Streptomyces matensis laminaripentaose hydrolase is an ‘inverting’ β-1,3-glucanase
| Autor: | T. Nishimura, J. Allouch, Mirjam Czjzek, Christophe Bignon, Takehiko Watanabe, Bernard Henrissat, Hervé Darbon |
|---|---|
| Jazyk: | angličtina |
| Předmět: |
Laminaripentaose hydrolase
Anomer Magnetic Resonance Spectroscopy beta-Glucans Recombinant Fusion Proteins Streptomyces matensis Biophysics Biochemistry law.invention chemistry.chemical_compound Biopolymers Structural Biology law Polysaccharides Hydrolase Genetics Escherichia coli Glycoside hydrolase Histidine Protein Structure Quaternary Molecular Biology Glucans Reaction mechanism chemistry.chemical_classification Hydrolysis beta-Glucosidase β-1 3-Glucanase Stereoisomerism Cell Biology Glucan 1 3-beta-Glucosidase Glucanase Streptomyces Monomer Enzyme chemistry Recombinant DNA Chromatography Gel Peptides Protein Binding |
| Zdroj: | FEBS Letters. (1-2):187-190 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/S0014-5793(01)02551-0 |
| Popis: | The laminaripentaose-producing β-1,3-glucanase of Streptomyces matensis is a member of the glycoside hydrolase family GH-64. We have constructed and purified a recombinant hexahistidine-tagged form of the enzyme for characterisation. The enzyme, which exists as a monomer in solution, hydrolyses β-1,3-glucan by a mechanism leading to overall inversion of the anomeric configuration. This is the first determination of the mechanism prevailing in glycoside hydrolase family GH-64 and this is the first characterisation of an ‘inverting’ β-1,3-glucanase. |
| Databáze: | OpenAIRE |
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