (Gcd1) and gluconate kinase (Idn1) act together to shunt glucose into the pentose phosphate pathway, creating an alternative route for directing glucose into the pentose phosphate pathway that bypasses hexokinase and the rate-limiting enzyme glucose-6-phosphate dehydrogenase
-
physiological function
-
the enzyme is important for oxidative triphosphate and lipogenesis, as well as proliferative and tumor growth potential of cancer cells
physiological function
-
the enzyme is involved in tellurite detoxification and resistance in Escherichia coli
physiological function
the peroxisomal isoform is mainly involved in xenobiotic response, growth, and developmental processes
physiological function
acute myeloid leukemia cells require 6-phosphogluconate dehydrogenase for cell growth and NADPH-dependent metabolic reprogramming
physiological function
in the oxidative pentose phosphate pathway, 6-phosphogluconate dehydrogenase (6PGDH) is one of the enzymes that catalyzes reactions generating NADPH
physiological function
D4ZTT4
in the oxidative pentose phosphate pathway, 6-phosphogluconate dehydrogenase (6PGDH) is one of the enzymes that catalyzes reactions generating NADPH
physiological function
-
isoenzyme PGD3 is critical for endosperm starch accumulation. The cytosolic isozymes, PGD1 and PGD2, are not required for kernel development
physiological function
key enzyme of the oxidative pentose phosphate pathway
physiological function
the enzyme (Os6PGDH1) plays a pivotal role in rice growth and also in the resistance of rice to brown planthopper (BPH) Nilaparvata lugens by modulating jasmonic acid, ethylene, and H2O2 pathways
physiological function
the enzyme involved in carbohydrate metabolism, is required for endoplasmic reticulum structural integrity and protein secretion
physiological function
the enzyme is a modulator of CD8+ T cell activation and differentiation
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
physiological function
the enzyme is responsible for NADPH formation in the pentose phosphate pathway
physiological function
the enzyme plays an important function in various biochemical processes as it generates reducing power ofthe cell
physiological function
the NADPH produced by 6PGD is crucial for antioxidant defense and redox regulation and ribose 5-phosphate is essential for DNA and RNA synthesis in the rapidly growing parasite
physiological function
-
the enzyme is responsible for NADPH formation in the pentose phosphate pathway
-
physiological function
-
key enzyme of the oxidative pentose phosphate pathway
-
physiological function
-
the enzyme is involved in tellurite detoxification and resistance in Escherichia coli
-
physiological function
-
in the oxidative pentose phosphate pathway, 6-phosphogluconate dehydrogenase (6PGDH) is one of the enzymes that catalyzes reactions generating NADPH
-