Results 251 to 260 of about 38,132 (292)
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Glycosyltransferase structure and mechanism
Current Opinion in Structural Biology, 2000The high-resolution X-ray crystal structures of a new form of bacteriophage T4 beta-glucosyltransferase, Escherichia coli MurG, Bacillus subtilis SpsA, bovine beta-1,4-galactosyltransferase 1 and rabbit N-acetylglucosaminyltransferase I have now been solved.
U M, Unligil, J M, Rini
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Exploring genomes for glycosyltransferases
Molecular BioSystems, 2010Abstract Glycosyltransferases are one of the largest and most diverse enzymegroups in Nature. They catalyse the synthesis of glycosidic linkages by the transfer of a sugar residue from a donor to an acceptor substrate. These enzymes have been classified into families on the basis of amino acid sequence similarity that are kept updated
Fasmer Hansen, Sara +4 more
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Engineering of glycosidases and glycosyltransferases
Current Opinion in Chemical Biology, 2006In recent years, substantial advances have been made in the engineering of glycosidases and glycosyltransferases for the synthesis and degradation of glycan structures. Key developments include improvement of the thermostability of xylanase through comprehensive saturation mutagenesis, creation of the first glycosynthase derived from an inverting ...
Susan M, Hancock +2 more
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Molecular Modeling of Glycosyltransferases
2006Glycosyltransferases, the enzymes that build oligosaccharides and glycoconjugates, have received much interest in recent years owing to their biological functions and their potential uses in biotechnology. The analysis of the wealth of sequences that are now available in databases allowed the classification in different families characterized by ...
Imberty, A. +3 more
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Affinity chromatography of glycosyltransferases
Journal of Chromatography A, 1981This review summarizes the use of biospecific chromatography techniques in the purification of mammalian glycosyltransferases. Ligands that are analogues of donor or acceptor substrates have been linked to cyanogen bromide-activated agarose for use as affinity adsorbents.
J E, Sadler, T A, Beyer, R L, Hill
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The conformational plasticity of glycosyltransferases
Current Opinion in Structural Biology, 2016Glycosyltransferases (GTs) catalyze the transfer of a sugar moiety from nucleotide-sugar or lipid-phospho-sugar donors to a broad range of acceptor substrates, generating a significant amount of structural diversity in biological systems. GTs are highly selective in nature, allowing the recognition of subtle structural differences in the sequences and ...
David Albesa-Jové, Marcelo E Guerin
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Photoaffinity labelling of glycosyltransferases
Glycobiology, 1992The photoaffinity analogues 5-azido-UDP-glucose and 5-azido-UDP-glucuronic acid have proven to be valuable biochemical tools in the studies of nucleoside diphosphate sugar-utilizing enzymes, especially membrane-associated glycosyltransferases. A summary of the past and current uses of these analogues is presented, as well as photoaffinity data for the ...
R R, Drake, A D, Elbein
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Glycosyltransferases in SWISS-PROT
Glycoconjugate Journal, 1998SWISS-PROT is a curated protein sequence database with a high level of annotation (such as description of the function of a protein, its domain structure, post-translational modification, variants, etc), a minimal level of redundancy and a high level of integration with other databases.
C, O'Donovan, N, Mitaritonna
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Mechanisms of Glycosyltransferases: The In and the Out
ChemBioChem, 2011Getting into a transition state: Glycosyltransferases retain a critical role in glycobiology. The design of potent glycosyltransferase inhibitors may be facilitated by considering the mechanistic evidence presented by Davies and Davis and co-workers that strengthens the case that retaining glycosyltransferases function through a single front-side, S(N ...
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Activity Determination of Glycosyltransferases
2019The unique chemistry of 2-aminobenzoic acid (2-AA, anthranilic acid, AA) for labeling glycans in aqueous buffer solutions was crucial in developing the assays for measuring the activity of transferases (Anumula, Anal Biochem 457:31-37, 2014).
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