Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “PENTOSES”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 469 records · Page 26Linked to original sources
PubMed1978

Comparison of the kinetic properties of ribulose bisphosphate carboxylase in chloroplast extracts of spinach, sunflower and four other reductive pentose phosphate-pathway species.

Extracts from chloroplasts of spinach, sunflower and four other reductive pentose phosphate (C3)-pathway species were measured spectrophotometrically with or without a modified preactivation procedure. In all six species this modification yielded Km (CO2) values in the range of 7-15 micron and maximum velocities, at 20 degrees C, of 129-431 mumol of CO2 carboxylated/h per mg of chlorophyll. In general, both the carboxylation and electron-transport capacities of sunflower were somewhat greater than that of the other species, and this is discussed in relation to the superior rates of photosynthesis believed to be displayed by the parent tissue.

Brassica↗
PubMed1981

Effect of fructose feeding on the activity of enzymes of glycolysis, gluconeogenesis, and the pentose phosphate shunt in the liver and jejunal mucosa of rats.

The influence of fructose feeding for 1 to 12 days on the activity of enzymes of glycolysis and gluconeogenesis was studied in the jejunal mucosa and the liver of rats. In the jejunal mucosa fructose feeding leads to an increase in the activity of 6-phosphofructokinase (p less than 0.05) and fructose-1.6-bisphosphate aldolase (p less than 0.05), while the activity of hexokinase and glucose-6-phosphate dehydrogenase remains unchanged. Fructose feeding increases the activity of fructose-bisphosphatase in the jejunal mucosa, however, the absolute values of this enzyme remain low (less than 10%) when compared to those in the liver. In the liver fructose feeding is followed by a marked increase of the activity of fructose-bisphosphatase and glucose-6-phosphate dehydrogenase. In contrast, the activity of glucose-6-phosphatase decreases significantly under a fructose enriched diet. The enzyme activity rose to a maximum within 3 days; in the following time of observation no major changes occurred. The results are in accordance with the assumption that fructose feeding leads in the jejunal mucosa mainly to adaptive alterations of the activity of those enzymes which are involved in the breaking-down of fructose, whereas in the liver the activity of those enzymes is increased, which take part in the new synthesis of glucose-6-phosphate or which direct glucose-6-phosphate into the pentose-phosphate.

Animals↗
PubMed1983

Enzyme relationships in a sorbitol pathway that bypasses glycolysis and pentose phosphates in glucose metabolism.

A pathway from glucose via sorbitol bypasses the control points of hexokinase and phosphofructokinase in glucose metabolism. It also may produce glycerol, linking the bypass to lipid synthesis. Utilization of this bypass is favored by a plentiful supply of glucose--hence, conditions under which glycolysis also is active. The bypass further involves oxidation of NADPH, so the pentose phosphate pathway and the bypass are mutually facilitative. Possible consequences in different organs under normal and pathological, especially diabetic, conditions are detailed. Enzymes with related structures (for example, sorbitol dehydrogenase and alcohol dehydrogenase, and possibly, aldehyde reductase and aldose reductase, respectively) are linked functionally by this scheme. Some enzymes of the bypass also feature in glycolysis (aldolase and alcohol dehydrogenase), and these enzymes, with the reductases involved, are proteins known to occur in different classes or multiple isozyme forms. Two of the enzymes (aldolase and alcohol dehydrogenase) both involve classes with and without a catalytic metal (zinc). The existence of parallel pathways and the occurrence of similar enzymic steps in one pathway may help to explain the abundance and multiplicity of enzymes such as reductases, aldolases, and alcohol dehydrogenases.

Alcoholism↗
PubMed1995

Enzymatic Evidence for a Complete Oxidative Pentose Phosphate Pathway in Chloroplasts and an Incomplete Pathway in the Cytosol of Spinach Leaves.

