Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Heterogeneity of homologously expressed Hypocrea jecorina (Trichoderma reesei) Cel7B catalytic module
Show others and affiliations
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
Identifiers
URN: urn:nbn:se:kth:diva-23271DOI: 10.1111/j.1432-1033.2004.04031.xISI: 000220355100004Scopus ID: 2-s2.0-1942455827OAI: oai:DiVA.org:kth-23271DiVA: diva2:341969
Note
QC 20100525 QC 20111028Available from: 2010-08-10 Created: 2010-08-10 Last updated: 2017-12-12Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textScopus

Search in DiVA

By author/editor
Brumer, Harry
By organisation
Biotechnology
In the same journal
European Journal of Biochemistry
Biochemistry and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar

doi
urn-nbn

Altmetric score

doi
urn-nbn
Total: 59 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf