Lack of the evidence for the enzymatic catabolism of Man₁GlcNAc₂ in Saccharomyces cerevisiae

References

• Varki A. Biological roles of oligosaccharides: all of the theories are correct. Glycobiology. 1993;3:97–130. 10.1093/glycob/3.2.97
   PubMed Web of Science ®Google Scholar
• Helenius A, Aebi M. Roles of N-linked glycans in the endoplasmic reticulum. Annu. Rev. Biochem. 2004;73:1019–1049. 10.1146/annurev.biochem.73.011303.073752
   PubMed Web of Science ®Google Scholar
• Harada Y, Hirayama H, Suzuki T. Generation and degradation of free asparagine-linked glycans. Cell. Mol. Life Sci. 2015;72:2509–2533. 10.1007/s00018-015-1881-7
   PubMed Web of Science ®Google Scholar
• Suzuki T, Harada Y. Non-lysosomal degradation pathway for N-linked glycans and dolichol-linked oligosaccharides. Biochem. Biophys. Res. Commun. 2014;453:213–219. 10.1016/j.bbrc.2014.05.075
   PubMed Web of Science ®Google Scholar
• Suzuki T, Park H, Hollingsworth NM, Sternglanz R, Lennarz WJ. PNG1, a yeast gene encoding a highly conserved peptide: N-glycanase. J. Cell Biol. 2000;149:1039–1052. 10.1083/jcb.149.5.1039
   PubMed Web of Science ®Google Scholar
• Chantret I, Frénoy JP, Moore SE. Free-oligosaccharide control in the yeast Saccharomyces cerevisiae: roles for peptide: N-glycanase (Png1p) and vacuolar mannosidase (Ams1p). Biochem. J. 2003;373:901–908. 10.1042/BJ20030384
   PubMed Web of Science ®Google Scholar
• Hirayama H, Seino J, Kitajima T, Jigami Y, Suzuki T. Free oligosaccharides to monitor glycoprotein endoplasmic reticulum-associated degradation in Saccharomyces cerevisiae. J. Biol. Chem. 2010;285:12390–12404. 10.1074/jbc.M109.082081
   PubMed Web of Science ®Google Scholar
• Chantret I, Kodali VP, Lahmouich C, Harvey DJ, Moore SE. Endoplasmic reticulum-associated degradation (ERAD) and free oligosaccharide generation in Saccharomyces cerevisiae. J. Biol. Chem. 2011;286:41786–41800. 10.1074/jbc.M111.251371
   PubMed Web of Science ®Google Scholar
• Harada Y, Buser R, Ngwa EM, Hirayama H, Aebi M, Suzuki T. Eukaryotic oligosaccharyltransferase generates free oligosaccharides during N-glycosylation. J. Biol. Chem. 2013;288:32673–32684. 10.1074/jbc.M113.486985
   PubMed Web of Science ®Google Scholar
• Suzuki T. Introduction to “Glycometabolome”. Trends Glycosci. Glycotechnol. 2009;21:219–227. 10.4052/tigg.21.219
   Web of Science ®Google Scholar
• Winchester B. Lysosomal metabolism of glycoproteins. Glycobiology. 2005;15(6):1R–15R.
   PubMed Web of Science ®Google Scholar
• Suzuki T, Yano K, Sugimoto S, Kitajima K, Lennarz WJ, Inoue S, et al. Endo-β-N-acetylglucosaminidase, an enzyme involved in processing of free oligosaccharides in the cytosol. Proc. Natl. Acad. Sci. 2002;99:9691–9696. 10.1073/pnas.152333599
   PubMed Web of Science ®Google Scholar
• Murakami S, Takaoka Y, Ashida H, Yamamoto K, Narimatsu H, Chiba Y. Identification and characterization of endo-β-N-acetylglucosaminidase from methylotrophic yeast Ogataea minuta. Glycobiology. 2013;23:736–744. 10.1093/glycob/cwt012
   PubMed Web of Science ®Google Scholar
• Stals I, Samyn B, Sergeant K, White T, Hoorelbeke K, Coorevits A, et al. Identification of a gene coding for a deglycosylating enzyme in Hypocrea jecorina. FEMS Microbiol. Lett. 2010;303:9–17. 10.1111/fml.2010.303.issue-1
   PubMed Web of Science ®Google Scholar
• Suzuki T, Park H, Kitajima K, Lennarz WJ. Peptides glycosylated in the endoplasmic reticulum of yeast are subsequently deglycosylated by a soluble peptide: N-glycanase activity. J. Biol. Chem. 1998;273:21526–21530. 10.1074/jbc.273.34.21526
   PubMed Web of Science ®Google Scholar
• Ademark P, Lundqvist J, Hägglund P, et al. Hydrolytic properties of a β-mannosidase purified from Aspergillus niger. J. Biotechnol. 1999;75:281–289. 10.1016/S0168-1656(99)00172-8
   PubMed Web of Science ®Google Scholar
• Kulminskaya AA, Eneiskaya EV, Isaeva-Ivanova LS, Savel’ev AN, Sidorenko IA, Shabalin KA, et al. Enzymatic activity and β-galactomannan binding property of β-mannosidase from Trichoderm reesei. Enzyme Microb. Technol. 1999;25:372–377. 10.1016/S0141-0229(99)00056-3
   Web of Science ®Google Scholar
• Kanamasa S, Takada G, Kawaguchi T, Sumitani J, Arai M. Overexpression and purification of Aspergillus aculeatus β-mannosidase and analysis of the integrated gene in Aspergillus oryzae. J. Biosci. Bioeng. 2001;92:131–137. 10.1016/S1389-1723(01)80213-9
   PubMed Web of Science ®Google Scholar
• Oda Y, Tonomura K. Characterization of β-mannanase and β-mannosidase secreted from the yeast Trichosporon cutaneum JCM 2947. Lett. Appl. Microbiol. 1996;22:173–178. 10.1111/j.1472-765X.1996.tb01136.x
   Web of Science ®Google Scholar
• Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, Henrissat B. The carbohydrate-active enzymes database (CAZy): an expert resource for glycogenomics. Nucleic Acids Res. 2009;37:D233–D238. 10.1093/nar/gkn663
   PubMed Web of Science ®Google Scholar
• Eguchi H, Ikeda Y, Koyota S, Honke K, Suzuki K, Gutteridge JM, et al. Oxidative damage due to copper ion and hydrogen peroxide induces GlcNAc-specific cleavage of an Asn-linked oligosaccharide. J. Biochem. 2002;131:477–484.
   PubMed Web of Science ®Google Scholar