The intracellular localization of transaldolase, transketolase, ribose-5-phosphate isomerase, and ribulose-5-phosphate epimerase was reexamined in spinach (Spinacia oleracea L.) leaves. We found highly predominant if not exclusive localization of these enzyme activities in chloroplasts isolated by isopyknic centrifugation in sucrose gradients. Glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, glucose phosphate isomerase, and triose phosphate isomerase activity was present in the chloroplast fraction but showed additional activity in the cytosol (supernatant) fraction attributable to the cytosol-specific isoforms known to exist for these enzymes. Anion-exchange chromatography of proteins of crude extracts on diethylaminoethyl-Fractogel revealed only a single enzyme each for transaldolase, transketolase, ribose-5-phosphate isomerase, and ribulose-5-phosphate epimerase. The data indicate that chloroplasts of spinach leaf cells possess the complete complement of enzymes of the oxidative pentose phosphate path-way (OPPP), whereas the cytosol contains only the first two reactions, contrary to the widely held view that plants generally possess a cytosolic OPPP capable of cyclic function. The chloroplast enzymes transketolase, ribose-5-phosphate isomerase, and ribulose-5-phosphate epimerase appear to be amphibolic for the Calvin cycle and OPPP.

Journal Article↗
PubMed1967

Photosynthesis in Rhodospirillum rubrum. 3. Metabolic control of reductive pentose phosphate and tricarboxylic acid cycle enzymes.

Enzymes of the reductive pentose phosphate cycle including ribulose-diphosphate carboxylase, ribulose-5-phosphate kinase, ribose-5-phosphate isomerase, aldolase, glyceraldehyde-3-phosphate dehydrogenase and alkaline fructose-1,6-diphos-phatase were shown to be present in autotrophically grown Rhodospirillum rubrum. Enzyme levels were measured in this organism grown photo- and dark heterotrophically as well. Several, but not all, of these enzymes appeared to be under metabolic control, mediated by exogenous carbon and nitrogen compounds. Light had no effect on the presence or levels of any of these enzymes in this photosynthetic bacterium. The enzymes of the tricarboxylic acid cycle and enolase were shown to be present in R. rubrum cultured aerobically, autotrophically, or photoheterotrophically, both in cultures evolving hydrogen and under conditions where hydrogen evolution is not observed. Light had no clearly demonstrable effect on the presence or levels of any of these enzymes.

Alkaline Phosphatase↗
PubMed1968

Evidence for the participation of the reductive pentose phosphate cycle in photoreduction and the oxyhydrogen reaction.

The assimilation of (14)C-sodium bicarbonate has been measured in Scenedesmus obliquus as 1) photosynthesis, 2) photoreduction (light dependent incorporation of carbon dioxide by hydrogen adapted cells under conditions where photosynthesis is inoperative), and 3) the oxyhydrogen reaction (dark assimilation of carbon dioxide by hydrogen adapted cells in an atmosphere of hydrogen and 1% oxygen). Degradation of the glucose formed in each of these reactions using the Leuconostoc technique establishes the participation of the reductive pentose phosphate cycle.

Journal Article↗
PubMed1968

Inositol Metabolism in Plants. V. Conversion of Myo-inositol to Uronic Acid and Pentose Units of Acidic Polysaccharides in Root-tips of Zea mays.

The metabolism of myo-inositol-2-(14)C, d-glucuronate-1-(14)C, d-glucuronate-6-(14)C, and l-methionine-methyl-(14)C to cell wall polysaccharides was investigated in excised root-tips of 3 day old Zea mays seedlings. From myo-inositol, about one-half of incorporated label was recovered in ethanol insoluble residues. Of this label, about 90% was solubilized by treatment, first with a preparation of pectinase-EDTA, then with dilute hydrochloric acid. The only labeled constituents in these hydrolyzates were d-galacturonic acid, d-glucuronic acid, 4-O-methyl-d-glucuronic acid, d-xylose, and l-arabinose, or larger oligosaccharide fragments containing these units. Medium external to excised root-tips grown under sterile conditions in myo-inositol-2-(14)C contained labeled polysaccharide.When label was supplied in the form of d-glucuronate, the pattern of labeled uronic acid and pentose units in cell wall polysaccharides resembled that obtained from labeled myo-inositol, indicating that both substances were metabolized along a common path during polysaccharide formation, and that methylation occurred at a step subsequent to uronic acid formation. When label was supplied in the form of l-methionine-methyl-(14)C, 4-O-methyl-d-glucuronic acid was the only labeled monosaccharide component that survived enzymatic or acid hydrolysis.Zea mays endosperm, a known source of phytin, developed maximal phytase activity after the third day of germination. Results obtained here suggest that myo-inositol released by hydrolysis of phytin represents the initial precursor of a normal, possibly predominant pathway for the formation of uronic acids in plants.

Journal Article↗
PubMed1970

Chloroplast and cytoplasmic enzymes: three distinct isoenzymes associated with the reductive pentose phosphate cycle.

Three pea (Pisum sativum) leaf chloroplast enzymes-triose phosphate isomerase, glyceric acid 3-phosphate kinase, and fructose 1,6-diphosphate aldolase-have been separated from the corresponding cytoplasmic enzymes by isoelectric focusing. These three enzymes of the reductive pentose phosphate cycle are therefore distinct proteins, not identical with the analogous enzymes of the Embden-Meyerhof-Parnas pathway.

Journal Article↗
PubMed1978

Pentose phosphate metabolism of potato tuber discs as influenced by prior storage temperature.

Tubers of Solanum tuberosum L. var. Russet Burbank, Kennebec, and Targhee were stored at 95% relative humidity and at 1.7, 4.4, 5.8, 7.2 or 10 C. Rates of O(2) consumption were measured periodically by removing individual tubers from storage, excising discs of pith parenchyma tissue, and incubating the discs in a Gilson respirometer at 30 C. With all three varieties, data suggest a greater involvement of pentose phosphate metabolism with tissues from tubers stored at 1.7 C as compared to those from higher temperatures. Discs from tubers stored at 1.7 C had higher respiratory quotient values (CO(2)/O(2)), were substantially less sensitive to the inhibitory effects of iodoacetic acid, and were somewhat more sensitive to the inhibitory effects of salicylhydroxamic acid than the discs from tubers stored at higher temperatures. Using [(14)C]glucose labeled in the 1 or the 6 carbon, mean C(1) to C(6) ratios in the Gilson after 3.5 hours of aging were 4.8:1 with discs from tubers stored at 1.7 C and 2.5:1 with discs from tubers stored at 7.2 C. Prior storage history is important in metabolic studies using potato tubers.

Journal Article↗
PubMed1982

The Effects of Cyanide and Azide on the Photoreduction of 3-Phosphoglycerate and Oxaloacetate by Wild Type and Two Reductive Pentose Phosphate Cycle Mutants of Chlamydomonas reinhardtii.

3-Phosphoglycerate- and oxaloacetate-dependent O(2) photoevolution by permeabilized cell preparations (Pressates), prepared from wild type (Wt) and two reductive pentose phosphate cycle mutants of Chlamydomonas reinhardtii showed different sensitivities to the inhibitors sodium cyanide and sodium azide. NaCN (1.5 millimolar) severely inhibits both CO(2)- and 3-phosphoglycerate-dependent O(2) photoevolution by the Wt Pressate, but does not inhibit 3-phosphoglycerate-dependent O(2) photoevolution by Pressates prepared from the mutants rcl-u-1-10-6C (which lacks ribulose, 1-5, bisphosphate carboxylase activity) and F60 (which lacks phosphoribulokinase activity). NaN(3) (0.5 millimolar) inhibits 3-phosphoglycerate-dependent O(2) photoevolution by the rcl-u-1-10-6C Pressate more severely than in the Pressates prepared from F60 and Wt. A higher concentration of NaN(3) (2.0 millimolar) severely inhibited oxaloacetate-dependent O(2) photoevolution by the rcl-u-1-10-6C, but not by the F60 Pressate. O(2) exchange-dependent upon methyl viologen was not strongly inhibited by 2 millimolar NaN(3) in either of the mutant Pressates. The data suggests that the mutational lesions which resulted in decreased ribulose-1,5-bisphosphate carboxylase and phosphoribulokinase activities effected changes in other photosynthetic reactions, either by direct interactions between component proteins or by causing changes in substrate or cofactor availability to the partial reactions.

Journal Article↗
PubMed1985

Changes in Levels of Intermediates of the C(4) Cycle and Reductive Pentose Phosphate Pathway during Induction of Photosynthesis in Maize Leaves.

