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Heterogeneity of homologously expressed Hypocrea jecorina (Trichoderma reesei) Cel7B catalytic module
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2004 (English)In: European Journal of Biochemistry, ISSN 0014-2956, E-ISSN 1432-1033, Vol. 271, no 7, 1266-1276 p.Article in journal (Refereed) Published
Abstract [en]

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. GlcNAc(2)Man(5) was identified as the predominant N-glycan, although lesser amounts of GlcNAc(2)Man(7) 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.

Place, publisher, year, edition, pages
2004. Vol. 271, no 7, 1266-1276 p.
Keyword [en]
protein glycosylation, O-glycan, N-glycan, Trichoderma reesei, cellulase, cellobiohydrolase-i cel7a, aqueous 2-phase systems, endoglucanase-i, asparagine residues, crystal-structure, n-glycosylation, sequence, protein, identification, deamidation
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:kth:diva-23271DOI: 10.1111/j.1432-1033.2004.04031.xISI: 000220355100004ScopusID: 2-s2.0-1942455827OAI: diva2:341969
QC 20100525 QC 20111028Available from: 2010-08-10 Created: 2010-08-10 Last updated: 2011-10-28Bibliographically approved

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