Streptomyces matensis laminaripentaose hydrolase is an 'inverting' beta-1,3-glucanase

FEBS Lett. 2001 Jun 15;499(1-2):187-90. doi: 10.1016/s0014-5793(01)02551-0.

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

  • Biopolymers / chemistry
  • Biopolymers / metabolism
  • Chromatography, Gel
  • Escherichia coli / genetics
  • Glucan 1,3-beta-Glucosidase
  • Glucans / chemistry
  • Glucans / metabolism
  • Histidine*
  • Hydrolysis
  • Magnetic Resonance Spectroscopy
  • Peptides / genetics
  • Peptides / metabolism
  • Polysaccharides / chemistry
  • Polysaccharides / metabolism*
  • Protein Binding
  • Protein Structure, Quaternary
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / isolation & purification
  • Recombinant Fusion Proteins / metabolism
  • Stereoisomerism
  • Streptomyces / enzymology*
  • Streptomyces / genetics
  • beta-Glucans*
  • beta-Glucosidase / chemistry
  • beta-Glucosidase / genetics
  • beta-Glucosidase / isolation & purification
  • beta-Glucosidase / metabolism*

Substances

  • Biopolymers
  • Glucans
  • Peptides
  • Polysaccharides
  • Recombinant Fusion Proteins
  • beta-Glucans
  • polyhistidine
  • Histidine
  • laminaran
  • beta-1,3-glucan
  • beta-Glucosidase
  • Glucan 1,3-beta-Glucosidase