Changes in the level of metabolites of the C(4) cycle and reductive pentose phosphate (RPP) pathway were measured simultaneously with induction of photosynthesis in maize (Zea mays L.) to evaluate what may limit carbon assimilation during induction in a C(4) plant.After 20 minutes in the dark, there was an immediate rise in photosynthesis during the first 30 seconds of illumination, followed by a gradual rise approaching steady-state rate after 20 minutes of illumination. Among metabolites of the C(4) cycle, there was a net increase in the level of C(3) compounds (the sum of pyruvate, alanine, and phosphoenolpyruvate) during the first 30 seconds of illumination, while there was a net decrease in the level of C(4) acids (malate plus aspartate). The total level of metabolites of the C(4) cycle underwent a sharp increase during this period. At the same time, there was a sharp rise in the level of intermediates of the RPP pathway (ribulose-1,5-bis-phosphate, 3-phosphoglycerate, dihydroxyacetonephosphate, and fructose-1,6-bisphosphate) during the first minute of illumination. The net increase of carbon among intermediates of the C(4) cycle and RPP pathway was far above that of carbon input from CO(2) fixation, and the increase in intermediates of the RPP pathway could not be accounted for by decarboxylation of C(4) acids, suggesting that an endogenous source of carbon supplies the cycles. After 3 minutes of illumination there was a gradual rise in the levels of intermediates of the C(4) cycle and in the total level of metabolites measured in the RPP pathway. This rise in metabolite levels occurs as photosynthesis gradually increases and may be required for carbon assimilation to reach maximum rates in C(4) plants. This latter stage of inductive autocatalysis through the RPP pathway may contribute to the final buildup of these intermediates.

Journal Article↗
PubMed1987

Changes in Levels of Intermediates of the C(4) Cycle and Reductive Pentose Phosphate Pathway under Various Light Intensities in Maize Leaves.

The rate of CO(2) assimilation and levels of metabolites of the C(4) cycle and reductive pentose phosphate pathway in attached leaves of maize (Zea mays L.) were measured over a range of light intensity from 0 to 1,900 microEinsteins per square meter per second under a saturated CO(2) concentration of 350 microliters per liter and a limiting CO(2) concentration of 133 microliters per liter. The level of ribulose 1,5-bisphosphate (RuBP) stayed almost constant (around 60 nanomoles per milligram chlorophyll [Chl]) from low to high light intensities under 350 microliters per liter. Levels of 3-phosphoglycerate (PGA) increased from 100 to 650 nanomoles per milligram Chl under 350 microliters per liter CO(2) with increasing light intensity. The calculated RuBP concentration of 6 millimolar (corresponded to 60 nanomoles per milligram Chl) was about two times above the estimated RuBP binding-site concentration on ribulose bisphosphate carboxylase-oxygenase (Rubisco) of approximately 2.6 millimolar in maize bundle sheath chloroplasts in the light. The ratio of RuBP/PGA increased with decreasing light intensity under 350 microliters per liter CO(2). These results suggest that RuBP carboxylation is under control of light intensity possibly due to a limited supply of CO(2) to Rubisco through the C(4) cycle whose activity is highly dependent on light intensity. Pyruvate level increased with increasing light intensity as long as photosynthesis rate increased. A positive relationship between levels of PGA and those of pyruvate during steady-state photosynthesis under various conditions suggests that an elevated concentration of PGA increases the carbon input into the C(4) cycle through the conversion of PGA to PEP and consequently the level of total intermediates of the C(4) cycle can be raised to mediate higher photosynthesis rate.

Journal Article↗
PubMed1990

Enzyme Sets of Glycolysis, Gluconeogenesis, and Oxidative Pentose Phosphate Pathway Are Not Complete in Nongreen Highly Purified Amyloplasts of Sycamore (Acer pseudoplatanus L.) Cell Suspension Cultures.

Differential centrifugation and Percoll-gradient centrifugation of protoplast lysates of suspension-cultured cells of sycamore (Acer pseudoplatanus L.) yielded pure amyloplasts. Contamination of the final amyloplast preparation by foreign compartments was assessed by measuring marker enzyme activities. The activity of alkaline pyrophosphatase was taken as a 100% plastid marker; relative to this marker, mitochondria (cytochrome c oxidase) averaged 0.34%, microbodies (catalase) 0.61%, and cytosol (alcohol dehydrogenase) 0.09%. Enzymatic activities of the glycolytic, gluconeogenic, pentose phosphate and the starch degradation pathways were found to be present in these amyloplast extracts in appreciable amounts. But the pyrophosphate-dependent phosphofructokinase and phosphoglyceromutase were judged to be essentially absent from amyloplasts because the activities of these enzymes were not enriched above the level of contaminating enzymatic activities in the amyloplast fractions. Additionally, the in vitro activities of starch phosphorylase, ATP dependent phosphofructokinase, NAD dependent glyceraldehyde-3 phosphate dehydrogenase, and glucose-6 phosphate dehydrogenase did not seem to support carbon fluxes from starch to triose phosphates as calculated from the rate of starch disappearance during carbon starvation of the cells. These results provide additional, indirect evidence for the recently emerged view that, in addition to the well known phosphate-triosephosphate translocator, another hexose phosphate and possibly also an ATP/ADP translocating system play major roles in nongreen plastids.

