The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

Accepted name: mannosyl-oligosaccharide glucosidase
Reaction: Exohydrolysis of the non-reducing terminal glucose residues in the mannosyl-oligosaccharide Glc3Man9GlcNAc2
Other name(s): Glc3Man9NAc2 oligosaccharide glucosidase; trimming glucosidase I
Systematic name: mannosyl-oligosaccharide glucohydrolase
Comments: Also acts, more slowly, on the corresponding glycolipids and glycopeptides. Involved in the formation of high-mannose and complex glycoproteins.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, 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. [PMID: 7356331]
[EC created 1984]

Data © 2001–2018 IUBMB
Web site © 2005–2018 Andrew McDonald