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PubMed1986

Purification and properties of the enzyme 6-phosphogluconate dehydrogenase from Dicentrarchus labrax L. liver.

The enzyme 6-phosphogluconate dehydrogenase (6-phospho-D-gluconate: NADP+ oxidoreductase, decarboxylating EC 1.1.1.44) from bass liver has been purified to over 95% of homogeneity by gel filtration, affinity and ion exchange chromatographies. The apparent molecular weight was estimated by gel filtration chromatography to about 100,000. Analysis of the enzyme on sodium dodecyl sulphate polyacrylamide gel electrophoresis showed to be a dimeric protein. The effect of pH and kinetic properties were studied.

Animals↗
PubMed1997

The cross-linking by o-phthalaldehyde of two amino acid residues at the active site of 6-phosphogluconate dehydrogenase.

o-phthalaldehyde inactivates homodimeric, NADP+ dependent, 6-phosphogluconate dehydrogenase from sheep liver, upon formation of a single isoindole derivative per enzyme subunit. This indicates that the thiol group of a cysteine residue or the epsilon-amino group of a lysine residue located within 3 A and crosslinked by the reagent is essential for catalysis. Fluorescence analyses of the modified enzyme suggest that the isoindole derivative forms at the binding site of the nicotinamide moiety of NADP+. The enzymes from Trypanosoma brucei and Lactococcus lactis are also inactivated suggesting a similar three-dimensional structure in this domain. The isoindole derivative does not form with two mutants of the T. brucei enzyme (Lys185His and Lys185Leu), this allowing to identify not only the lysine but also the cysteine involved in the cross-linking. The formation of the isoindole derivative inactivates not only the oxidative decarboxylation, but also two partial reactions catalysed by the enzyme.

Animals↗
PubMed1983

Age-dependent changes in glucose 1,6-bisphosphate levels and in the activities of glucose 1,6-bisphosphatase, and particulate hexokinase and 6-phosphogluconate dehydrogenase in rat skin.

The levels of glucose 1,6-bisphosphate (Glc-1,6-P2), the powerful regulator of carbohydrate metabolism, changed in rat skin during growth: Glc-1,6-P2 increased during the first week of age, and thereafter was dramatically reduced during maturation. The activity of glucose 1,6-bisphosphatase, the enzyme that degradates Glc-1,6-P2, changed with age in an invert manner as compared to the changes in Glc-1,6-P2. These findings suggest that the age dependent changes in this enzyme's activity may account for the changes in intracellular Glc-1,6-P2 concentration. The age-related changes in Glc-1,6-P2 were accompanied by concomitant changes in the activities of particulate (mitochondrial) hexokinase and 6-phosphogluconate dehydrogenase, the two enzymes known to be inhibited by Glc-1,6-P2. The activities of both these enzymes in the soluble fraction were not changed with age. The particulate enzymes were more susceptible to inhibition by Glc-1,6-P2 than the soluble activities, which may explain why only the particulate, but not the soluble activities, correlated with the age-dependent changes in tissue Glc-1,6-P2. These results suggest that the changes in particulate hexokinase and 6-phosphogluconate dehydrogenase resulted from changes in intracellular concentration of Glc-1,6-P2. The marked reduction in Glc-1,6-P2 during maturation, accompanied by activation of mitochondrial hexokinase and 6-phosphogluconate dehydrogenase, may reflect an enhancement in skin metabolism during growth.

Aging↗
PubMed1995

Purification and properties of 6-phosphogluconate dehydrogenase from beet leaves.

We have purified to homogeneity 6-Phosphogluconate dehydrogenase from leaves of silver beet (Beta vulgaris L.) by means of cation-exchange and affinity chromatography. The enzyme is a homodimer of 52 kDa subunits; it catalyzes NADP dependent oxidation of 6-P-gluconate with Michaelian substrate saturation. The activity is affected by some intermediates of carbohydrate metabolism, particularly erythrose-4-P. Subcellular fractionation studies indicate the cytosolic location of the enzyme.

Chromatography, Affinity↗
PubMedDate not supplied

General stability of thermophilic enzymes: studies on 6-phosphogluconate dehydrogenase from Bacillus stearothermophilus and yeast.

The thermophilic enzyme 6-phosphogluconate dehydrogenase (6-phospho-D-gluconate:NADP oxidoreductase, decarboxylating, EC 1.1.1.44) from Bacillus stearothermophilus was much more resistant to inactivation under different conditions of temperature, pH, guanidine-hydrochloride, and organic solvents (dioxane, dimethylformamide, acetone) than its mesophilic counterpart from yeast. In addition, the thermophilic enzyme largely withstands proteolysis with trypsin, chymotrypsin, and elastase when compared with the yeast enzyme. It is proposed that thermophilic enzymes are not only thermostable, but also generally more stable to most common protein denaturants than their mesophilic counterparts. Because of their remarkable stability, enzymes isolated from thermophilic microorganisms may be ideally suited for technological applications.

Geobacillus stearothermophilus↗
PubMed1991

Implication of lysine residues in the loss of 6-phosphogluconate dehydrogenase activity in aging human erythrocytes.

The activity of 6-phosphogluconate dehydrogenase (6-PGDH) decreases in aged human erythrocyte populations. The aged enzyme has 11 lysine residues less than the young enzyme, when they are measured with 2,4,6-trinitro-benzenesulfonic acid (TNBS). Treatment of young enzyme with ascorbate for 15 min produces the loss of 8 lysine residues and the diminution of enzymatic activity. These results suggest that there is a modification of lysine residue in human erythrocytes during senescence, probably caused by oxidation. This modification of lysine residue could imply the loss of enzymatic activity. This result is similar to that found in rat liver 6-PGDH during aging, described previously (Gordillo et al., J. Biol. Chem. 264 (1989) 17014-17019).

Adult↗
PubMed1978

6-Phosphogluconate Dehydrogenase Isoenzymes from the Developing Endosperm of Ricinus communis L.

The cytosolic and proplastid isoenzymes of 6-phosphogluconate dehydrogenase were purified from the developing endosperm of the castor bean (Ricinis communis L.). No differences in physical or kinetic properties were found for the purified isoenzymes. Each was composed of two identical 55,000 subunits. They had identical pH optima of 7.8 to 8.0 and similar MgCl(2) stimulation for the oxidative decarboxylation of 6-phosphogluconate. The Km values for 6-phosphogluconate were 12 and 9.6 micromolar and for NADP(+) were 4.1 and 5.4 micromolar for the cytosolic and proplastid isoenzymes, respectively. Therefore, the synthesis of two distinct 6-phosphogluconate dehydrogenase isoenzymes does not appear to have any kinetic significance for the developing seed. However, changes in the proplastid contribution toward carbohydrate metabolism occur in the developing seed and may necessitate independent gene expression to allow for a unique and flexible subcellular distribution of isoenzymes during development.

Journal Article↗
PubMedDate not supplied

The effects of oral and intraperitoneal administration of ethanol on the activities of hepatic glucose-6-phosphate and 6-phosphogluconate dehydrogenases in rats.

The activities of hepatic glucose-6-phosphate and 6-phosphogluconate dehydrogenases decreased significantly only in male rats, when rats of both sexes were fed a 2% sucrose solution containing 25% ethanol for six weeks. Sucrose (2%) activation of these enzymes was significant only in female rats. The daily administration of ethanol (5 g/kg body wt.) by intraperitoneal injection for two weeks significantly decreased the activities of these enzymes and eliminated the sex differences in the response to ethanol ingestion.

Administration, Oral↗
PubMed1992

Expression and distribution of cytosolic 6-phosphogluconate dehydrogenase isozymes in maize.

Maize (Zea mays L.) cytosolic 6-phosphogluconate dehydrogenase isozymes (EC 1.1.1.44; 6-PGD) are encoded by unlinked loci Pgd1 and Pgd2. Two families from a Robertson's Mutator line were isolated which have no detectable expression of Pgd2. These Pgd2-null mutants and a Pgd1-null line were used to generate plants homozygous for null alleles at both cytosolic 6-PGD loci. The specific activity of 6-PGD in the double-null mutant was between 20 and 30% of wild-type levels in root extracts. The double-null mutant was reproductively viable in a moderate environment, suggesting that wild-type levels of cytosolic 6-PGD activity are not essential for growth. Isozyme dimer ratios in roots, leaves, and scutellum were binomial and reflected the wild-type gene copy number. 6-PGD isozymes showed tissue- and cell type-specific expression.

Cytosol↗
PubMedDate not supplied

6-phosphogluconate dehydrogenase, glucose-6-phosphate dehydrogenase, glucose-6-phosphate isomerase, and hexokinase activity ratios in some human tumor cytosols.

The ratios of some key enzymatic activities of carbohydrate metabolism have been measured in human tumor cytosols. The activities of whole hexokinase (low Km, EC 2.7.1.1 and high Km, EC 2.7.1.2), 6-phosphogluconate dehydrogenase (EC 1.1.1.43), glucose-6-phosphate dehydrogenase (EC 1.1.1.49) and glucose-6-phosphate isomerase (EC 5.3.1.9) change according to a biochemical pattern coherent with cell growth requirements. 6-phosphogluconate dehydrogenase activity was in each sample tested higher than glucose-6-phosphate dehydrogenase activity; this indicates that 6-phosphogluconate, a powerful inhibitor of glucose-6-phosphate isomerase, is unlikely to accumulate and inhibit this enzyme and glucose-6-phosphate channelling into glycolysis.

Cytosol↗
PubMed1981

[6-phosphogluconate dehydrogenase of Aspergillus oryzae (Ahlburg). II. Separation and study of isoenzymes].

