Disease relevance of Methyl alpha-D-glucopyranoside

• Active transport of glucose and alpha-methylglucoside in the cyanobacterium Plectonema boryanum [1].
• There was rapid efflux of L-leucine, L-phenylalanine, and alpha-methyl-D-glucoside after infection of Salmonella typhimurium with the clear plaque mutant C1 of phage P22 [2].
• A competitive (nonmetabolizable) inhibitor of glucose uptake, alpha-methylglucoside, was used to limit the growth of Escherichia coli [3].
• The removal of the lectin from the cells with alpha-methyl-D-glucoside 3 h after infection was followed by the immediate release of mature virus particles [4].
• Bacillus stearothermophilus reacted to pseudomonic acid-induced inhibition of isoleucine-transfer ribonucleic acid (RNA) acylation and to energy downshift caused by alpha-methylglucoside addition with accumulation of guanosine 3',5'-polyphosphates [(p)ppGpp] and restriction of RNA synthesis [5].

High impact information on Methyl alpha-D-glucopyranoside

• We show that Mlc binds specifically to membrane fractions which carry PtsG and that excess Mlc can inhibit Enzyme IICB(Glc) phosphorylation by the general PTS proteins and also Enzyme IICB(Glc)-mediated phosphorylation of alpha-methylglucoside [6].
• Equilibrium dialysis with alpha-methyl D-glucoside and subsequent Scatchard plot analysis revealed an association constant (Ka) of 1.2 X 10(3) liters/mol and a valence of 1 [7].
• TRH caused a 2-fold increase in secretion of [3H]mannose-labeled TSH glycopeptides due almost exclusively to a specific increase in structures that bound to ConA-Sepharose and eluted with 10mM alpha-methylglucoside, corresponding to biantennary complex or unusual hybrid species [8].
• Although it showed a relatively neutral pH optimum, the taurodeoxycholate-activated galactosylceramidase is not a nonlysosomal "neutral" beta-galactosidase, because unlike the latter, it was adsorbed to Concanavalin A-Sepharose after solubilization with 0.5% sodium taurodeoxycholate and was eluted by alpha-methylmannoside or alpha-methylglucoside [9].
• Consistently, the cell membrane remains intact after T1 infection: proteins, like beta-galactoside, amino acids, and alpha-methylglucoside cannot passively penetrate the membrane of T1-infected cells [10].

Chemical compound and disease context of Methyl alpha-D-glucopyranoside

• Cells of Escherichia coli ML308-225, harvested from the exponential phase, were heated in 50 mM potassium phosphate, and the loss in viability and inability to transport lactose, proline, and alpha-methylglucoside was compared [11].
• Phosphoenolpyruvate-dependent phosphorylation of alpha-methylglucoside in Streptococcus sanguis ATCC 10556 [12].
• 1. Glycerol-grown cells of Escherichia coli and its mutant uncA, treated with colicin E1 or K, exhibited a several-fold higher level of alpha-methylglucoside uptake than untreated cells [13].
• Among a total of 26 Yersinia strains isolated the following species were recognized: Y. enterocolitica, 12 strains, Y. intermedia, 5 strains, Y. frederiksenii, 2 strains, Y. kristensenii and Y. aldovae, 1 strain each; 5 were atypical Yersinia strains (rhamnose+, citrate+, alpha-methyl-D-glucoside+) [14].

Biological context of Methyl alpha-D-glucopyranoside

• In the absence of glycolytic substrates, alpha-methyl-D-glucoside stimulated Isc and oxygen consumption, although the Isc came to a steady state 50% less than when glycolytic substrates were present [15].
• 1. The effects of tricarboxylic acid cycle intermediates on the renal transport of alpha-methyl-D-glucoside and alpha-amino-isobutyric acid were examined using separated renal tubules of the rabbit [16].
• The binding activity for human 125I-labelled-somatotropin was adsorbed to a concanavalin-A-Sepharose column and was dissociated from the column with alpha-methyl-D-glucoside, suggesting that the binding protein may be a glycoprotein [17].
• Here we present evidence that lambda O degradation is energy dependent: it is impaired by cyanide and alpha-methylglucoside, both of which inhibit cellular energy metabolism [18].
• All attractants tested, including a non-metabolizable attractant (alpha-methyl-D-glucoside) stimulated methylation of the presumptive MCPs (from 1.7 to 4.3 times the level of methylation in unstimulated cells) [19].

Anatomical context of Methyl alpha-D-glucopyranoside

• 125I-Concanavalin A was found to bind to purified Golgi membranes in a manner which was time-dependent, proportional to the amount of Golgi protein, saturable, and inhibited by alpha-methyl-D-glucoside and unlabeled concanavalin A [20].
• The binding of thyroid peroxidase to Con A-agarose can be inhibited by sugars in the following order: alpha-methyl-D-mannoside greater than D-mannose greater than alpha-methyl-D-glucoside greater than D-glucose greater than D-galactose [21].
• 2. In the brush-border membrane, LS adaptation had no effect on Km for alpha-methyl-D-glucoside while Vmax values were significantly reduced in the ileum and in the rectum [22].
• 3. The route of uptake of alpha-methyl-D-glucoside into separated renal tubules is primarily across the brush border (luminal) membrane [16].
• Active transport of amino acids and the sugar, alpha-methyl-D-glucoside (alpha-MG) caused an increase in the rate of K efflux from isolated rabbit enterocytes [23].

Associations of Methyl alpha-D-glucopyranoside with other chemical compounds

• Moreover, synthetic chloropyruvate irreversibly inactivates both active transport of proline and phosphotransferase system-dependent group translocation of alpha-methylglucoside [24].
• In the GPT- mutant, alpha-methylglucoside does not inhibit adenylate cyclase and is not phosphorylated, while 2-deoxyglucose is inhibitory and phosphorylated [25].
• Subconfluent cultures of LLC-PK1 cells are unable to accumulate alpha-methyl-D-glucoside, and their transport of this glucose analog is less sensitive to phlorizin inhibition than is the transport system in confluent cultures [26].
• Electrical measurements in Xenopus oocytes revealed that alpha-methyl-D-glucoside and beta-methyl-D-glucoside are transported by the human SGLT1 transporter with similar maximal transport rates and apparent Michaelis-Menten constant values [27].
• Con-A-Sepharose affinity chromatography of the Triton X-100 placenta extract resulted in the same proportion (30%) of these two activities bound to the lectin, which were subsequently eluted in the same fractions by a linear gradient of alpha-methyl-D-glucoside [28].

Gene context of Methyl alpha-D-glucopyranoside

• ECE activity in M1 was able to bind to a concanavalin A-agarose column and was eluted by alpha-methyl-D-glucoside, indicating that the ECE is glycosylated [29].
• The third class of malK mutations resulted in resistance to the enzyme IIIGlc-mediated inhibitory effects of alpha-methylglucoside [30].
• All csm strains were sensitive to catabolite repression mediated by alpha-methylglucoside [31].
• Relipidation of fraction eluted by alpha-methyl-D-glucoside was essential to detect tissue factor activity, it was also necessary to recover full thrombomodulin activity [28].
• In a further purification step, the CSF was retained selectively by concanavalin A sepharose and eluted with alpha-methylglucoside [32].

Analytical, diagnostic and therapeutic context of Methyl alpha-D-glucopyranoside

• Oligosaccharides that bound to ConA and were eluted with alpha-methylglucoside, when analyzed by anion-exchange HPLC, consisted of species with 1 and 2 negative charges, whereas oligosaccharides that were unbound to ConA were predominantly species with three negative charges [33].
• Regardless of the previous diet fed, force-feeding the high fat, alpha-methylglucoside diet produced significantly greater sucrase and lactase activities in the upper jejunum than force-feeding the high fat diet without alpha-methylglucoside; comparable or only slightly greater sucrase and lactase activities were seen in the lower jejunum [34].
• Rats previously fed a high fat, low starch diet or a high starch low fat diet were force-fed three times over 12 h isoenergic high fat diets with or without alpha-methylglucoside, or a low fat diet containing alpha-methylglucoside [34].
• Approximately 2% of the added protein obtained as an albumin peak in DEAE-cellulose chromatography was adsorbed on and eluted with alpha-methyl-D-glucoside from the concanavalin A-Sepharose column, and resolved into three components by gel electrophoresis [35].
• The effect of dibutyryl cyclic AMP on the transport of alpha-methyl-D-glucoside and alpha-aminoisobutyric acid in separated tubules and purified brush border membranes from rabbit kidney was investigated using a rapid filtration procedure [36].

References