[10] Glycosyltransferases involved in elongation of N-glycosidically linked oligosaccharides of the complex or N-acetyllactosamine type
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The production of biopharmaceuticals in plant systems
2009, Biotechnology AdvancesCitation Excerpt :Many different factors may influence the distribution of glycoforms produced on a protein such as the polypeptide itself, the glycosylation site in the polypeptide, the host cell, and the environment of the host cell (Dwek, 1996). On the level of the individual cell, the microheterogeneity of the N-glycans on a given protein depends on glycosylation enzyme levels, their competition for a common substrate, substrate availability, and controls at the level of substrate specificity (e.g., critical sugar residues which turn enzyme activity on or off, branch specificity, and the role of the polypeptide in the glycoprotein substrate) (Schachter et al., 1983). In recombinantly produced proteins, cultivation conditions such as ammonia concentration, glucose concentration, presence or absence of serum, concentration of nucleotide-sugars, and pH are known to influence glycosylation of the protein (Bailey et al., 1998).
Use of synthetic oligosaccharide substrate analogs to map the active sites of N-acetylglucosaminyltransferases I and II
2003, Methods in EnzymologyCitation Excerpt :The second stage begins with the transfer of Glc3Man9GlcNAc2 from Glc3Man9GlcNAc2-pyrophosphate-dolichol to an Asn residue of the nascent glycoprotein followed by processing to Man5GlcNAc2-Asn-X. The third stage occurs primarily in the Golgi apparatus and starts when UDP-GlcNAc:α3-d-mannoside β1,2-N-acetylglucosaminyltransferase I (GlcNAc-T I, EC 2.4.1.101) transfers a GlcNAc residue in β1,2 linkage to the Man-α1,3 arm of Man5GlcNAc2-Asn-X, followed by the removal of two mannose residues by α3,6-mannosidase II to form the substrate for UDP-GlcNAc:α6-d-mannoside β1,2-N-acetylglucosaminyltransferase II (GlcNAc-T II, EC 2.4.1.143) (Fig. 1).6 GlcNAc-T II transfers GlcNAc in β1,2 linkage to the Man-α1,6 arm of the product of α3,6-mannosidase II (Fig. 1).
Activity of UDP-GlcNAc:GLcNacβ1→6(GlcNacβ1→2)Manα1→R[GlcNAc to Man]β1→4AN-Acetyglucosaminyltransferase VI (GNT VI) from the ovaries of Oryzias latipes (Medaka fish)
1997, Biochemical and Biophysical Research CommunicationsGlycosylation defect in Lec1 Chinese hamster ovary mutant is due to a point mutation in N-acetylglucosaminyltransferase 1 gene
1996, Journal of Biological Chemistry