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Structural characterization of N-linked oligosaccharides from cellobiohydrolase I secreted by the filamentous fungus Trichoderma reesei RUTC 30.

Authors
  • Maras, M
  • De Bruyn, A
  • Schraml, J
  • Herdewijn, P
  • Claeyssens, M
  • Fiers, W
  • Contreras, R
Type
Published Article
Journal
European journal of biochemistry / FEBS
Publication Date
May 01, 1997
Volume
245
Issue
3
Pages
617–625
Identifiers
PMID: 9182997
Source
Medline
License
Unknown

Abstract

We have characterized the primary structures of the predominant N-linked oligosaccharides on cellobiohydrolase I from the filamentous fungus Trichoderma reesei RUTC30. Different enzymatic and chromatographic techniques were used to analyze six oligosaccharides. The combined data showed that the fungal carbohydrates have a core structure that is identical to the mammalian N-linked core. In the bulk of the N-glycans, the alpha-1,3 arm is extended with two mannoses and a glucose, suggesting incomplete processing of the oligosaccharides in the endoplasmic reticulum. The alpha-1,6 arm shows a remarkable heterogeneity: in addition to alpha-1,2-Man and alpha-1,6-Man, the presence of a terminal mannose alpha-1,6-phosphodiester was observed. This latter substituent has not been characterized before on mannosidase-processed N-glycan and its function and synthesis pathway are entirely unknown. The predominant N-glycans on cellobiohydrolase I can be represented as follows: GlcMan8GlcNAc2, GlcMan7GlcNAc2, Man7GlcNAc2, ManPGlcMan7GlcNAc2, GlcMan5GlcNAc2 and Man5GlcNAc2.

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