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Heterogeneity of homologously expressed Hypocrea jecorina (Trichoderma reesei) Cel7B catalytic module.

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Author

Summary, in English

The catalytic module of Hypocrea jecorina (previously Trichoderma reesei) Cel7B was homologously expressed by transformation of strain QM9414. Post-translational modifications in purified Cel7B preparations were analysed by enzymatic digestions, high performance chromatography, mass spectrometry and site-directed mutagenesis. Of the five potential sites found in the wild-type enzyme, only Asn56 and Asn182 were found to be N-glycosylated. GlcNAc2Man5 was identified as the predominant N-glycan, although lesser amounts of GlcNAc2Man7 and glycans carrying a mannophosphodiester bond were also detected. Repartition of neutral and charged glycan structures over the two glycosylation sites mainly accounts for the observed microheterogeneity of the protein. However, partial deamidation of Asn259 and a partially occupied O-glycosylation site give rise to further complexity in enzyme preparations.

Publishing year

2004

Language

English

Pages

1266-1276

Publication/Series

European Journal of Biochemistry

Volume

271

Issue

7

Document type

Journal article

Publisher

Wiley-Blackwell

Topic

  • Biological Sciences

Keywords

  • N-glycan
  • protein glycosylation
  • O-glycan
  • Tricho-derma reesei
  • cellulase.

Status

Published

ISBN/ISSN/Other

  • ISSN: 0014-2956