glycosidase/dantų ėduonis

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Crystal structures of Paenibacillus polymyxa beta-glucosidase B complexes reveal the molecular basis of substrate specificity and give new insights into the catalytic machinery of family I glycosidases.

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Bacteria species involved in degradation of cellulosic substrates produce a variety of enzymes for processing related compounds along the hydrolytic pathway. Paenibacillus polymyxa encodes two homologous beta-glucosidases, BglA and BglB, presenting different quaternary structures and substrate

Dextran glucosidase: a potential target of iminosugars in caries prevention.

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It is well known that iminosugars are inhibitors of glycosyltransferases (GTFs) and glucosidases. Because of iminosugars' inhibitory effect on GTFs, scientists have made great effort to verify their roles in the prevention of caries. The inhibition of GTFs can reduce the synthesis of extracellular

Structural analysis of Saccharomyces cerevisiae alpha-galactosidase and its complexes with natural substrates reveals new insights into substrate specificity of GH27 glycosidases.

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Alpha-galactosidases catalyze the hydrolysis of terminal alpha-1,6-galactosyl units from galacto-oligosaccharides and polymeric galactomannans. The crystal structures of tetrameric Saccharomyces cerevisiae alpha-galactosidase and its complexes with the substrates melibiose and raffinose have been

Insights into the pH-dependent catalytic mechanism of Sulfolobus solfataricus β-glycosidase: A molecular dynamics study.

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Sulfolobus solfataricus β-glycosidase (SS-βGly) belongs to Glycosyl Hydrolase family1 (GH1) with broad substrate specificity. SS-βGly catalyzes both hydrolysis and transglycosylation reactions. SS-βGly is commonly used to synthesize variety of galacto-oligosaccharides. A comparison of SS-βGly with

Structural and mechanistic analyses of endo-glycoceramidase II, a membrane-associated family 5 glycosidase in the Apo and GM3 ganglioside-bound forms.

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endo-Glycoceramidase, a membrane-associated family 5 glycosidase, deviates from the typical polysaccharide substrate specificity of other soluble members of the family, preferentially hydrolyzing glycosidic linkages between the oligosaccharide and ceramide moieties of gangliosides. Here we report

Structural Insights into the Broad Substrate Specificity of a Novel Endoglycoceramidase I Belonging to a New Subfamily of GH5 Glycosidases.

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Endoglycoceramidases (EGCases) specifically hydrolyze the glycosidic linkage between the oligosaccharide and the ceramide moieties of various glycosphingolipids, and they have received substantial attention in the emerging field of glycosphingolipidology. However, the mechanism regulating the strict

Crystal structure of the beta-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus: resilience as a key factor in thermostability.

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Enzymes from hyperthermophilic organisms must operate at temperatures which rapidly denature proteins from mesophiles. The structural basis of this thermostability is still poorly understood. Towards a further understanding of hyperthermostability, we have determined the crystal structure of the

A universal fluorometric assay strategy for glycosidases based on functional carbon quantum dots: β-galactosidase activity detection in vitro and in living cells.

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The development of highly sensitive assays for glycosidases is of critical significance to understand their functions, facilely detect associated diseases and screen potential new drugs. In this work, we develop a universal assay strategy for glycosidase enzymes and inhibitor screening based on

Design of mutants for enhanced thermostability of β-glycosidase BglY from Thermus thermophilus.

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Three design strategies, based on rational and semi-rational approaches, were employed to investigate the functional impact of thermostability-related amino acid substitutions in the β-glycosidase BglY from Thermus thermophilus. Five beneficial mutations were identified, of which 1 mutation was

Origin and developmental patterns of lactase and other glycosidases in sheep amniotic and allantoic fluid.

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Intestinal lactase activity (with its associated cellobiase, 4-methylumbelliferyl-beta-galactosidase and -beta-glucosidase activities) was used as a specific intestinal marker enzyme to study the release of protein and enzymes of intestinal origin in sheep amniotic fluid during gestation. In

Physiological and serological variation in Streptococcus mitis biovar 1 from the human oral cavity during the first year of life.

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OBJECTIVE The purpose of the study was to explore the physiological and antigenic diversity of a large number of Streptococcus mitis biovar 1 isolates in order to begin to determine whether these properties contribute to species persistence. METHODS S. mitis biovar 1 was collected from four infants

Identification of pioneer viridans streptococci in the oral cavity of human neonates.

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Three hundred and sixty-seven strains of pioneer streptococci isolated from the mouths of 40 healthy, full-term infants during the first month of life were examined by two taxonomic schemes that incorporated biochemical and physiological characteristics, IgA1 protease production and glycosidase

Minority species influences microbiota formation: the role of Bifidobacterium with extracellular glycosidases in bifidus flora formation in breastfed infant guts.

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The human body houses a variety of microbial ecosystems, such as the microbiotas on the skin, in the oral cavity and in the digestive tract. The gut microbiota is one such ecosystem that contains trillions of bacteria, and it is well established that it can significantly influence host health and

Lysosomal exoglycosidases in nasal polyps.

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BACKGROUND Nasal polyps are smooth outgrowths assuming a shape of grapes, formed from the nasal mucosa, limiting air flow by projecting into a lumen of a nasal cavity. Up to now the surgical resection is the best method of their treatment, but etiology and pathogenesis of the nasal polyps is not yet

Inhibition of rabbit muscle glycogen phosphorylase by D-gluconohydroximo-1,5-lactone-N-phenylurethane.

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The effect of the beta-glycosidase inhibitor D-gluconohydroximo-1,5-lactone-N-phenylurethane (PUG) on the kinetic and ultracentrifugation properties of glycogen phosphorylase has been studied. Recent crystallographic work at 2.4 A resolution [D. Barford et al. (1988) Biochemistry 27, 6733-6741] has

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