Journal Article↗
PubMed1975

The effect of o-salicylate upon pentose phosphate pathway activity in normal and G6PD-deficient red cells.

The effect of the major metabolite of aspirin, namely salicylic acid, upon the pentose phosphate pathway (PPP) of normal and G6PD-deficient red cells has been studied. Salicylic acid was shown to inhibit this pathway in proportion to the amount present. At any concentration of this substance there was greater inhibition of the PPP in G6PD-deficient than in normal red cells.

Blood Glucose↗
PubMed1983

Effect of dexamethasone on testicular enzymes of the Embden-Meyerhof and pentose-phosphate pathways.

The influence of dexamethasone on the specific activities of testicular enzymes involved in the Embden-Meyerhof and pentose-phosphate pathways was studied in pre-pubertal, pubertal and adult rats. All of the enzymes showed a decrease in specific activity after dexamethasone treatment, an effect which was most drastic in pre-pubertal animals. After cessation of treatment, the specific activity of all the enzymes reverted to normal levels, except for glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase in the pre-pubertal group.

Aging↗
PubMed1981

Glycolytic, pentose-phosphate shunt and transaminase enzymes in gastrocnemius muscle, liver, heart, and brain of two mouse mutants, 129 J-dy and A2g-adr, with abnormal muscle function.

Aldolase and phosphoglycerate kinase activity were markedly reduced in muscle from two mouse mutants, 129 J-dy and A2G-adr, with abnormal muscle development. The pentose-phosphate shunt enzymes, glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase, were both greatly increased in the gastrocnemius of 129 J-dy mice, but only the former was slightly increased in A2G-adr muscle. Alanine and aspartate aminotransferase activities were normal or low in 129 J-dy muscle but increased to approximately 200% in A2G-adr muscle. Liver from 129 J-dy mice showed increased activity of glucose-6-phosphate dehydrogenase. These findings are compatible with the well-recognised lipid involvement in the 129 J-dy mutant but indicate that an abnormality of amino acid metabolism in relation to energy supply is probably more important in the A2G-adr mutant.

Animals↗
PubMed1976

Effects of phospholine iodide on the metabolites of the glycolytic, pentose phosphate and sorbitol pathways in the rabbit lens.

Steady-state concentrations of the key intermediates from the glycolytic, pentose phosphate, and sorbitol pathways as well as the pyridine nucleotides were measured from the lens after 0.25% phospholine iodide had been instilled into rabbits' eyes twice a day for 18 weeks. In the lenses of those rabbits which had received treatment in both eyes fructose-1,6-diphosphate and pyruvate levels were increased, whereas 6-phosphogluconate, sorbitol and alpha-glycer0phosphate concentrations were decreased. alpha-Ketoglutarate and concentrations and ratios of NAD+ and NADH did not show any changes. In contrast, NADPH and total NADP concentrations as well as the NADPH/NADP+ ratio were decreased, and therefore total NAD/total NADP ratio increased after treatment. It appears that instillation of long-acting 0.25% phospholine iodide into rabbits' eyes results in increased glycolytic activity in the lens in response to the increased energy demand, wheras the activities of other metabolic pathways are suppressed.

Animals↗
PubMed1970

The effect of insulin on the kinetics of pentose permeation of the rat heart.

1. The kinetics of permeation of pentoses into the rat heart in the presence of insulin are similar in nature to those in the absence of insulin.2. The half-saturation concentration of the carrier system is increased by insulin in a manner which is independent of insulin concentration.3. The V(max) of the carrier system is altered by insulin in a graded fashion: at low insulin concentrations it may be lower than in the absence of insulin.4. It is shown that these effects can be accounted for if insulin combines with the carrier and thereby increases either the rate constant governing the mobility of the carrier in the membrane or the rate constant governing dissociation of the sugar-carrier complex.5. The effects cannot be accounted for by a graded action of insulin on the membrane as distinct from the carrier.

Animals↗