β-甘露聚糖酶的结构生物学研究现状和展望  

Recent advances and prospect on structural biology of β-mannanase-A review

作　　者：赵月菊[1,2] 薛燕芬[1] 马延和[1] 

机构地区：[1]中国科学院微生物研究所极端微生物实验室,北京100101 [2]中国科学院研究生院,北京100049

出　　处：《微生物学报》2009年第9期1131-1137,共7页Acta Microbiologica Sinica

基　　金：国家"973项目"(2003CB716001)~~

摘　　要：β-甘露聚糖酶是一种半纤维素水解酶,广泛存在于动植物和微生物中,在造纸,纺织印染,洗涤,食品,饲料,医药和石油开采等工业中有着广阔的应用前景。β-甘露聚糖酶往往由催化域和非催化域两部分组成的。催化域折叠成TIM桶状结构,参与底物的结合和催化;碳水化合物结合域,作为最常见的一种非催化域,采用经典的β三明治结构,可以增强结合有纤维素的甘露糖水解能力。本文主要对组成β-甘露聚糖酶的各个模块三维结构特征和功能进行了系统的综述。β- （β-1,4-D-mannanase, EC 3.2.1.78）, as a hemicellulose hydrolase, are widely distributed in bacteria, fungi, plants and even animals. They can randomly hydrolyze the β-1,4-mannosidic linkages in mannan and heteromannan and have great potential in the food/feed, pulp/paper, medicine, oil exploitation and detergent industries. Most β- often display a modular organization and usually contain structurally discrete catalytic and non-catalytic modules. Catalytic domains of these enzymes share a （β/α）s-barrel fold, which play important roles in substrate binding and catalysis. Carbohydrate binding modules, as the most common non-catalytic modules, fold as β-sandwich and facilitate the targeting of these enzymes to polysaccharide. In this review, a brief introduction is given concerning structural characteristics and function of these β-mannanase modules.

关 键 词：Β-甘露聚糖酶 催化域 碳水化合物结合域 结构功能 

分 类 号：Q55[生物学—生物化学]