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Exploring genomes for glycosyltransferases

Molecular BioSystems, 2010
Abstract 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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Affinity chromatography of glycosyltransferases

Journal of Chromatography A, 1981
This 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, 2016
Glycosyltransferases (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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Comparative aspects of glycosyltransferases

Biochemical Society Symposia, 2002
Glycosyltransferases, 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. Despite the fact that many glycosyltransferases recognize similar donor or acceptor substrates, there is surprisingly limited sequence identity ...
Breton, C.   +4 more
openaire   +2 more sources

Mechanisms of Glycosyltransferases: The In and the Out

ChemBioChem, 2011
Getting 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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Collagen Glycosyltransferases

1979
K I, Kivirikko, R, Myllylä
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