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13类α-淀粉酶对不同生活条件的适应性。

Adaptation of class-13 alpha-amylases to diverse living conditions.

作者信息

Linden Anni, Wilmanns Matthias

机构信息

EMBL-Hamburg c/o DESY, Notkestrasse 85, 22603 Hamburg, Germany.

出版信息

Chembiochem. 2004 Feb 6;5(2):231-9. doi: 10.1002/cbic.200300734.

Abstract

There are currently 35 available nonredundant molecular structures of class-13 alpha-amylases (EC 3.2.1.1), mostly from microbial organisms living under a wide range of environmental conditions. One of the most recent additions has been the first alpha-amylase structure of a hyperthermophilic archaeon [Linden et al., J. Biol. Chem. 2003, 278, 9875-9884]. The structure has been used for comparative analyses with a representative set of three alpha-amylases from thermophilic, mesophilic and psychrophilic sources to identify molecular parameters for environmental adaptation. Our analysis supports generally observed trends such as an increase in structural compactness as well as an increase in salt bridges in order to cope with high-temperature conditions. The two representative thermophilic structures used in this comparative study have independently evolved di-metal centres--not present in the mesophilic and psychrophilic structures--in the vicinity of the active site. These observations may provide impetus for the design of alpha-amylases with improved molecular properties to enhance their utility in biotechnological processes.

摘要

目前有35种可用的13类α-淀粉酶(EC 3.2.1.1)的非冗余分子结构,大多来自生活在各种环境条件下的微生物。最新增加的结构之一是嗜热古菌的首个α-淀粉酶结构[林登等人,《生物化学杂志》,2003年,第278卷,第9875 - 9884页]。该结构已用于与一组分别来自嗜热、嗜温和嗜冷源的具有代表性的三种α-淀粉酶进行比较分析,以确定环境适应性的分子参数。我们的分析支持了一些普遍观察到的趋势,比如为了应对高温条件,结构紧凑性增加以及盐桥数量增多。在这项比较研究中使用的两种具有代表性的嗜热结构在活性位点附近独立进化出了二金属中心,而嗜温和嗜冷结构中不存在这种中心。这些观察结果可能为设计具有改进分子特性的α-淀粉酶提供动力,以提高它们在生物技术过程中的效用。

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