The difference in affinity between two fungal cellulose-binding domains is dominated by a single amino acid substitution

Markus Linder , Gunnar Lindeberg, Tapani Reinikainen, Tuula T. Teeri, Göran Pettersson

Research output: Contribution to journalArticleScientificpeer-review

Abstract

Cellulose-binding domains (CBDs) form distinct functional units of most cellulolytic enzymes. We have compared the cellulose-binding affinities of the CBDs of cellobiohydrolase I (CBHI) and endoglucanase I(EGI) from the fungus Trichoderma reesei. The CBD of EGI had significantly higher affinity than that of CBHI. Four variants of the CBHI CBD were made in order to identify the residues responsible for the increased affinity in EGI. Most of the difference could be ascribed to a replacement of a tyrosine by a tryptophan on the flat cellulose-binding face.

Original languageEnglish
Pages (from-to)96-98
Number of pages3
JournalFEBS Letters
Volume372
Issue number1
DOIs
Publication statusPublished - 18 Sep 1995
MoE publication typeA1 Journal article-refereed

Keywords

  • CELLULOSE-BINDING DOMAIN
  • SYNTHETIC PEPTIDE
  • PROTEIN CARBOHYDRATE INTERACTION
  • CELLULASE
  • TRICHODERMA REESEI
  • NUCLEAR MAGNETIC-RESONANCE
  • CELLOBIOHYDROLASE-I
  • TRICHODERMA-REESEI
  • SEQUENCE

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