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)

Larval and adult Psacothea hilaris feed on mulberry wood and leaves, respectively. High levels of endogenous activity against the major dietary carbohydrates, cellulose, hemicellulose, starch and soluble sugars were secreted in the gut of larvae and adults. Activity against pectin was also high and multiple polygalacturonase (EC 3.2.1.15) components were secreted in the gut of larvae. One glycanase component, beta-EG1, which was primarily an endo-beta-1,4-glucanase (EC 3.2.1.4) and another, beta-EG2, which was mostly an endo-beta-1,4-xylanase (EC 3.2.1.8), were also secreted, while at least four additional components hydrolysed laminarin, lichenin and crystalline cellulose. The beta-glycosidase component beta-GD1 was associated with most of the beta-mannosidase (EC 3.2.1.25) and beta-xylosidase (EC 3.2.1.37) activity secreted in the gut of larvae, while another, beta-GD2, was a beta-glucosidase (EC 3.2.1.21), the activity of which was directed against cellobiose and other beta-linked disaccharides, and a beta-fucosidase (EC 3.2.1.38). A beta-galactosidase (EC 3.2.1.23), which did not hydrolyse lactose, was also secreted, as were distinct beta-N-acetylhexosaminidase (EC 3.2.1.52), trehalase (EC 3.2.1.28), alpha-L-arabinosidase (EC 3.2.1.55), alpha-galactosidase (EC 3.2.1.22) and a minimum of four alpha-glucosidase (EC 3.2.1.20) components, one of which was also likely to be associated with a peak of alpha-mannosidase (EC 3.2.1.24) activity. The alpha-glucosidase components varied in their specificity for alpha-linked disaccharides, but none was active against sucrose, which was hydrolysed by a beta-fructofuranosidase (EC 3.2.1.26) component. Overall average levels of activity in larvae were twice those of adults, but the secretion of individual carbohydrases in both was not regulated in response to the relative abundance of particular carbohydrate components in their respective diets.
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PMID:Diet and carbohydrate digestion in the yellow-spotted longicorn beetle Psacothea hilaris. 1277 Apr 76

Activities of seven acid glycosidases: beta-N-acetylhexosaminidase (beta-HEX), alpha- and beta-galactosidase (alpha- and beta-GAL), alpha- and beta-mannosidase (alpha- and beta-MAN), alpha-glucosidase and alpha-fucosidase in magnum region of hen (Gallus gallus domesticus) oviduct, and four acid glycosidases: beta-HEX, beta-GAL, alpha- and beta-MAN in egg albumen, were investigated. beta-HEX from magnum and egg albumen hydrolysed 4-methylumbelliferyl-beta-N-acetylhexosamine-6-sulphate (4-MeUmbGlcNAc-6-SO(4)) like mammalian beta-HEX form A. Multiple forms of magnum and egg albumen beta-HEX, beta-GAL, alpha- and beta-MAN were separated by strong anion exchange chromatography and chromatofocusing method. Chromatofocusing of the magnum resulted in the appearance of multiple forms for beta-HEX with pI of 6.18, 5.43, 5.55, 5.34, 5.27 and 5.16, for beta-GAL with pI of 4.98, 4.84, 4.77, 4.64 and 4.68-4.63, for alpha-MAN with pI of >or=7.4, 6.75, 6.62 and 6.26, and for beta-MAN two forms with pI of 6.37 and 5.77. Chromatofocusing of egg albumen yields multiple forms for beta-HEX with pI of 6.24, 6.08, 5.55 and 5.35, for beta-GAL two forms with pI of 5.10 and 4.86-4.80 for alpha-MAN multiple forms with pI of >or=7.4, 6.80, 6.60 and 6.30, and for beta-MAN forms with pI of 6.30 and 5.77. In conclusion, this study was the first to show beta-HEX activity against 4-MeUmbGlcNAc-6-SO(4) in the magnum and albumen of bird eggs, corresponding to beta-HEX A activity in mammals. Main multiple forms of beta-HEX, beta-GAL, alpha- and beta-MAN occurring in the magnum were revealed in the egg albumen. Comparison with a cock of the same breed showed that hen egg magnum and albumen has the same multiple forms of the enzymes that are found in the epididymides and seminal plasma of the cock.
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PMID:Acid glycosidases from hen oviduct and egg albumen. 1623 36

The cell surface of Candida albicans is enriched in highly glycosylated mannoproteins that are involved in the interaction with the host tissues. N glycosylation is a posttranslational modification that is initiated in the endoplasmic reticulum (ER), where the Glc(3)Man(9)GlcNAc(2) N-glycan is processed by alpha-glucosidases I and II and alpha1,2-mannosidase to generate Man(8)GlcNAc(2). This N-oligosaccharide is then elaborated in the Golgi to form N-glycans with highly branched outer chains rich in mannose. In Saccharomyces cerevisiae, CWH41, ROT2, and MNS1 encode for alpha-glucosidase I, alpha-glucosidase II catalytic subunit, and alpha1,2-mannosidase, respectively. We disrupted the C. albicans CWH41, ROT2, and MNS1 homologs to determine the importance of N-oligosaccharide processing on the N-glycan outer-chain elongation and the host-fungus interaction. Yeast cells of Cacwh41Delta, Carot2Delta, and Camns1Delta null mutants tended to aggregate, displayed reduced growth rates, had a lower content of cell wall phosphomannan and other changes in cell wall composition, underglycosylated beta-N-acetylhexosaminidase, and had a constitutively activated PKC-Mkc1 cell wall integrity pathway. They were also attenuated in virulence in a murine model of systemic infection and stimulated an altered pro- and anti-inflammatory cytokine profile from human monocytes. Therefore, N-oligosaccharide processing by ER glycosidases is required for cell wall integrity and for host-fungus interactions.
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PMID:Endoplasmic reticulum alpha-glycosidases of Candida albicans are required for N glycosylation, cell wall integrity, and normal host-fungus interaction. 1793 9


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