Biochemical and Biophysical Research Communications
A novel glycosyl-amino acid linkage: Rabbit-muscle glycogen is covalently linked to a protein via tyrosine
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2020, PeptidesCitation Excerpt :Although this fragment does not actually bind to a GPCR, it is still an interesting O-linked glycopeptide worthy of discussion. Glycogenin is a primer glycoprotein involved in glycogen biosynthesis that aquires a glucose residue through the phenolic side chain of Tyr194 via a reaction with uridine 5’’-diphospho(UDP)-glucose (Fig. 27) [128,129]. Following the addition of the first glucose residue, seven more glucose residues are added autocatalytically [130] The purpose of this work was to explore how the anomeric configuration of the carbohydrate linkage at Tyr194 influenced the ability of the fragments to undergo glucosyl transfer by recombinant glycogenin.
Starch biosynthesis in higher plants: The starch granule
2019, Comprehensive BiotechnologyUnusual glycosylation of proteins: Beyond the universal sequon and other amino acids
2017, Biochimica et Biophysica Acta - General SubjectsCitation Excerpt :It was hypothesized that biosynthesis of such Tyr O-glycosylation is controlled by GalNAc-transferases. Glycogenin, an autocatalytic protein, takes part in glycogen synthesis and auto-glycosylates Tyr194 [114–116]. The transforming protein RhoA has an atypical glycosylation of Tyr32, which is catalysed by a glycosyltransferase (PAToxA), a toxin from Photorhabdus asymbiotica.
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2015, Molecular Aspects of MedicineCitation Excerpt :Glycogenin-1 is a glycosyltransferase (EC 2.4.1.186), and catalyzes two autoglucosylation reactions using UDP-glucose as donor (Fig. 2). A glucose-O-tyrosine linkage is formed with the hydroxyl group of tyrosine 195 (Alonso et al., 1994a; Cao et al., 1993; Rodriguez and Whelan, 1985) and then several α-1,4-glucosidic linkages are formed to produce an oligosaccharide containing approximately 8–13 glucose residues (Alonso et al., 1994b; Romero et al., 2008). The priming oligosaccharide chain is used for elongation by glycogen synthase (EC 2.4.1.11) and introduction of α-1,6 branching points by branching enzyme (EC 2.4.1.18) to form glycogen (Roach, 2002).
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2012, The Biochemistry of Plants: A Comprehensive TreatiseMolecular pathogenesis of a new glycogenosis caused by a glycogenin-1 mutation
2012, Biochimica et Biophysica Acta - Molecular Basis of DiseaseCitation Excerpt :Glycogenin-1 is a glycosyltransferase (EC 2.4.1.186) catalyzing two autoglucosylation reactions using UDP-glucose as donor substrate (Fig. 1A). First, a glucose-O-tyrosine linkage is formed with the hydroxyl group of tyrosine 195 [10–14] and second, several α1,4 glucosidic linkages are formed to produce an oligosaccharide containing approximately 8–13 glucose residues [13,15,16]. The priming oligosaccharide chain is required for elongation by glycogen synthase (EC 2.4.1.11) and the introduction of α1,6 branching points by branching enzyme (EC 2.4.1.18) to produce glycogen [17].