The Enzyme Database

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Accepted name: mannosyl-oligosaccharide glucosidase
Reaction: Glc3Man9GlcNAc2-[protein] + H2O = Glc2Man9GlcNAc2-[protein] + β-D-glucopyranose
Glossary: Glc3Man9GlcNAc2 = [α-D-Glc-(1→2)-α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-{α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)}-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc]-N-Asn-[protein]
Glc2Man9GlcNAc2-[protein] = [α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-{α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)}-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc]-N-Asn-[protein]
Other name(s): Glc3Man9NAc2 oligosaccharide glucosidase; trimming glucosidase I; CWH41 (gene name); MOGS (gene name); mannosyl-oligosaccharide glucohydrolase
Systematic name: Glc3Man9GlcNAc2-[protein] glucohydrolase (configuration-inverting)
Comments: This enzyme catalyses the first step in the processing of the N-glycan tetradecasaccharide precursor Glc3Man9GlcNAc2, which takes place in the endoplasmic reticulum, by removing the distal α-1,2-linked glucose residue. This and subsequent processing steps are required before complex N-glycans can be synthesized.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 78413-07-7
1.  Elting, J.J., Chen, W.W. and Lennarz, J. Characterization of a glucosidase involved in an initial step in the processing of oligosaccharide chains. J. Biol. Chem. 255 (1980) 2325–2331. [PMID: 7358674]
2.  Grinna, L.S. and Robbins, P.W. Glycoprotein biosynthesis. Rat liver microsomal glucosidases which process oligosaccharides. J. Biol. Chem. 254 (1979) 8814–8818. [PMID: 479161]
3.  Kilker, R.D., Saunier, B., Tkacz, J.S. and Herscovics, A. Partial purification from Saccharomyces cerevisiae of a soluble glucosidase which removes the terminal glucose from the oligosaccharide Glc3Man9GlcNAc2. J. Biol. Chem. 256 (1981) 5299–5603. [PMID: 7014569]
4.  Grinna, L.S. and Robbins, P.W. Substrate specificities of rat liver microsomal glucosidases which process glycoproteins. J. Biol. Chem. 255 (1980) 2255–2258. [PMID: 7358666]
5.  Mark, M.J. and Kornfeld, S. Partial purification and characterization of the glucosidases involved in the processing of asparagine-linked oligosaccharides. Arch. Biochem. Biophys. 199 (1980) 249–258. [DOI] [PMID: 7356331]
[EC created 1984, modified 2018]

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