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

被引：38

作者：

Sunna, A

Gibbs, MD

Bergquist, PL ^{[1
]}

机构：

[1] Macquarie Univ, Dept Biol Sci, Sydney, NSW 2109, Australia

[2] Univ Auckland, Sch Med, Dept Mol Med, Auckland, New Zealand

来源：

BIOCHEMICAL JOURNAL | 2001年 / 356卷 / 356期

关键词：

affinity electrophoresis; modular glycoside hydrolases; non-catalytic modules;

D O I：

10.1042/0264-6021:3560791

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Many glycoside hydrolases, which degrade long-chain carbohydrate polymers. possess distinct catalytic modules and noncatalytic 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.

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收藏

页码：791 / 798

页数：8

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