Abstract
The laminaripentaose-producing beta-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 beta-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' beta-1,3-glucanase.
MeSH terms
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Biopolymers / chemistry
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Biopolymers / metabolism
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Chromatography, Gel
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Escherichia coli / genetics
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Glucan 1,3-beta-Glucosidase
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Glucans / chemistry
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Glucans / metabolism
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Histidine*
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Hydrolysis
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Magnetic Resonance Spectroscopy
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Peptides / genetics
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Peptides / metabolism
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Polysaccharides / chemistry
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Polysaccharides / metabolism*
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Protein Binding
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Protein Structure, Quaternary
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / isolation & purification
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Recombinant Fusion Proteins / metabolism
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Stereoisomerism
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Streptomyces / enzymology*
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Streptomyces / genetics
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beta-Glucans*
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beta-Glucosidase / chemistry
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beta-Glucosidase / genetics
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beta-Glucosidase / isolation & purification
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beta-Glucosidase / metabolism*
Substances
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Biopolymers
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Glucans
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Peptides
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Polysaccharides
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Recombinant Fusion Proteins
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beta-Glucans
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polyhistidine
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Histidine
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laminaran
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beta-1,3-glucan
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beta-Glucosidase
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Glucan 1,3-beta-Glucosidase