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Glucose-6-Phosphate

Glucose-6-Phosphate is a key metabolite that plays a crucial role in various biological processes.
It is an intermediate in the glycolytic pathway, serving as a substrate for the enzyme glucose-6-phosphate dehydrogenase in the pentose phosphate pathway.
Glucose-6-Phosphate also participates in glycogen synthesis and gluconeogenesis, making it a central player in carbohydrate metabolism.
Researchers studying Glucose-6-Phosphate may investigate its regulation, enzymatic activities, and implications in metabolic disorders such as glucose-6-phosphate dehydrogenase deficiency.
This MeSh term provides a concise overview of the importance and functions of Glucose-6-Phosphate in the human body and its relevance to biomedical research.

Most cited protocols related to «Glucose-6-Phosphate»

Cells were washed twice with phosphate buffered saline (Mediatech, Manassas, VA) (1 mM pH 7.4) before being scraped into 750 µL of ice-cold methanol/water (4/1 v/v). For cells treated with rapamycin, samples were spiked with internal standards (500 ng [13C4]-succinate, 500 ng [13C6]-citrate, 500 ng [13C3]-pyruvate, 2 µg [13C3]-lactate, 500 ng [13C4,15N]-aspartate, 2 µg [13C5,15N]-glutamate and 500 ng [13C6]-glucose 6-phosphate). Samples were pulse-sonicated for 30 s with a probe tip sonicator and centrifuged at 16,000 × g for 10 min. The supernatant was transferred to two new tubes: 50 µL were transferred to one tube and diluted 5 times with 50 mM ammonium carbonate for direct analysis of the underivatized redox cycling metabolites (Figure 2) and 700 µL were transferred to one tube containing 300 µL of phenylhydrazine in water (3 mg/mL) for analysis of underivatized and derivatized metabolites (Figure 2). Derivatization was conducted by incubation at room temperature for 2 h before evaporation to dryness under nitrogen. 100 µL of water was used to re-suspend the samples. Injection volume was 5 µL in both methods. The phenylhydrazine-derivatized samples were run with gradient 1 and the underivatized samples were run with gradient 2.
Publication 2016
ammonium carbonate Aspartate Cells Citrates Cold Temperature Glucose-6-Phosphate Glutamates Ice Lactates Methanol Nitrogen Oxidation-Reduction phenylhydrazine Phosphates Pulse Rate Pyruvate Saline Solution Sirolimus Succinate

