Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.20 (alpha-glucosidase)
 4,237 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The mechanism of starch degradation by the fungus Trichoderma viride was studied in strain CBS 354.44, which utilizes glucose, starch and dextrins but is unable to assimilate maltose. It was shown that the amylolytic enzyme system is completely extracellular, equally well induced by starch, amylose or amylopectin and that it consists mainly of enzymes of the glucoamylase type which yield glucose as the main product of starch hydrolysis. Small amounts of alpha-amylase are produced also. The enzymes produced in starch cultures degrade starch, amylose and amylopectin equally well. Enzyme synthesis in starch media takes place to a considerable extent after exhaustion of the carbon source when maximum growth has been attained. Low-molecular dextrins are degraded by extracellular enzymes of the glucoamylase type. These enzymes are produced in media containing starch or dextrins. Maltotriose is consumed for only one third leaving maltose in the culture filtrate. Maltose is hardly attacked and hardly induces any amylolytic enzyme activity. No stable alpha-glucosidase appears to be produced.
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PMID:Starch degradation by the mould Trichoderma viride. I. The mechanism of starch degradation. 1 Aug 32

An assay for alpha-1,4-glucosidase (acid maltase) activity which is deficient in Pompe's disease is described. The assay can be used to measure the enzyme in cultured skin fibroblasts, cultured amniotic cells and peripheral blood leucocytes. [U-14 C]Maltose is used as the substrate in a total assay volume of 8 microliter. The product, [U-14C]glucose, is separated from the substrate by cellulose thin-layer chromatography. The procedure permits replicate assays from 400 microliter whole blood and from amniotic cells in primary culture. Discrimination of the heterozygous Pompe state appears to be facilitated.
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PMID:A micro-radiochemical assay for alpha-1,4-glucosidase and its use in the assessment of type II glycogenosis (Pompe's disease). 1 94

[14C]Glucose taken up by Epidinium ecaudatum caudatum was found in the pool, in the protozoal polysaccharide and in the bacteria associated with the protozoa. The amount incorporated into the polysaccharide depended on the square of the glucose concentration. Evidence was obtained that glucose was probably taken up initially into the pool unchanged, and then rapidly converted into glucose 6-phosphate and maltose which were subsequently hydrolysed to glucose. [14C]-Maltose was taken up at 20 to 30% of the rate of [14C]glucose, with 14C appearing initially in maltose and glucose 6-phosphate. 14C from 14C-labelled soluble starch appeared in the pool as maltose, glucose 6-phosphate and glucose in that order, but incorporation into protozoal polysaccaride was poor. Hexokinase, phosphoglucomutase, alpha-glucan and maltose phosphorylases, glucose 6-phosphatase and maltase activities were found in the protozoa.
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PMID:The uptake and metabolism of glucose, maltose and starch by the rumen ciliate Epidinium ecaudatum caudatum. 18 7

The organism Bacillus amyloliquefaciens is capable of producing alpha-amylase (1,4-alpha-D-glucan glucanohydrolase, EC 3.2.1.1) and isoamylase (glycogen 6-glucanohydrolase, EC 3.2.1.68) extracellurlarly and a membrane-bound, intracellular alpha-glucosidase (alpha-D-glucoside glucohydrolase, EC 3.2.1.20). The amounts of alpha-glucosidase in cells of B. amyloliquefaciens grown on amylaceous polysaccharides were significantly higher then in cells grown on non-carbohydrate carbon sources. alpha-Glucosidase was exclusively found associated with membranes from ruptured spheroplasts by subcellular fractionation and solubilization studies. Salt solutions and chelating agents alone did not dislodge alpha-glucosidase from membranes, but in combination with detergents were most effective in solubilizing active enzyme (0.1% sodium cholate (pH 8.0)/0.4 M sodium chloride). Purified alpha-glucosidase very rapidly hydrolized p-nitrophenyl alpha-D-glucopyranoside and sucrose. Maltose, maltotriose, isomaltose and isomaltotriose were hydrolized at slower rates, whereas beta-glucosides and polymeric alpha-glucans were not attacked. Other properties of the purified enzyme were as follows: Temperature optimum for catalysis = 39 +/- 1 degrees C; pH optimum = 6.8; molecular weight = 27,000 +/- 1000. alpha-Glucosidase is proposed to function in the endogenous metabolism of alpha-glucans provided extracellularly as carbon sources for growth of B. amyloliquefaciens.
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PMID:alpha-Glucosidase, a membrane-bound enzyme of alpha-glucan metabolism in Bacillus amyloliquefaciens. Purification and partial characterization. 33 55

Maltose fermentation in Saccharomyces yeasts requires one of five unlinked MAL loci: MAL1, 2, 3, 4, or 6. Each locus consists of three genes encoding maltose permease, maltase and the MAL activator. At MAL6 the genes are called MAL61, MAL62 and MAL63, respectively. Transcription of MAL61 and MAL62 is coordinately induced by maltose and repressed by glucose and this regulation is mediated by the MAL activator. By deletion analysis of the MAL61-MAL62 intergenic region, we show that a 68-basepair region, from base pairs -515 to -582 upstream of the MAL61 start codon, contains a sequence necessary for the maltose-induced expression of MAL61 and MAL62, the UAS(MAL). This sequence contains two copies of an 11-basepair dyad which may be the active elements of the UAS(MAL). Using heterologous gene plasmid constructs, we demonstrate that the UAS(MAL) sequence is sufficient for maltose inducibility of MAL62 and that this regulated expression requires a functional MAL activator. Our results suggest that the MAL61-MAL62 intergenic region contains additional distinct elements which function to precisely regulate MAL61 and/or MAL62 expression. Among these are repressing sequences, including a glucose-responsive element located between base pairs -583 and -638, which is partially responsible for mediating glucose-repression of MAL62 expression.
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PMID:The UAS(MAL) is a bidirectional promotor element required for the expression of both the MAL61 and MAL62 genes of the Saccharomyces MAL6 locus. 152 71

Maltose fermentation in Saccharomyces species requires the presence of at least one of five unlinked MAL loci: MAL1, MAL2, MAL3, MAL4 and MAL6. Each MAL locus is complex consisting of at least three genes: a trans-acting activator, a maltose permease, and maltase. All the MAL loci show homology to each other both at the sequence level as determined by Southern transfer analysis and at the functional level as determined by complementation. We describe the organization of the MAL loci in yeast and the basic features of their regulation. The analysis of MAL has contributed to our understanding of the evolution of multigenic families, the global integration of carbohydrate metabolism, and gene regulation.
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PMID:Control of maltase synthesis in yeast. 176 81

When Saccharomyces cerevisiae CBS 8066 was grown under maltose limitation, two enzymes specific for maltose utilization were present: a maltose carrier, and the maltose-hydrolysing alpha-glucosidase. The role of these two enzymes in the physiology of S. cerevisiae was investigated in a comparative study in which Candida utilis CBS 621 was used as a reference organism. Maltose pulses to a maltose-limited chemostat culture of S. cerevisiae resulted in 'substrate-accelerated death'. This was evident from: (1) enhanced protein release from cells; (2) excretion of glucose into the medium; (3) decreased viability. These effects wee specific with respect to both substrate and organism: pulses of glucose to maltose-limited cultures of S. cerevisiae did not result in cell death, neither did maltose pulses to maltose-limited cultures of C. utilis. The maltose-accelerated death of s. cerevisiae is most likely explained in terms of an uncontrolled uptake of maltose into the cell, resulting in an osmotic burst. Our results also provide evidence that the aerobic alcoholic fermentation that occurs after pulsing sugars to sugar-limited cultures of s. cerevisiae (short-term Crabtree effect) cannot solely be explained in terms of the mechanism of sugar transport. Both glucose and maltose pulses to maltose-limited cultures triggered aerobic alcohol formation. However, glucose transport by S. cerevisiae occurs via facilitated diffusion, whereas maltose entry into this yeast is mediated by a maltose/proton symport system.
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PMID:Substrate-accelerated death of Saccharomyces cerevisiae CBS 8066 under maltose stress. 218 22

Maltose fermentation in Saccharomyces species requires the presence of at least one of five unlinked MAL loci: MAL1, MAL2, MAL3, MAL4, and MAL6. Each of these loci consists of a complex of genes involved in maltose metabolism; the complex includes maltase, a maltose permease, and an activator of these genes. At the MAL6 locus, the activator is encoded by the MAL63 gene. While the MAL6 locus has been the subject of numerous studies, the binding sites of the MAL63 activator have not been determined. In this study, we used Escherichia coli extracts containing the MAL63 protein to define the binding sites of the MAL63 protein in the divergently transcribed MAL61-62 promotor. When a DNA fragment containing these sites was placed upstream of a CYC1-lacZ gene, maltose induced beta-galactosidase. These sites therefore constitute an upstream activating sequence for the MAL genes.
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PMID:Identification of the upstream activating sequence of MAL and the binding sites for the MAL63 activator of Saccharomyces cerevisiae. 219 62

We investigated the effects of pectin, a soluble dietary fiber, on functional and morphological parameters of the small intestine in rats. A control group and a pectin-fed group were given a fiber-free elemental liquid diet and an elemental liquid diet containing 2.5% (w/w) pectin, respectively, for 2 weeks. The ileal mucosal specific activities of maltase, sucrase and alkaline phosphatase increased significantly in the pectin-fed group. Maltose absorption of the ileum, studied in vitro by the method of everted sacs and disaccharide-dependent potential difference, increased significantly in the pectin-fed group. The length of the small intestine as well as the villus height and crypt depth of both the jejunum and the ileum were significantly greater in the pectin-fed group. The crypt cell production rate of the jejunum and the ileum was also significantly greater in the pectin-fed group. Plasma enteroglucagon, but not gastrin, increased significantly in the pectin-fed group. These data suggest that pectin feeding results in hyperplasia of the small-intestinal mucosa and a significant increase in the enzyme activities of the brush border membrane of the ileum.
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PMID:Effect of pectin, a soluble dietary fiber, on functional and morphological parameters of the small intestine in rats. 254 93

Starch is the main carbohydrate in the food of poultry. Starch granules are digested by pancreatic alpha-amylase in the small intestine. Intestinal villi have enterocytes that project microvilli with a fibrous glycocalyx from the surface. These fine structures are envisaged to entrap water that is mixed with mucin from nearby goblet cells to form the "unstirred water layer." Maltose, maltotriose and alpha-limit dextrins must diffuse across this first barrier to absorption to be hydrolyzed by maltase and sucrase-isomaltase immobilized at the membrane; however, the resultant glucose, once formed, accrues at the surface to provide a concentration advantage. Fowl adjust to changes in dietary starch by altering the amount of amylase released, intestinal surface area and enterocyte carbohydrase concentration. Enterocytes arising during embryonic development have no carbohydrases and are not involved with glucose absorption, but they appear to be specialized for maternal immunoglobin transfer in ovo. Embryonic villi are stimulated by transfer activity, and their growth depends on enterocytes arising from the crypt. Mature crypt cells are capable of digestion-absorptive activities and dominate the villus shortly after the chick hatches when yolk sac reserves are depleted.
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PMID:Digestion and absorption of carbohydrates in fowl and events through perinatal development. 258 3


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