Studying non-covalent enzyme carbohydrate interactions by STD NMR
| ISSN: | 0008-6215 |
|---|---|
| Přístupová URL adresa: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5bb95d0ef12c5858b4ca937eb42c6ad4 https://doi.org/10.1016/j.carres.2007.12.023 |
| Rights: | CLOSED |
| Přírůstkové číslo: | edsair.doi.dedup.....5bb95d0ef12c5858b4ca937eb42c6ad4 |
| Autor: | Bernd Nidetzky, Regina Kratzer, Christiane Goedl, Alexandra Schwarz, Catrin Tyl, Lothar Brecker |
| Rok vydání: | 2008 |
| Předmět: |
Glycoside Hydrolases
Mutant Corynebacterium Schizophyllum Ligands Biochemistry Analytical Chemistry Aldehyde Reductase Point Mutation Glycoside hydrolase Nuclear Magnetic Resonance Biomolecular Candida chemistry.chemical_classification Starch phosphorylase biology Aspergillus fumigatus beta-Glucosidase Organic Chemistry Schizophyllum commune Substrate (chemistry) Starch Phosphorylase General Medicine Nuclear magnetic resonance spectroscopy Carbohydrate biology.organism_classification Enzyme chemistry Glucosyltransferases Carbohydrate Metabolism |
| Zdroj: | Carbohydrate Research. 343:2153-2161 |
| ISSN: | 0008-6215 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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