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Publication 2019
ARID1A protein, human Carbon fructose-6-phosphate Gas Chromatography-Mass Spectrometry Glucose Glucose-6-Phosphate Ions Isotopes norvaline Proteins Pyruvate Radionuclide Imaging Vertebral Column
The intracellular levels of NADPH and total NADP (NADPH+NADP+) were measured with previously described enzymatic cycling methods, with modifications32 (link),33 (link). In brief, 1.8 × 106 cells were plated in 10-cm dishes; on the next day, the cells were lysed in 400 µl of extraction buffer (20 mM nicotinamide, 20 mM NaHCO3, 100 mM Na2CO3) and centrifuged. For NADPH extraction, 150 µl of the supernatant was incubated at 60 °C for 30 min. Next, 160 µl of NADP-cycling buffer (100 mM Tris-HCl pH 8.0, 0.5 mM thiazolyl blue, 2 mM phenazine ethosulfate, 5 mM EDTA) containing 1.3U of G6PD was added to a 96-well plate containing 20 µl of the cell extract. After a 1-min incubation in the dark at 30 °C, 20 µl of 10 mM glucose 6-phosphate (G6P) was added to the mixture, and the change in absorbance at 570 nm was measured every 30 s for 4 min at 30 °C with a microplate reader. The concentration of NADP+ was calculated by subtracting[NADPH] from [total NADP]. The intracellular levels of GSH and total glutathione (GSSG + GSH) were measured with the use of enzymatic cycling methods, as described previously34 . The intracellular level of ATP was measured with an ATPlite assay kit (Perkin Elmer).
Publication 2012
5-ethylphenazine Bicarbonate, Sodium Biological Assay Buffers Cell Extracts Cells Edetic Acid Enzymes Glucose-6-Phosphate Glucosephosphate Dehydrogenase Glutathione Disulfide Hyperostosis, Diffuse Idiopathic Skeletal NADP Niacinamide Protoplasm thiazolyl blue Tromethamine
The activities of the photosynthetic enzymes Rubisco and PEPC were measured as previously described by Cousins et al. (2007) (link), with some changes. Frozen leaf tissue was processed in ice-cold glass homogenizers with 500 μl of extraction buffer (50 mM HEPES-KOH pH 7.8, 1 mM EDTA, 0.1% Triton-X, 10 mM dithiothreitol, and 1% polyvinylpolypyrrolidone) and 10 μl of protease inhibitor cocktail (Sigma). The homogenate was briefly centrifuged and the supernatant used for assays. For PEPC, 10 μl of leaf extract was combined with 980 μl of assay buffer (50 mM EPPS-NaOH pH 8, 10 mM MgCl2, 0.5 mM EDTA, 0.2 mM NADH, 5 mM glucose-6-phosphate 1 mM NaHCO3, and 1 U ml−1 malate dehydrogenase) and the reaction initiated by the addition of 10 μl of 400 mM PEP. For Rubisco, 10 μl of leaf extract was combined with 970 μl of assay buffer (50 mM EPPS-NaOH pH 8, 10 mM MgCl2, 0.5 mM EDTA, 1 mM ATP, 5 mM phosphocreatine, 20 mM NaHCO3, 0.2 mM NADH, 50 U ml−1 creatine phosphokinase, 0.2 mg carbonic anhydrase, 50 U ml−1 3-phosphoglycerate kinase, 40 U ml−1 glyceraldehyde-3-phosphate dehydrogenase, 113 U m;−1 Triose-phosphate isomerase, 39 U ml−1 glycerol 3 phosphate dehydrogenase) and the reaction initiated by the addition of 20 μl of 21.9 mM ribulose-1, 5-bisphosphate (RuBP). The activity of both enzymes was calculated by monitoring the decrease of NADH absorbance at 340 nm with a diode array spectrophotometer (Hewlett Packard) after initiation of the reaction.
Chlorophyll was extracted from frozen leaf discs in a glass homogenizer with 80% acetone. The chlorophyll a and b contents of extracts were measured in a quartz cuvette at 663.3 nm and 646.6 nm, and calculated according to Porra et al. (1989) .
Publication 2010
Acetone Bicarbonate, Sodium Biological Assay Buffers Chlorophyll Chlorophyll A Cold Temperature Creatine Kinase Dehydratase, Carbonate Dithiothreitol Edetic Acid enzyme activity Freezing Glucose-6-Phosphate Glyceraldehyde-3-Phosphate Dehydrogenases Glycerol-3-Phosphate Dehydrogenase HEPES Magnesium Chloride Malate Dehydrogenase NADH Phosphocreatine Phosphotransferases Photosynthesis Plant Leaves polyvinylpolypyrrolidone Protease Inhibitors Quartz ribulose Ribulose-Bisphosphate Carboxylase Tissues Triose-Phosphate Isomerase
All strains were derived from Escherichia coli K12 strain NCM3722 (Soupene et al, 2003; Lyons et al, 2011) as listed in Supplementary Table 1 and detailed in Supplementary Methods. MOPS-buffered minimal media (pH 7.4) were used for cell growth as described by Neidhardt et al (1974). For carbon sources, glycerol (0.4% w/v), glucose (0.4% w/v), or 10 mM each of glucose-6 phosphate and gluconate were used. For nitrogen sources, different concentrations of NH4Cl were used as specified. All the media were filtered through 0.45 μm filters.
Publication 2012
Carbon Cells Escherichia coli K12 gluconate Glucose Glucose-6-Phosphate Glycerin morpholinopropane sulfonic acid Nitrogen

Most recents protocols related to «Glucose-6-Phosphate»

