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EC Number
Posttranslational Modification
Commentary
Reference
1.13.12.6
glycoprotein
glycosylation pattern analysis using LCMS/MS. In the recombinnat enzyme, two potential N-glycosylation sites are modified with plant-type oligosaccharide chains. Partial deglycosylation (trimming) of recombinant Cluc by beta-N-acetylhexosaminidase, HexNAc residues at the non-reducing termini of glycopeptides (Pronase E-digested) are completely eliminated at both glycosylation sites after beta-N-acetylhexosaminidase treatment (at Asn182 and Asn404). The glycan compositions after treatment displays trimannosyl cores (Hex3HexNAc2)+/-Fuc+/-Xyl. Specifically, because the trimannosyl core is fully occupied by Fuc and Xyl on Asn404, only a single signal corresponding to the trimannosyl core +Fuc +Xyl remains after treatment. This glycan-trimmed recombinant protein still exhibits nearly the same level of activity as the unmodified glycoprotein
746376
1.13.12.6
glycoprotein
N-glycosylation sites: T184 and N404
764716
1.13.12.6
glycoprotein
the enzyme has two N-glycosylation sites with the consensus sequence for N-glycosylation (Asn-X-Ser/Thr). The producibility and relative specific activity are apparently reduced in Cluc mutated in the phosphorylation sites, although the thermostability and secretion efficiency are not affected. N-glycosylation modifications and the proper amino acid sequence of the N-glycan binding sites of Cluc are required for the complete protein folding to form a stable catalytic center, for the proper conformation of substrate-protein interaction residues, or for both. Defects in the glycosylation modification are not related to secretion process and stability of the protein
745977
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