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cellobiose/zubný kaz
Odkaz sa uloží do schránky
Strana 1 od 21 výsledky
Diverse substrate recognition mechanism revealed by Thermotoga maritima Cel5A structures in complex with cellotetraose, cellobiose and mannotriose.
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The hyperthermophilic endoglucanase Cel5A from Thermotoga maritima can find applications in lignocellulosic biofuel production, because it catalyzes the hydrolysis of glucan- and mannan-based polysaccharides. Here, we report the crystal structures in apo-form and in complex with three ligands,
Potential physiological functions of acceptor products of dextransucrase with cellobiose as an inhibitor of mutansucrase and fungal cell synthase.
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A series of oligosaccharides (cellobio-oligosaccharides) ranging from degrees of polymer 3 to 6 were synthesized by Leuconostoc mesenteroides B-512 FMCM in the presence of cellobiose. The major oligosaccharides were the trisaccharides, α-D-glucopyranosyl-(1 → 2)-β-D-glucopyranosyl-(1 →
Prevotella fusca sp. nov. and Prevotella scopos sp. nov., isolated from the human oral cavity.
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Two strains of anaerobic, Gram-negative bacilli isolated from the human oral cavity were subjected to a comprehensive range of phenotypic and genotypic tests and were found to belong to two separate taxa. Phylogenetic analysis of full-length 16S rRNA gene sequences showed that the strains were both
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
The structure of enzyme IIAlactose from Lactococcus lactis reveals a new fold and points to possible interactions of a multicomponent system.
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BACKGROUND
The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) is responsible for the binding, transmembrane transport and phosphorylation of numerous sugar substrates. The system is also involved in the regulation of a variety of metabolic and transcriptional processes. The PTS
Structural basis of increased resistance to thermal denaturation induced by single amino acid substitution in the sequence of beta-glucosidase A from Bacillus polymyxa.
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The increasing development of the biotechnology industry demands the design of enzymes suitable to be used in conditions that often require broad resistance against adverse conditions. beta-glucosidase A from Bacillus polymyxa is an interesting model for studies of protein engineering. This is a
Prevotella multiformis sp. nov., isolated from human subgingival plaque.
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Four bacterial strains isolated from the human oral cavity, PPPA19, PPPA21(T), PPPA28 and PPPA30, were characterized by determining phenotypic and biochemical features, cellular fatty acid profiles and the phylogenetic position based on 16S rRNA gene sequence analysis. 16S rRNA gene sequence
Crystal structures of phosphotransferase system enzymes PtxB (IIB(Asc)) and PtxA (IIA(Asc)) from Streptococcus mutans.
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Streptococcus mutans is the primary etiological agent of dental caries in man and other mammalian organisms. This bacterium metabolizes carbohydrates actively and thrives under anaerobic conditions by fermenting l-ascorbate (Asc) via the sga operon, which includes SgaT, PtxB, and PtxA. These three
Crystal structure of beta-glucosidase A from Bacillus polymyxa: insights into the catalytic activity in family 1 glycosyl hydrolases.
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Family 1 glycosyl hydrolases are a very relevant group of enzymes because of the diversity of biological roles in which they are involved, and their generalized occurrence in all sorts of living organisms. The biological plasticity of these enzymes is a consequence of the variety of beta-glycosidic
Molecular details of ligand selectivity determinants in a promiscuous β-glucan periplasmic binding protein.
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BACKGROUND
Members of the periplasmic binding protein (PBP) superfamily utilize a highly conserved inter-domain ligand binding site that adapts to specifically bind a chemically diverse range of ligands. This paradigm of PBP ligand binding specificity was recently altered when the structure of the
Electrospray ionization mass spectrometry studies of cyclodextrin-carboxylate ion inclusion complexes.
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Aqueous solutions containing simple model aliphatic and alicyclic carboxylic acids (surrogates 1-4) were studied using negative ion electrospray mass spectrometry (ESI-MS) in the presence and absence of alpha-, beta-, and gamma-cyclodextrin. Molecular ions were detected corresponding to the parent
Preferred Hexoses Influence Long-Term Memory in and Induction of Lactose Catabolism by Streptococcus mutans.
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Bacteria prioritize sugar metabolism via carbohydrate catabolite repression, which regulates global gene expression to optimize the catabolism of preferred substrates. Here, we report an unusual long-term memory effect in certain Streptococcus mutans strains that alters adaptation to growth on
Characterization of sugar receptor expression by neoglycoproteins in oral and oropharyngeal squamous cell carcinomas.
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Recognition of the carbohydrate part of cellular glycoconjugates by sugar receptors like lectins may contribute to biosignaling and interactions between normal and transformed cells. Such recognitions may be essential for establishing phenotypic characteristics in neoplastic cells, including
Investigation of disaccharide recognition by molecularly imprinted polymers.
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The selectivity of carbohydrate-imprinted polymers for several disaccharides, namely cellobiose, maltose, lactose and gentiobiose, is investigated. An ternary ligand-Cu(II)-carbohydrate complex was formed in alkaline solution and captured afterwards in the polymer. The accessibility of the polymer
Directed Evolution of Clostridium thermocellum β-Glucosidase A Towards Enhanced Thermostability.
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β-Glucosidases are key enzymes in the process of cellulose utilization. It is the last enzyme in the cellulose hydrolysis chain, which converts cellobiose to glucose. Since cellobiose is known to have a feedback inhibitory effect on a variety of cellulases, β-glucosidase can prevent this inhibition
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