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The most recent review of oligosaccharyltransferase, including a summary of mechanistic studies. of special interest
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Silberstein S, Gilmore R. Biochemistry, molecular biology, and genetics of the oligosaccharyltransferase. FASEB J. 10:1996;849-858 The most recent review of oligosaccharyltransferase, including a summary of mechanistic studies. of special interest.
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Bause E, Breuer W, Peters S. Investigation of the active site of oligosaccharyltransferase from pig liver using synthetic tripeptides as tools. Biochem J. 312:1995;979-985.
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Synthesis and evaluation of synthetic analogues of dolichyl-P-P-chitobiose as oligosaccharyltransferase substrates
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Fang X, Gibbs BS, Coward JK. Synthesis and evaluation of synthetic analogues of dolichyl-P-P-chitobiose as oligosaccharyltransferase substrates. Bioorg Med Chem Lett. 5:1995;2701-2706.
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0030656964
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Efficient enzymatic synthesis of the core trisaccharide of N-glycans using a recombinant β-mannosyltransferase
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Watt GM, Revers L, Webberley MC, Wilson IBH, Flitsch SL. Efficient enzymatic synthesis of the core trisaccharide of N-glycans using a recombinant β-mannosyltransferase. Int Ed Angew Chem. 36:1997;. in press.
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Enzymatic glycoprotein synthesis: Preparation of ribonuclease glycoforms via enzymatic glycopeptide condensation and glycosylation
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The synthesis of a novel glycoprotein is described utilising purified glycosyltransferases and a peptide ligase. It is shown that glycosyltransferases can recognize unnatural glycoprotein acceptors and that glycopeptides can be ligated under thermodynamic conditions to give full length proteins. of outstanding interest
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Witte K, Sears P, Martin R, Wong C-H. Enzymatic glycoprotein synthesis: preparation of ribonuclease glycoforms via enzymatic glycopeptide condensation and glycosylation. J Am Chem Soc. 119:1997;2114-2118 The synthesis of a novel glycoprotein is described utilising purified glycosyltransferases and a peptide ligase. It is shown that glycosyltransferases can recognize unnatural glycoprotein acceptors and that glycopeptides can be ligated under thermodynamic conditions to give full length proteins. of outstanding interest.
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Firefly luciferase: Alteration of the color of emitted light resulting from substitutions at position 286
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The first example of the site-specific incorporation of a glycosylated amino acid into a protein via the techniques of unnatural amino acid mutagenesis and in vitro translation. of outstanding interest
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Mamaev SV, Laikhter AL, Arslan T, Hecht SM. Firefly luciferase: alteration of the color of emitted light resulting from substitutions at position 286. J Am Chem Soc. 118:1996;7243-7244 The first example of the site-specific incorporation of a glycosylated amino acid into a protein via the techniques of unnatural amino acid mutagenesis and in vitro translation. of outstanding interest.
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Recombinant whole cells as catalysts for the enzymatic synthesis of oligosaccharides and glycopeptides
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Herrmann GF, Wang P, Shen G-J, Wong C-H. Recombinant whole cells as catalysts for the enzymatic synthesis of oligosaccharides and glycopeptides. Int Ed Angew Chem. 33:1994;1241-1242.
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Borsig L, Ivanox SX, Herrmann GF, Kragl U, Wandrey C, Berger EG. Scaled-up expression of human α2,6(N)sialyltransferase in Saccharomyces cerevisiae. Biochem Biophys Res Commun. 210:1995;14-20.
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Herrmann GF, Elling L, Krezdorn CH, Kleene R, Berger EG, Wandrey C. Use of transformed whole yeast cells expressing β-1,4-galactosyltransferase for the synthesis of N-acetyllactosamine. Biorg Med Chem Lett. 5:1995;673-676.
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