Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.2.1.26 (invertase)
4,927 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The denaturation of eight purified yeast enzymes, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, 3-phosphoglycerate kinase, alcohol dehydrogenase, beta-fructosidase, hexokinase and glucose-6-phosphate isomerase, promoted under controlled conditions by the free fatty acids myristic and oleic, is selective. Glucose-6-phosphate dehydrogenase (D-glucose-6-phosphate:NADP+ 1 oxidoreductase, EC 1.1.1.49) is extremely sensitive to destabilization and was studied in greater detail. Results show that chain length and degree of unsaturation of fatty acids are important to their destabilizing effect, and that ligands of the enzyme can afford protection. The denaturation process results in more than one altered form. These results can be viewed in the perspective of the possibility that amphipathic substances, and in particular free fatty acids, may play a role for enzyme degradation in vivo, by initiating steps of selective denaturation.
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PMID:Selective denaturation of several yeast enzymes by free fatty acids. 35 87

Carboxypeptidase Y, a yeast vacuolar glycoprotein was expressed in oocytes from Xenopus laevis and its biosynthesis and sorting were examined. In yeast, targeting to the vacuole, the functional equivalent of the lysosome, is not mannose-6-phosphate-receptor dependent. It was found that carboxypeptidase enters the secretory pathway of the oocyte and is there glycosylated, phosphorylated in the carbohydrate part and delivered to the lysosome. Deletion of an amino acid sequence, previously shown to determine intracellular targeting of this enzyme in yeast, caused a loss of phosphorylation and mislocalization of carboxypeptidase Y into the oocyte medium. Inhibition of glycosylation of carboxypeptidase by tunicamycin did not lead to its secretion. In-frame fusion of the targeting domain to a secretory yeast glycoprotein, invertase, did not prevent its secretion. However, a hybrid containing 80% carboxypeptidase abolished invertase secretion. The results indicate that the vacuolar protein-targeting signal from yeast carboxypeptidase can, in principal, function in a higher eukaryote.
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PMID:The vacuolar protein-targeting signal of yeast carboxypeptidase is functional in oocytes from Xenopus laevis. 199 65

In synchronized continuous cultures of Saccharomyces cerevisiae CBS 8066, the production of the extracellular invertase (EC 3.2.1.26) showed a cyclic behavior that coincided with the budding cycle. The invertase activity increased during bud development and ceased at bud maturation and cell scission. The cyclic changes in invertase production resulted in cyclic changes in amounts of invertase localized in the cell wall. However, the amount of enzyme invertase present in the culture liquid remained constant throughout the budding cycle. Also, in asynchronous continuous cultures of S. cerevisiae, the production and localization of invertase showed significant fluctuation. The overall invertase production in an asynchronous culture was two to three times higher than in synchronous cultures. This could be due to more-severe invertase-repressive conditions in a synchronous chemostat culture. Both the intracellular glucose-6-phosphate concentration and residual glucose concentration were significantly higher in synchronous chemostat cultures than in asynchronous chemostat cultures. In the asynchronous and synchronous continuous cultures of S. cerevisiae, about 40% of the invertase was released into the culture liquid; it has generally been believed that S. cerevisiae releases only about 5% of its invertase. In contrast to invertase production and localization in the chemostat cultures of S. cerevisiae, no significant changes in inulinase (EC 3.2.1.7) production and localization were observed in chemostat cultures of Kluyveromyces maxianus CBS 6556. In cultures of K. marxianus about 50% of the inulinase was present in the culture liquid.
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PMID:Production and localization of beta-fructosidase in asynchronous and synchronous chemostat cultures of yeasts. 201 91

The effects of Gossypol acetic acid (10 mg/kg b. wt. daily for 15 days), an experimental male antifertility agent and its subsequent withdrawal for another 15 days, on the structure and functions of the rat small intestinal tract have been investigated. Gossypol feeding causes a reduction in body weight and intestinal weight, length, protein, and nucleic acid contents. A 27%-50% reduction in the uptake of glucose, alanine, leucine, and calcium is observed after Gossypol feeding which is found to be reversible after 15 days of withdrawal of the drug. Gossypol also causes a significant reduction in the activities of sucrase, lactase, maltase and alkaline phosphatase in the intestinal homogenates as well as in the purified brush border membrane of the microvillus. A decrease in the maximum of apparent enzyme velocity and no change in the substrate affinity constant in these digestive hydrolases are observed on Gossypol treatment. It also causes a shift in the transition temperature in these enzymes and predictably changes the energy of activation both below and above the temperature of transition, although the Arrhenius expression of the temperature dependence still shows proximity, non-linearity, and is parallel to the control group. These changes are reversed on withdrawal of the drug and during the subsequent recovery period. Recovery experiments also show near identical values in kinetic parameters (Kt and Jmax) of 14C-glucose uptake in jejunal segments both in the presence and absence of Na+ ions. Also, no difference is observed between the control and recovery groups with respect to body and intestinal weight, intestinal length, and DNA, RNA, protein, lactate dehydrogenase and glucose-6-phosphate phosphohydrolase values in the intestinal homogenates. Phospholipid, cholesterol and sialic acid levels in both the groups also show nearly identical values. Molecular mechanism of the effects of Gossypol on brush border membrane-bound enzyme/carrier molecules operation is discussed in view of the kinetic and thermodynamic data obtained.
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PMID:Reversibility of the effects of gossypol acetic acid, an antispermatogenic/antifertility agent on the intestinal structure and functions of male albino rats. 274 9

