• Kenji Yamamoto
Reference work entry


Endoglycosidases release oligosaccharides from a sugar chain by cleaving defined sites within the sugar chain of glycoconjugates. There are two types of endoglycosidases acting on the sugar chains of glycoproteins. One is an endoglycosidase that hydrolytically cleaves the core region of N-linked sugar chains of glycoproteins, and the representative member of this type is endo-β-N-acetylglucosaminidase. The second type of endoglycosidases hydrolyzes the linkage between the O-linked sugar chain and the protein of glycoproteins, and endo-α-N-acetylgalactosaminidase is a representative member of this class. These endoglycosidases from microbial sources are indispensable tools for analyzing the structure and function of sugar chains in glycoproteins and glycopeptides. Endo-β-mannosidase is a plant-specific endoglycosidase that acts on the N-linked sugar chain of glycoproteins. It is suggested that there are three enzymes acting on the common core region between the peptide and the glycosaminoglycan in various proteoglycans. They are endo-β-xylosidase, endo-β-galactosidase, and endo-β-glucuronidase. The catabolic mechanism of glycosaminoglycans is complex and the role of these endoglycosidases is important. In regard to glycosphingolipid-degrading enzymes, real glycosphingolipid-degrading enzymes had remained undiscovered until endoglycoceramidase was isolated and characterized. This novel enzyme hydrolyzes the β-glucosidic linkage between oligosaccharides and ceramides of various acidic and neutral glycosphingolipids. Most endoglycosidases show transglycosylation activity and this activity is useful for synthesizing various glycosylated compounds, including bioactive glycoconjugates. Some bioactive compounds have been synthesized with the transglycosylation activity of microbial endo-β-N-acetylglucosaminidase.


Endoglycosidase Endo-β-N-acetylglucosaminidase Endo-α-N-acetylgalactosaminidase Endo-β-mannosidase Endo-β-galactosidase Endoglycoceramidase Transglycosylation Chemo-enzymatic synthesis Remodeling 


  1. Bhavanandan VP (2006) Endoglycosidases that relate to O-glycans. In: Endo M, Hase K, Yamamoto K, Takagaki K (eds) Endoglycosidases. Kodansha, Tokyo, pp 84–94Google Scholar
  2. Fujita K, Oura F, Nagamine N, Katayama T, Hiratake J, Sakata K, Kumagai H, Yamamoto K (2005) Identification and molecular cloning of a novel glycoside hydrolase family of core 1 type O-tpinsglycan-specific endo-alpha-N-acetylgalactosaminidase from Bifidobacterium longum. J Biol Chem 280:37415–37422Google Scholar
  3. Ito M, Yamagata T (1986) A novel glycosphingolipid-degrading enzyme cleaves of the linkage between the oligosaccharide and ceramide of neutral and acidic glycosphingolipid. J Biol Chem 261:14278–14282Google Scholar
  4. Muramatsu T (1971) Demonstration of an endo-glycosidase acting on a glycoprotein. J Biol Chem 246:5535–5537PubMedGoogle Scholar
  5. Sasaki A, Yamagishi M, Mega T, Norioka S, Natsuka S, Hase S (1999) Partial purification and characterization of a novel endo-beta-mannosidase acting on N-linked sugar chains from Lilium longflorum thumb. J Biochem 125:363–367Google Scholar
  6. Takagaki K (2006) Endoglycosidases that relate to proteoglycans. In: Endo M, Hase K, Yamamoto K, Takagaki K (eds) Endoglycosidases. Kodansha, Tokyo, pp 101–109Google Scholar
  7. Tarentino AL, Plummer TH, Maley F (1972) A re-evaluation of the oligosaccharide sequence associated with ovalbumin. J Biol Chem 247:2629–2631PubMedGoogle Scholar
  8. Yamamoto K (2006) Endoglycosidases that relate to N-glycans. In: Endo M, Hase K, Yamamoto K, Takagaki K (eds) Endoglycosidases. Kodansha, Tokyo, pp 55–69Google Scholar
  9. Yamamoto K, Fujimori K, Haneda K, Mizuno M, Inazu T, Kumagai H (1998) Chemoenzymatic synthesis of a novel glycopeptides using a microbial endoglycosidase. Carbohydr Res 305:415–422Google Scholar

Copyright information

© Springer Japan 2015

Authors and Affiliations

  1. 1.Research Institute for Bioresources and BiotechnologyIshikawa Prefectural UniversityIshikawaJapan

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