Incubations were performed with 0.1 mg/mL human liver microsomes (purchased from BD Gentest as a pooled batch from 150 donors) in a final incubation volume of 0.25 mL. The incubation medium contained 0.05 M phosphate buffer (pH 7.4) containing an NADPH regenerating system (including 1.3 mM NADP, 3.3 mM glucose 6-phosphate,3.3 mM MgCl2, and 1.0 U/mL glucose 6-phosphate dehydrogenase). Probe CYP3A4 substrates (midazolam at 3 μM and testosterone at 50 μM), were incubated for 10 and 30 min, respectively, with increasing concentrations of GM, MGM or CGM (concentration range: 1 - 30 μM). The reaction was stopped by adding acetonitrile to precipitate the proteins. The incubation mixtures were then centrifuged for 5 min at 10,000 × g, and an aliquot of the supernatant was analyzed using high-performance liquid chromatography coupled to mass spectrometry for the assessment of 1’-hydroxymidazolam and 6β-hydroxytestosterone metabolite formation.
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Publication 2023
acetonitrile Buffers Cytochrome P-450 CYP3A4 Donors Glucose-6-Phosphate Glucosephosphate Dehydrogenase High-Performance Liquid Chromatographies Homo sapiens Magnesium Chloride Mass Spectrometry Microsomes, Liver Midazolam NADP Phosphates Proteins Psychological Inhibition Testosterone
The very high lipophilicity of DEHTP resulted in the formation of an insoluble film on the surface of the reaction medium which precluded the measurement of in vitro clearance which is consistent with previous studies (McNally et al., 2019 (link); McNally et al., 2021 (link)). Therefore, only the measurement of in vitro clearance of MEHTP was possible (Figure 1). In vitro incubations, the determination of in vitro half-life, in vitro intrinsic clearance and the calculation of in vivo clearance were identical to previous studies and are described therein (McNally et al., 2019 (link); McNally et al., 2021 (link)).
The NADPH regenerating system consisted of the following final concentrations: 1.3 mM NADP+; 3.3 mM glucose-6-phosphate; 5 mM magnesium chloride; 0.4 U/ml glucose-6-phosphate dehydrogenase; 50 mM phosphate buffer (pH 7.4). Final microsomal protein concentration was 0.5 mg/ml. Incubations were performed in polypropylene tubes and pre-warmed reaction mixtures were started by addition of substrate dissolved in acetonitrile. The final acetonitrile concentration was less than 1% and, typically, a substrate concentration of 10 µM was used (initial investigations were performed to check solubility in the reaction mixture). Incubations were conducted in a water bath at 37°C. At the time points chosen for measurement, tubes were mixed by inversion and an aliquot removed and quenched by adding to an equal volume of ice-cold methanol followed by centrifugation to precipitate the protein as a pellet. The supernatant was removed for analysis. Three replicates were sampled at each time point. Control incubations consisted of a reaction mix excluding glucose-6-phosphate dehydrogenase (for evaluation of non-specific binding) and reaction mix excluding microsomes (for evaluation of substrate stability).
The method of Jones and Houston (2004) (link) was used to determine the in vitro half-life of substrate depletion. At least three independent incubations were performed, and results were assessed visually for reproducibility. However, due to differences in sampling time points between experiments, results from individual incubations were not combined.
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Publication 2023
acetonitrile Bath Buffers Centrifugation Cold Temperature Glucose-6-Phosphate Glucosephosphate Dehydrogenase Inversion, Chromosome Magnesium Chloride Methanol Microsomes NADP Phosphates Polypropylenes Proteins Staphylococcal Protein A
