Studying non-covalent enzyme carbohydrate interactions by STD NMR

Lothar Brecker, Alexandra Schwarz, Christiane Goedl, Regina Kratzer, Catrin E. Tyl, Bernd Nidetzky

Research output: Contribution to journalArticlepeer-review

10 Scopus citations


Saturation transfer difference NMR spectroscopy is used to study non-covalent interactions between four different glycostructure transforming enzymes and selected substrates and products. Resulting binding patterns represent a molecular basis of specific binding between ligands and biocatalysts. Substrate and product binding to Aspergillus fumigatus glycosidase and to Candida tenuis xylose reductase are determined under binding-only conditions. Measurement of STD effects in substrates and products over the course of enzymatic conversion provides additional information about ligand binding during reaction. Influences of co-substrates and co-enzymes in substrate binding are determined for Schizophyllum commune trehalose phosphorylase and C. tenuis xylose reductase, respectively. Differences between ligand binding to wild type enzyme and a corresponding mutant enzyme are shown for Corynebacterium callunae starch phosphorylase and its His-334→Gly mutant. The resulting binding patterns are discussed with respect to the possibility that ligands do not only bind in the productive mode.

Original languageEnglish (US)
Pages (from-to)2153-2161
Number of pages9
JournalCarbohydrate Research
Issue number12
StatePublished - Aug 11 2008

Bibliographical note

Funding Information:
We thank Susanne Felsinger (University of Vienna) for assistance in measuring NMR spectra. Financial support from the Austrian Science Funds (P15118-MOB, P18038-B09, and the DK Molecular Enzymology W901-B05) is gratefully acknowledged.


  • Binding-only conditions
  • Co-substrate binding
  • Glycostructures transforming enzyme
  • Point mutated enzyme


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