Through ammonium sulphate fractionation followed by ion-exchange chromatography, two forms of 6-phosphogluconate dehydrogenase (6j-phosphogluconate: NADP+ oxidoreductase E.C. 1.1.1.44) were isolated from mycelium of Aspergillus oryzae. The Km values for 6PG were the same, but the Km for NADP+ was smaller for isoenzyme I. The Vmx values were also different, with greater activity for isoenzyme II. The optimum pH for isoenzyme I was 7.5. whereas the isoenzyme II had two maximum peaks, at pH 7.5 and 9. Isoenzyme II was the more resistant to thermal inactivation. Inhibition by NADPH was competitive with respect to NADP+, with a Ki value similar for both isoenzymes. The GSSG inhibits isoenzyme I and activates isoenzyme II. The apparent molecular weights determined by gel filtration were 79,000 +/- 2,000 daltons for isoenzyme I and 112,000 +/- 2,000 daltons for isoenzyme II.

Aspergillus↗
PubMed2006

Gender- and age-related changes in 6-phosphogluconate dehydrogenase gene expression in white adipose tissue of rats (Rattus norvegicus) are not related to serum testosterone concentration.

Previously, we have shown that the age-related changes in 6-phosphogluconate dehydrogenase (6PGDH) activity depend on sex, and that oestradiol is playing a crucial role in the regulation of 6PGDH gene expression in rat liver, but not in other tissues [Pankiewicz, A., Sledzinski, T., Nogalska, A., Swierczynski, J., 2003. Tissue specific, sex and age-related differences in the 6-phosphogluconate dehydrogenase gene expression. Int. J. Biochem. Cell Biol. 35, 235-245.]. To complete the knowledge on the influence of sex hormones on 6PGDH activity, experiments have been performed on the effect of testosterone on 6PGDH gene expression in rat white adipose tissue and liver. The results presented here disclosed that in young male rats high serum testosterone concentration was associated with high white adipose tissue 6PGDH activity. After orchidectomy, a decrease in serum testosterone concentration (both in young and old rats) was observed. In contrast, no changes in white adipose tissue and liver 6PGDH activity were found. In female rats, both young and old, serum testosterone concentration was below the limit of detection, whereas 6PGDH activity was much higher in young than in old animals. Moreover, the testosterone administration to 9-month old male rats (which displayed much lower serum testosterone concentration that young animals) resulted in no effect on 6PGDH activity either in WAT or in the liver. In conclusion, the results presented in this paper indicate that testosterone does not play any role in the age- and gender-related differences in 6PGDH gene expression in white adipose tissue.

Adipose Tissue↗
PubMed1979

Binding of coenzyme and substrate and coenzyme analogues to 6-phosphogluconate dehydrogenase from sheep liver. An X-ray study at 0.6 nm resolution.

The analogues of the coenzyme NADP+, nicotinamide--8-bromo-adenine dinucleotide phosphate (Nbr8ADP+) and 3-iodopyridine--adenine dinucleotide phosphate (io3PdADP+), were prepared. Nbr8ADP+ was found to be active in the hydrogen transfer adn io3PdADP+ is a coenzyme competitive inhibitor for 6-phosphogluconate dehydrogenase. The binding of NADP+, NADPH and NADPH together with 6-phosphogluconate as well as that of both analogues to crystals of the enzyme 6-phosphogluconate dehydrogenase has been investigated at 0.6-nm resolution using difference electron density maps. The molecules bind in a similar position in a cleft in the enzyme subunit distant from the dimer interface. The orientation of the coenzyme in the site has been determined from the io3PdADP+ -NADP+ difference density. The ternary complex difference density extends beyond that of the nicotinamide moiety of the coenzyme and tentatively indicates substrate binding. No clear identification of the bromine atom of Nbr8ADP+ can be made. However, the analogue is bound more deeply in the cleft than is NADP+. The NADPH density is the most clearly defined and has thus been used to fit a molecular model using an interactive graphics system, checking for preferred geometry. A possible conformation is presented which is significantly different from that of NAD+ in the lactate dehydrogenase ternary complex.

Animals↗
PubMed1992

Increased activity of 6-phosphogluconate dehydrogenase and glucose-6-phosphate dehydrogenase in purified cell suspensions and single cells from the uterine cervix in cervical intraepithelial neoplasia.

The activities of 6-phosphogluconate dehydrogenase and glucose-6-phosphate dehydrogenase have been measured in squamous epithelial cells of the uterine cervix from normal patients and cases of cervical intraepithelial neoplasia (CIN). A biochemical cycling method, which uses only simple equipment and is suited to routine use and to automation, was applied to cells separated by gradient centrifugation. In addition, cells were examined cytochemically, and the intensity of staining in the cytoplasm of single whole cells was measured using computerised microcytospectrophotometry. Twenty per cent of cells in samples from normal patients (n=61) showed staining intensities above an extinction of 0.15 at 540 nm, compared to 71% of cases of CIN 1 (n=14), 91% of cases of CIN 2 (n=11) and 67% of cases of CIN 3 (n=15). The cytochemical data do not allow definitive distinctions to be made between different grades of CIN whereas the biochemical assay applied to cell lysates shows convincing differences between normal samples and cases of CIN. There are no false negatives for CIN 3 (n=14) and CIN 2 (n=10) and 11% false negatives for CIN 1 (n=9) and 14% of false positives for normal cases (n=21). The results of this preliminary study with reference to automation are discussed [corrected].

Cell Separation↗