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)

Enzymatic activity was measured on two beaches of the Ligurian Sea (NW Mediterranean) during late spring and summer 2003. The detected activities (leucine aminopeptidase, beta-glucosidase, alpha-glucosidase, and beta-N-acetylglucosaminidase) were related to the available organic substrates (proteins and carbohydrates) and to the bacterial community (expressed in terms of abundance, biomass, and frequency of cell division). The very low chlorophyll a concentrations (never higher than 40 ng g(-1)) suggested that heterotrophic microorganisms play a major role in the beach ecosystem. Enzymatic activities devoted to organic matter degradation were lower in the emerged part of the beaches and higher in the sites covered, permanently or temporarily, by seawater, suggesting that sea action enlivens the degradation processes. Leucine aminopeptidase ranged from 0.26 to 13.02 nmol g(-1)h(-1), and beta-glucosidase (the most expressed glycolytic enzyme) from 0.03 to 4.51 nmol g(-1)h(-1). Strong changes in the proteolytic/glycolytic activity ratio were observed, with a sudden rise in glycolysis during summer, leading to ratio values from about 30 down to 1. Thus, beaches were identified as preferential degradation sites, where very refractory compounds such as cellulose may also be efficiently processed.
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PMID:Enzymatic activity on sandy beaches of the Ligurian Sea (NW Mediterranean). 1605 75

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

A novel 5-membered iminocyclitol derivative was found to be a potent and selective inhibitor of the glycoprotein-processing alpha-glucosidase with a Ki value of 53 nM. This compound was further derivatized to antiviral agents against Japanese encephalitis virus, dengue virus serotype 2 (DEN-2), human SARS coronavirus, and human beta-hexosaminidase (Ki = 2.6 nM), a new target for the development of osteoarthritis therapeutics.
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PMID:Novel five-membered iminocyclitol derivatives as selective and potent glycosidase inhibitors: new structures for antivirals and osteoarthritis. 1639 76

Specific activities of seven acid glycosidases: beta-hexosaminidase, alpha- and beta-galactosidase, alpha- and beta-mannosidase, alpha-glucosidase and alpha-fucosidase were determined in various parts of the domestic hen oviduct (infundibulum, isthmus, shell gland and vagina). The activity of most enzymes was the highest in the isthmus. Multiple forms of all acid glycosidases from the isthmus were separated by strong anion exchange chromatography at pH 6.0. The isoelectric points of the isthmus forms of beta-hexosaminidase, beta-galactosidase and alpha- and beta-mannosidase were determined by chromatofocusing. For the first time the high beta-galactosidase activity was found in hen egg shell membranes.
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PMID:Acid glycosidases in the isthmus of the hen oviduct and egg shell membranes. 1722 Sep 42

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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