6-Phosphogluconic acid
6-Phosphogluconic acid structure
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Common Name | 6-Phosphogluconic acid | ||
|---|---|---|---|---|
| CAS Number | 921-62-0 | Molecular Weight | 276.135 | |
| Density | 2.0±0.1 g/cm3 | Boiling Point | 774.8±70.0 °C at 760 mmHg | |
| Molecular Formula | C6H13O10P | Melting Point | N/A | |
| MSDS | Chinese USA | Flash Point | 422.4±35.7 °C | |
| Symbol |
GHS07 |
Signal Word | Warning | |
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Inferring the metabolism of human orphan metabolites from their metabolic network context affirms human gluconokinase activity.
Biochem. J. 449(2) , 427-35, (2013) Metabolic network reconstructions define metabolic information within a target organism and can therefore be used to address incomplete metabolic information. In the present study we used a computational approach to identify human metabolites whose metabolism... |
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Phosphoglycerate mutase 1 coordinates glycolysis and biosynthesis to promote tumor growth.
Cancer Cell 22(5) , 585-600, (2012) It is unclear how cancer cells coordinate glycolysis and biosynthesis to support rapidly growing tumors. We found that the glycolytic enzyme phosphoglycerate mutase 1 (PGAM1), commonly upregulated in human cancers due to loss of TP53, contributes to biosynthe... |
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A novel NADPH:(bound) NADP+ reductase and NADH:(bound) NADP+ transhydrogenase function in bovine liver catalase.
Biochem. J. 385(Pt 3) , 763-8, (2005) Many catalases have the shared property of containing bound NADPH and being susceptible to inactivation by their own substrate, H2O2. The presence of additional (unbound) NADPH effectively prevents bovine liver and human erythrocytic catalase from becoming co... |
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Importance in catalysis of the 6-phosphate-binding site of 6-phosphogluconate in sheep liver 6-phosphogluconate dehydrogenase.
J. Biol. Chem. 281(35) , 25568-76, (2006) The 6-phosphate of 6-phosphogluconate (6PG) is proposed to anchor the sugar phosphate in the active site and aid in orientating the substrate for catalysis. In order to test this hypothesis, alanine mutagenesis was used to probe the contribution of residues i... |
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6-Phosphogluconate dehydrogenase mechanism: evidence for allosteric modulation by substrate.
J. Biol. Chem. 285(28) , 21366-71, (2010) The reductive carboxylation of ribulose-5-phosphate (Ru5P) by 6-phosphogluconate dehydrogenase (6PGDH) from Candida utilis was investigated using kinetic isotope effects. The intrinsic isotope effect for proton abstraction from Ru5P was found at 4.9 from deut... |
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Compartmentalized glucose metabolism in Pseudomonas putida is controlled by the PtxS repressor.
J. Bacteriol. 192(17) , 4357-66, (2010) Metabolic flux analysis revealed that in Pseudomonas putida KT2440 about 50% of glucose taken up by the cells is channeled through the 2-ketogluconate peripheral pathway. This pathway is characterized by being compartmentalized in the cells. In fact, initial ... |
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The Entner-Doudoroff pathway has little effect on Helicobacter pylori colonization of mice.
Infect. Immun. 71(5) , 2920-3, (2003) Helicobacter pylori mutants deficient in 6-phosphogluconate dehydratase (6PGD) were constructed. Colonization densities were lower and minimum infectious doses were higher for mutant strains than for wild-type strains. In spite of better colonization, however... |
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Multinuclear NMR study of the complexes of 6-phospho-D-gluconic acid with W(VI) and Mo(VI).
Carbohydr. Res. 339(13) , 2225-32, (2004) Multinuclear ((1)H, (13)C, (17)O, (31)P, (95)Mo, (183)W) magnetic resonance spectroscopy (1D and 2D) has been used to show that 6-phospho-d-gluconic acid forms three complexes with tungsten(VI) and six complexes with molybdenum(VI) in aqueous solution, depend... |
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Thermodynamic characterization of substrate and inhibitor binding to Trypanosoma brucei 6-phosphogluconate dehydrogenase.
FEBS J. 274(24) , 6426-35, (2007) 6-Phosphogluconate dehydrogenase is a potential target for new drugs against African trypanosomiasis. Phosphorylated aldonic acids are strong inhibitors of 6-phosphogluconate dehydrogenase, and 4-phospho-d-erythronate (4PE) and 4-phospho-d-erythronohydroxamat... |
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Biochemical characterization of recombinant phosphoglucose isomerase of Mycobacterium tuberculosis.
Biochem. Biophys. Res. Commun. 337(2) , 626-32, (2005) Phosphoglucose isomerase (PGI) is a well-characterized ubiquitous enzyme involved in the glycolytic pathway. It catalyzes the reversible isomerization of D-glucopyranose-6-phosphate and D-fructofuranose-6-phosphate and is present in all living cells. However,... |