Structural andfunctional analysis of glycoside hydrolases with multiple catalytic domains.

在本研究中，我们通过酶学实验和结构生物学分析，分别揭示了两个催化结构域（CD），淀粉结合结构域（SBD）和CD-SBD之间的相互作用，分别来自链霉菌（Streptomyces corchorusiiand）的细胞表面相关淀粉酶和多粘类芽孢杆菌（Paenibacillus polymyxa）的-淀粉酶，表明含有多个CD的蛋白质比含有单个CD的蛋白质具有更好的催化效率。

In this study, we revealed the interactions between two catalytic domains (CD), starch-binding domains (SBD), and CD-SBD, respectively, by the experiments for enzymology and the analysis for structural biology, using cell-surface-associated amylase from Streptomyces corchorusiiand /-amylase from Paenibacillus polymyxa, suggesting that a protein hold multi CD shows better catalytic efficiency than a protein hold single CD.