α-淀粉酶淀粉结合结构域：多个串联排列结构域与淀粉颗粒结合的协同效应。
Alpha-amylase starch binding domains: cooperative effects of binding to starch granules of multiple tandemly arranged domains.
作者信息
Guillén D, Santiago M, Linares L, Pérez R, Morlon J, Ruiz B, Sánchez S, Rodríguez-Sanoja R
机构信息
Departamento de Biología Molecular y Biotecnología, Instituto de Investigaciones Biomédicas, UNAM, A.P. 70228, 04510 México D.F., Mexico.
出版信息
Appl Environ Microbiol. 2007 Jun;73(12):3833-7. doi: 10.1128/AEM.02628-06. Epub 2007 Apr 27.
Abstract
The Lactobacillus amylovorus alpha-amylase starch binding domain (SBD) is a functional domain responsible for binding to insoluble starch. Structurally, this domain is dissimilar from other reported SBDs because it is composed of five identical tandem modules of 91 amino acids each. To understand adsorption phenomena specific to this SBD, the importance of their modular arrangement in relationship to binding ability was investigated. Peptides corresponding to one, two, three, four, or five modules were expressed as His-tagged proteins. Protein binding assays showed an increased capacity of adsorption as a function of the number of modules, suggesting that each unit of the SBD may act in an additive or synergic way to optimize binding to raw starch.
摘要
解淀粉乳杆菌α-淀粉酶淀粉结合域（SBD）是一个负责与不溶性淀粉结合的功能域。在结构上，该结构域与其他已报道的SBD不同，因为它由五个相同的91个氨基酸的串联模块组成。为了了解该SBD特有的吸附现象，研究了其模块排列与结合能力之间关系的重要性。对应于一个、两个、三个、四个或五个模块的肽被表达为带有His标签的蛋白质。蛋白质结合试验表明，吸附能力随着模块数量的增加而增强，这表明SBD的每个单元可能以累加或协同的方式发挥作用，以优化与生淀粉的结合。
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