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Article summary:

1. ENGases are glycosidic hydrolases that act on the β-1,4-glycosidic linkage within the N,N′-diacetylchitobiose core of N-glycans and have wide applications in synthetic applications that need homogeneous glycosides of glycopeptides, glycoproteins, and glycoconjugates.

2. Endo-CC N180H is a mutant of endo-CC extracted from Coprinopsis cinerea that can transfer glycan to RNase B and has several advantages over other ENGase mutants.

3. The specificity of endo-CC N180H has not been well characterized, but this study reports its glycan transfer activity from sialylglycopeptide (SGP) 1 to various GlcNAc-containing potential substrates such as monosaccharides, glycopeptides, and a deglycosylated antibody.

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