Streptomyces matensis laminaripentaose hydrolase is an ‘inverting’ β-1,3-glucanase

• Published in: FEBS letters Vol. 499; no. 1; pp. 187 - 190
• Main Authors: Nishimura, T., Bignon, C., Allouch, J., Czjzek, M., Darbon, H., Watanabe, T., Henrissat, B.
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 15.06.2001
• Subjects: beta-Glucans; beta-Glucosidase - chemistry; beta-Glucosidase - genetics; beta-Glucosidase - isolation & purification; beta-Glucosidase - metabolism; Biopolymers - chemistry; Biopolymers - metabolism; Chromatography, Gel; Escherichia coli - genetics; Glucan 1,3-beta-Glucosidase; Glucans - chemistry; Glucans - metabolism; Histidine; Hydrolysis; IPTG, isopropyl 1-thio-β-D-galactoside; Laminaripentaose hydrolase; LPHase, laminaripentaose-producing β-1,3-glucanase; Magnetic Resonance Spectroscopy; Peptides - genetics; Peptides - metabolism; Polysaccharides - chemistry; Polysaccharides - metabolism; Protein Binding; Protein Structure, Quaternary; Reaction mechanism; Recombinant Fusion Proteins - chemistry; Recombinant Fusion Proteins - isolation & purification; Recombinant Fusion Proteins - metabolism; SDS–PAGE, sodium dodecyl sulphate–polyacrylamide gel electrophoresis; Stereoisomerism; Streptomyces - enzymology; Streptomyces - genetics; Streptomyces matensis; β-1,3-Glucanase; SDS–PAGE, sodium dodecyl sulphate–polyacrylamide gel electrophoresis; Reaction mechanism; Laminaripentaose hydrolase; Streptomyces matensis; LPHase, laminaripentaose-producing β-1,3-glucanase; IPTG, isopropyl 1-thio-β- D-galactoside; β-1,3-Glucanase
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(01)02551-0

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.