Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.21 (beta-glucosidase)
 3,280 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Vibrio mimicus is the closest organism to Vibrio cholerae. V. mimicus E-33, which is a highly adhesive and enteropathogenic strain, is known to produce three types of hemagglutinins (HAs), i.e., a 31-kDa exocellular metalloprotease (Vm-HA/protease), lipopolysaccharide (Vm-LPSHA), and a 39-kDa major outer membrane protein (Vm-OMPHA). Hemagglutination induced by Vm-LPSHA and Vm-OMPHA was inhibited by glycoproteins, including mucin, fetuin, and asialofetuin, but not by monosaccharides, disaccharides, or N-acetylated saccharides. The inhibitory potential of each glycoprotein for Vm-OMPHA was greatly augmented by treatment with a glycolytic enzyme such as beta-D-galactosidase or beta-D-glucosidase, while pronase treatment achieved complete abolition of the inhibitory potential. The inhibitory ability of the glycoproteins for Vm-LPSHA was also abolished by pronase treatment; however, glycolytic enzyme treatment showed no effect. Hence, the polypeptide portion of glycoproteins may directly associate with Vm-OMPHA and Vm-LPSHA, but the sugar moiety may act as a barrier to interaction with Vm-OMPHA. The glycoproteins as well as Fab antibodies against Vm-OMPHA and Vm-LPSHA eliminated the ability of E-33 cells to agglutinate rabbit erythrocytes and to attach to rabbit intestinal mucosa. Additionally, expression of the hemagglutinating ability by the bacterial cells was accompanied by efficient bacterial adherence to the intestinal mucosa. Finally, the hemagglutinating activity of Vm-OMPHA was markedly increased by incubation with Vm-HA/protease. These results indicate that all three HAs may have significant roles in the glycoprotein-mediated intestinal adherence of V. mimicus E-33.
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PMID:Vibrio mimicus attaches to the intestinal mucosa by outer membrane hemagglutinins specific to polypeptide moieties of glycoproteins. 928 34

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

The sand fly Phlebotomus papatasi Scopoli, 1786, the vector of Leishmania major Yakimoff et Schokhor, 1914, is found in desert areas where sugars are scarce but also in habitats that abound in sugar sources. The sand flies require sugar meals from plant sources for their energy requirements and to hydrolyze these complex sugars, they need a repertoire of glycosidases. We presumed that there are differences in the levels of glycosidase activities in flies from such habitats and also assumed that they may be instrumental in modulating the flies' susceptibility to L. major infections. Phlebotomus papatasi originating from diverse ecological habitats ranging from an oasis to desert sites were colonized. They were analyzed for weight changes and glycosidase activities before and after feeding on 1M sucrose solution. Oasis flies were smaller than desert flies but took larger sugar meals. Homogenates of these flies hydrolyzed 16 synthetic and 2 natural glycoside substrates to varying degrees. The arid-region flies tended to produce more glycosidase activity than those originating in sugar-rich environments, especially sucrase, alpha- and beta-glucosidase, aalpha-fucosidase, alpha-mannosidase, and alpha- and beta-N-acetylgalactosaminidase. However, chitinolytic enzyme activities and particularly the beta-N-acetylhexosaminidase activity of oasis flies were higher than other flies tested. In comparing the desert flies, there were also significant differences in glycolytic enzyme activities between the spring-line (flowering season) of flies and the autumn-line (end of dry season) flies. A range of saccharide inhibitors was tested to demonstrate the specificity of the enzymes.
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PMID:Glycolytic and chitinolytic activities of Phlebotomus papatasi (Diptera: Psychodidae) from diverse ecological habitats. 1830 72