The addition of 88 mM sucrose to the culture medium of human skin fibroblasts from normal subjects caused remarkable increase in the intracellular lysosomal hydrolase activities. The mechanism of this induction by sucrose loading was carefully studied with several fibroblast strains of different inherited lysosomal storage disorders. In single lysosomal hydrolase defect such as GM1-gangliosidosis, mannosidosis and Sandhoff disease, no induction of the deficient hydrolase was found with 88 mM sucrose loading. In contrast, sucrose loading caused normalization of intracellular lysosomal hydrolase activities in I-cell disease fibroblasts and cytoplasmic inclusion materials disappeared. Subsequent investigations reveal that I-cell disease cells are classified into three subgroups by the degree of hydrolase induction by sucrose loading; a high responding, an intermediate responding and a no-response group. The heterogeneity may be based upon different induction by sucrose loading of the enzyme, probably the residual phosphotransferase which is involved in the processing steps of lysosomal enzyme molecules. With the addition of mannose-6-phosphate and 10 mM NH4Cl to cultured skin fibroblasts, it was shown that sucrose loading caused increased synthesis of lysosomal enzyme proteins. The result of the test with 2,4-dinitrophenol suggests that sucrose is indeed pinocytosed by cultured human skin fibroblasts and localized in lysosomes and that this event is the essential factor to trigger the induction of lysosomal hydrolases. Simultaneous loading of both invertase and sucrose in cultured cells caused no induction of alpha-mannosidase activity. This result indicates that invertase is also pinocytosed, reaches the lysosomes and hydrolyzes sucrose in the lysosomes. Lysosomal overloading with sucrose resulted in induction of lysosomal hydrolases and invertase blocked the induction of alpha-mannosidase activity. However, some induction still exists in beta-galactosidase and alpha-fucosidase activity. Thus it is very likely that the induction of lysosomal hydrolases demands a complicated process. In this article, we investigated the effects of sucrose on the lysosomal hydrolases in cultured human skin fibroblasts of several inherited lysosomal storage disorders and normal subjects and discuss the possible mechanism of the induction of lysosomal hydrolase activities by sucrose loading.
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PMID:The effects of sucrose loading on lysosomal hydrolases. 670 43

Glycosidases and glycosyltransferases were electrophoresed in the presence of sodium dodecyl sulfate (SDS) in a thin-layer gel supported by a glass plate, treated with the nonionic detergent Triton X-100, and specifically stained for the sugar-releasing activity of these enzymes. Staining is based on conversion of monosugars or a sugar phosphate to glucose-6-phosphate by the appropriate intermediary enzymes, reduction of NADP+ to NADPH, and accumulation of reduced Nitroblue Tetrazolium in the gel. Among the enzymes tested, alpha-glucosidase, beta-glucosidase and beta-mannosidase could not be renatured, whereas beta-fructofuranosidase and alpha-mannosidase could be renatured unless heated before electrophoresis. Sucrose phosphorylase, glucosyltransferase and fructosyltransferase, which are single-peptide proteins with no cystine bond, could be renatured even after pretreatment with SDS and/or mercaptoethanol at 100 degrees C for 10 min. However, exclusive heating remarkably decreased the activities of these enzymes. Two-dimensional separation of the five renaturable enzymes was done in a single thin-layer gel, using SDS-electrophoresis in the first dimension and isoelectric focusing in the second dimension.
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PMID:Renaturation and activity staining of glycosidases and glycosyltransferases in gels after sodium dodecyl sulfate-electrophoresis. 752 70

The phosphorylation of glucose and fructose is an important step in regulating the supply of hexose sugars for biosynthesis and metabolism. Changes in leaf hexokinase (EC 2.7.1.1) activity and in vivo metabolite levels were examined during drying in desiccation-tolerant Sporobolus stapfianus and Xerophyta viscosa. Leaf hexokinase activity was significantly induced from 85% to 29% relative water content (RWC) in S. stapfianus and from 89% to 55% RWC in X. viscosa. The increase in hexokinase corresponded to the region of sucrose accumulation in both species, with the highest activity levels coinciding with region of net glucose and fructose removal. The decline of hexose sugars and accumulation of sucrose in both plant species was not associated with a decline in acid and neutral invertase. The increase in hexokinase activity may be important to ensure that the phosphorylation and incorporation of glucose and fructose into metabolism exceeded production from potential hydrolytic activity. Total cellular glucose-6-phosphate (Glc-6-P) and fructose-6-phosphate (Fru-6-P) levels were held constant throughout dehydration. In contrast to hexokinase, fructokinase activity was unchanged during dehydration. Hexokinase activity was not fully induced in leaves of S. stapfianus dried detached from the plant, suggesting that the increase in hexokinase may be associated with the acquisition of desiccation-tolerance.
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PMID:Changes in leaf hexokinase activity and metabolite levels in response to drying in the desiccation-tolerant species Sporobolus stapfianus and Xerophyta viscosa. 1143 13

