Identification of novel β-mannan- and β-glucan-binding modules: Evidence for a superfamily of carbohydrate-binding modules

A. Sunna, M. D. Gibbs, P. L. Bergquist*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

38 Citations (Scopus)

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 β-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.

Original languageEnglish
Pages (from-to)791-798
Number of pages8
JournalBiochemical Journal
Volume356
Issue number3
DOIs
Publication statusPublished - 15 Jun 2001

Fingerprint

Dive into the research topics of 'Identification of novel β-mannan- and β-glucan-binding modules: Evidence for a superfamily of carbohydrate-binding modules'. Together they form a unique fingerprint.

Cite this