Comparative NMR analysis of cellooligosaccharide hydrolysis by GH9 bacterial and plant endo-1,4-ss-glucanases

Ulla J. Rudsander, Corine Sandstrom, Kathleen Piens, Emma R. Master, David B. Wilson, Harry Brumer, Lennart Kenne, Tuula T. Teeri*

*Corresponding author for this work

Research output: Contribution to journalArticleScientificpeer-review

Abstract

H-1 NMR spectroscopy has been used to analyze the product profiles arising from the hydrolysis of cellooligosaccharides by family GH9 cellulases. The product profiles obtained with the wild type and several active site mutants of a bacterial processive endoglucanase, Tf Cel9A, were compared with those obtained by a randomly acting plant endoglucanase, PttCe19A. PttCe19A is an orthologue of the Arabidopsis endocellulase, Korrigan, which is required for efficient cellulose biosynthesis. As expected, poplar PttCe19A was shown to catalyze the degradation of cellooligosaccharides by inversion of the configuration of the anomeric carbon. The product analyses showed that the number of interactions between the glucose units of the substrate and the aromatic residues in the enzyme active sites determines the point of cleavage in both enzymes.

Original languageEnglish
Pages (from-to)5235-5241
Number of pages7
JournalBiochemistry
Volume47
Issue number18
DOIs
Publication statusPublished - 6 May 2008
MoE publication typeA1 Journal article-refereed

Keywords

  • THERMOMONOSPORA-FUSCA
  • TRICHODERMA-REESEI
  • SUBSTRATE-BINDING
  • PICHIA-PASTORIS
  • ENDO-1,4-BETA-GLUCANASE
  • PURIFICATION
  • MECHANISM
  • ENDO-BETA-1,4-GLUCANASE
  • OLIGOSACCHARIDES
  • STRAWBERRY

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