Human microsomes were purchased from Tebu-bio2 (Peterborough, UK). The microsomes were prepared from a pool of 50, mixed gender (20 mg protein ml⁻1) liver samples. DEHTP and MEHTP (purity 98.6%) were provided by BASF SE. All chemicals used were of analytical grade or higher; B-nicotinamide adenine dinucleotide phosphate (NADP), purity 97%, Glucose-6-phosphate, 98%–100%, Magnesium chloride, ACS reagent >99%, and Glucose-6-phosphate dehydrogenase (type V from baker’s yeast) were obtained from Sigma Aldrich. Potassium dihydrogen phosphate, analytical grade, and Di-potassium hydrogen phosphate, analytical grade, were obtained from Fisher Scientific.
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Publication 2023
Glucose-6-Phosphate Glucosephosphate Dehydrogenase Homo sapiens Liver Magnesium Chloride Microsomes NADP potassium phosphate, dibasic potassium phosphate, monobasic Proteins Saccharomyces cerevisiae
DNJ (purity >99.0%) and SZ-A extract (Lot No.: J202004007, containing 36.88% of DNJ, 8.78% of FA, and 5.83% of DAB; Lot No.: J202108007, containing 36.52% of DNJ, 9.60% of FA, and 7.62% of DAB) were provided by Beijing Wehand-bio Pharmaceutical Co. Ltd. (Beijing, China). The multiple reaction monitoring (MRM) chromatogram of SZ-A is shown in Supplementary Figure S1. Miglitol was obtained from TCI Shanghai Chemical Industrial Development Co., Ltd. (Shanghai, China). FA (purity >98.0%) was purchased from MedChemExpress (Monmouth Junction, NJ, United States ). DAB (purity >98.0%) was purchased from Sigma-Aldrich (St. Louis, MO, United States ). Human liver microsomes (HLMs) were purchased from Reid Liver Disease Research (Shanghai, China). Glucose-6-phosphate, oxidized coenzyme H (β-NADP), Glucose-6-phosphate dehydrogenase, midazolam, phenacetin, dextromethorphan, mephenytoin, chlorzoxazone, diclofenac sodium, 1-Hydroxy-midazolam, 4-hydroxy-mephenytoin, acetaminophen, 4-Hydroxy-diclofenac sodium, demethyldextromethorphan, 6-Hydroxy-chlorzoxazone, furaphylline, sulfafenpyrazole, quinidine, ketoconazole, and sodium diethyldithiacarbamate were purchased from Sigma-Aldrich (St. Louis, MO, United States ). All other organic reagents were of analytical grade and purchased from Sinopharm Chemical Reagent (Shanghai, China).
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Publication 2023
4'-hydroxydiclofenac Acetaminophen Chlorzoxazone Coenzymes Dextromethorphan Diclofenac Sodium Glucose-6-Phosphate Glucosephosphate Dehydrogenase Hepatobiliary Disorder Homo sapiens Ketoconazole Mephenytoin Microsomes, Liver Midazolam miglitol NADP Pharmaceutical Preparations Phenacetin Quinidine Sodium
The recombinant CYP6A14 and CYP6N6 proteins were tested in an in vitro nicotinamide adenine dinucleotide phosphate regeneration system to determine their deltamethrin degradation ability. The reaction system in 2 mL PBS (pH, 7.4) consisted of 1 mM glucose-6-phosphate dehydrogenase, 1 mM glucose 6-phosphate, 0.25 mM MgCl2, 0.1 mM NADP+, 1 mg/L deltamethrin, and 50 mg/L recombinant protein CYP6A14/CYP6N6. The reaction was performed at 30°C and 200 rpm for 5, 10, 30, and 60 minutes. Finally, the reaction was terminated by incubating with 100 μL methanol (chromatographic grade) for 5 minutes. The reaction without the recombinant protein was used as a blank control. The samples were centrifuged at 12,000 rpm and 4°C for 15 minutes. The obtained supernatants were used to measure the concentration and degradation products of deltamethrin by gas chromatography–tandem mass spectrometry (GC-MS/MS) using a C18 column. The conditions were as follows: sample size, 1 μL; column temperature, 30°C; flow rate, 0.3 mL/minute; mobile phase composition, distilled water, 0.1% formic acid, and chromatographic pure acetonitrile; injection volume, 2 μL; and automatic injection temperature, 4°C.
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Publication 2023
acetonitrile Chromatography decamethrin formic acid G6PD protein, human Gas Chromatography-Mass Spectrometry Glucose-6-Phosphate Magnesium Chloride Methanol NADP Proteins Recombinant Proteins Regeneration Tandem Mass Spectrometry

Top products related to «Glucose-6-Phosphate»

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Glucose-6-phosphate is a chemical compound that plays a crucial role in cellular metabolism. It is an intermediate in the glycolysis pathway, which is the process of breaking down glucose to generate energy for the cell. Glucose-6-phosphate is the product of the first step in glycolysis, where glucose is phosphorylated by the enzyme hexokinase. This compound is a key component in various biochemical processes, including energy production, glucose storage, and the pentose phosphate pathway.
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Glucose-6-phosphate dehydrogenase is an enzyme that catalyzes the conversion of glucose-6-phosphate to 6-phosphoglucono-δ-lactone, the first step of the pentose phosphate pathway. This enzyme plays a crucial role in maintaining cellular redox balance and generating NADPH, which is essential for various cellular processes.
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D-Glucose-6-phosphate is a chemical compound that serves as a key intermediate in carbohydrate metabolism. It is the product of the phosphorylation of glucose by the enzyme hexokinase. D-Glucose-6-phosphate is an important precursor for various metabolic pathways, including glycolysis and the pentose phosphate pathway.
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Phenacetin is a chemical compound used in the manufacturing of various pharmaceutical and laboratory products. It serves as a key ingredient in the production process. Phenacetin has specific functional properties that make it a valuable component in relevant applications, but a detailed description of its core function is beyond the scope of this response.
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NADPH, or Nicotinamide Adenine Dinucleotide Phosphate, is a cofactor essential for various cellular processes. It plays a crucial role in enzymatic reactions, serving as an electron donor in oxidation-reduction reactions. NADPH is a key component in several metabolic pathways, including biosynthesis, antioxidant defense, and energy production.
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Chlorzoxazone is a laboratory chemical used as a reference standard. It is a crystalline solid with a molecular formula of C7H5ClNO. Chlorzoxazone is primarily used for analytical purposes and quality control in various industries.
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DMSO is a versatile organic solvent commonly used in laboratory settings. It has a high boiling point, low viscosity, and the ability to dissolve a wide range of polar and non-polar compounds. DMSO's core function is as a solvent, allowing for the effective dissolution and handling of various chemical substances during research and experimentation.
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Formic acid is a colorless, pungent-smelling liquid chemical compound. It is the simplest carboxylic acid, with the chemical formula HCOOH. Formic acid is widely used in various industrial and laboratory applications.
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Quinidine is a pharmaceutical compound used as a laboratory reagent. It is a diastereomer of the alkaloid quinine and has a chemical structure that allows it to be used in various biochemical and analytical applications.
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Bovine serum albumin (BSA) is a common laboratory reagent derived from bovine blood plasma. It is a protein that serves as a stabilizer and blocking agent in various biochemical and immunological applications. BSA is widely used to maintain the activity and solubility of enzymes, proteins, and other biomolecules in experimental settings.

More about "Glucose-6-Phosphate"

Glucose-6-phosphate (G6P) is a crucial metabolite that plays a central role in various biological processes.
As an intermediate in the glycolytic pathway, G6P serves as a substrate for the enzyme glucose-6-phosphate dehydrogenase, which is a key player in the pentose phosphate pathway.
This versatile molecule also participates in glycogen synthesis and gluconeogenesis, making it a pivotal component in carbohydrate metabolism.
Researchers studying G6P may investigate its regulation, enzymatic activities, and implications in metabolic disorders such as glucose-6-phosphate dehydrogenase (G6PD) deficiency.
G6PD deficiency is a genetic condition that can lead to anemia and other health issues, and understanding the role of G6P is crucial for developing effective treatments.
In addition to its importance in metabolism, G6P is also related to other compounds like NADPH, which is generated in the pentose phosphate pathway and plays a vital role in cellular redox balance and antioxidant defense.
Other related terms include D-glucose-6-phosphate, phenacetin, chlorzoxazone, DMSO, formic acid, and quinidine, all of which may interact with or influence the behavior of G6P in the body.
Optimizing research on G6P can be greatly enhanced by leveraging the power of AI-driven platforms like PubCompare.ai.
These tools can help researchers easily locate the best protocols from literature, preprints, and patents, as well as identify the optimal products and procedures for their studies.
By utilizing the latest advancements in research optimization, scientists can uncover valuable insights and accelerate the progress of their work on this essential metabolite.