Identification of novel beta-mannan- and beta-glucan-binding modules: evidence for a superfamily of carbohydrate-binding modules

Biochem J. 2001 Jun 15;356(Pt 3):791-8. doi: 10.1042/0264-6021:3560791.

Abstract

Many glycoside hydrolases, which degrade long-chain carbohydrate polymers, possess distinct catalytic modules and non-catalytic carbohydrate-binding modules (CBMs). On the basis of conserved protein secondary structure, we describe here the identification and experimental characterization of novel type of mannanase-associated mannan-binding module and also characterization of two CBM family 4 laminarinase-associated beta-glucan-binding modules. These modules are predicted to belong to a superfamily of CBMs which include families 4, 16, 17, 22 and a proposed new family, family 27.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Electrophoresis, Polyacrylamide Gel
  • Glucans / metabolism*
  • Glycoside Hydrolases / chemistry
  • Glycoside Hydrolases / metabolism*
  • Mannans / metabolism*
  • Models, Molecular
  • Molecular Sequence Data
  • Plasmids
  • Protein Conformation
  • Sequence Homology, Amino Acid

Substances

  • Glucans
  • Mannans
  • Glycoside Hydrolases