We isolated spontaneous mutants from Saccharomyces cerevisiae (baker's yeast V1) that were resistant to 2-deoxy-D-glucose and had improved fermentative capacity on sweet doughs. Three mutants could grow at the same rate as the wild type in minimal SD medium (0.17% Difco yeast nitrogen base without amino acids and ammonium sulfate, 0.5% ammonium sulfate, 2% glucose) and had stable elevated levels of maltase and/or invertase under repression conditions but lower levels in maltose-supplemented media. Two of the mutants also had high levels of phosphatase active on 2-deoxy-D-glucose-6-phosphate. Dough fermentation (CO2 liberation) by two of the mutants was faster and/or produced higher final volumes than that by the wild type, both under laboratory and industrial conditions, when the doughs were supplemented with glucose or sucrose. However, the three mutants were slower when fermenting plain doughs. Fermented sweet bakery products obtained with these mutants were of better quality than those produced by the wild type, with regard to their texture and their organoleptic properties.
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PMID:Improved properties of baker's yeast mutants resistant to 2-deoxy-D-glucose. 1152 34

Seeds of pea (Pisum sativum L.) were germinated for 5d by soaking in distilled water or 5mM cadmium nitrate. The relationships among cadmium stress, germination rate, changes in respiratory enzyme activities and carbohydrates mobilization were studied. Two cell fractions were obtained from embryonic axis: (1) mitochondria, used to determine enzyme activities of citric acid cycle and electron transport chain, and (2) soluble, to measure some enzyme activities involved in fermentation and pentose phosphate pathway. Activities of malate- and succinate-dehydrogenases (MDH, SDH) and NADH- and succinate-cytochrome c reductases (NCCR, SCCR) were rapidly inhibited, while cytochrome c oxidase (CCO) was unaltered by cadmium treatment. However, this stimulated the NADPH-generating enzyme activities of the pentose phosphate pathway, glucose-6-phosphate- and 6-phosphogluconate-dehydrogenases (G6PDH, 6PGDH), as well as enzyme activity of fermentation, alcohol dehydrogenase (ADH), with concomitant inhibition in the capacity of enzyme inactivator (INADH). Moreover, Cd restricted carbohydrate mobilization in the embryonic axis. Almost no glucose and less than 7% of control fructose and total soluble sugars were available in the embryo tissues after 5d of exposure to cadmium. Cotyledonary invertase isoenzyme activity was also inhibited by Cd. The results indicate that cadmium induces disorder in the resumption of respiration in germinating pea seeds. The contribution of Cd-stimulated alternative metabolic pathways to compensate for the failure in mitochondrial respiration is discussed in relation to the delay in seed germination and embryonic axis growth.
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PMID:Respiratory metabolism in the embryonic axis of germinating pea seed exposed to cadmium. 1876 Apr 97

Cytosolic (U-IN-2) or apoplasmic (U-IN-1) targeting of yeast invertase in potato tubers leads to a reduction in sucrose and an increase in glucose content, but specific phenotypical changes are dependent on the subcellular targeting of the enzyme. Cytosolic expression leads to a more severe phenotype with the most striking aspects being reduced starch content and increased respiration. Despite extensive research, the regulatory mechanisms leading to these changes remain obscure. Recent technological advancements regarding potato transcriptional and genomic research presented us with the opportunity to revisit these lines and perform detailed gene expression analysis, in combination with extensive metabolic profiling, to identify regulatory networks underlying the observed changes. Our results indicate that in both genotypes reduced UDP-glucose production is associated with a reduced expression of cell wall biosynthetic genes. In addition, U-IN-1 tubers are characterized by elevated expression of senescence-associated genes, coupled to reduced expression of genes related to photosynthesis and the cytoskeleton. We provide evidence that increased respiration, observed specifically in U-IN-2 tubers, might be due to sugar signaling via released trehalose-6-phosphate inhibition of the SnRK1 complex. In both genotypes, expression of the plastidic glucose-6-phosphate transporter (GPT) is significantly down-regulated. This leads to a shift in the cytosolic to plastidic glucose-6-phosphate ratio and hence might limit starch synthesis but also the oxidative pentose phosphate pathway. This might explain the observed changes in several additional plastid localized pathways, most notably reduced expression of fatty acid biosynthetic genes and an accumulation of shikimate. Interestingly, a strict negative correlation between invertase and GPT expression could be observed in a wide range of potato tubers. This reciprocal regulation may be part of a more general switch controlling energy versus storage metabolism, suggesting that the fate of assimilate utilization is coordinated at the level of sucrose degradation.
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PMID:The mode of sucrose degradation in potato tubers determines the fate of assimilate utilization. 2263 42


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