用于二鸟苷酸环化酶和磷酸二酯酶活性测定的[P]-环二鸟苷酸的合成。
Synthesis of [P]-c-di-GMP for Diguanylate Cyclase and Phosphodiesterase Activity Determinations.
作者信息
Kazmierczak Barbara I
机构信息
Department of Medicine, Yale University, 333 Cedar St., New Haven, CT, 06520-8022, USA.
Department of Microbial Pathogenesis, Yale University, 333 Cedar St., New Haven, CT, 06520-8022, USA.
出版信息
Methods Mol Biol. 2017;1657:23-29. doi: 10.1007/978-1-4939-7240-1_3.
Diguanylate cyclases that synthesize and phosphodiesterases that hydrolyze the second messenger cyclic-di-GMP (c-di-GMP) are at the center of bacterial signaling pathways that control behaviors relevant to all aspects of microbial physiology and pathogenesis (Romling et al., Microbiol Mol Biol Rev 77(1):1-52, 2013). Bioinformatics tools can easily predict the presence of the diguanylate cyclase GGDEF domain, or the EAL and HD-GYP domains associated with phosphodiesterase activity. However, experimental confirmation of enzymatic activity is still necessary, as many proteins contain degenerate domains that lack catalytic activity but nonetheless function as c-di-GMP receptors.
合成第二信使环二鸟苷酸（c-di-GMP）的二鸟苷酸环化酶和水解c-di-GMP的磷酸二酯酶处于细菌信号通路的核心位置，这些信号通路控制着与微生物生理学和发病机制各个方面相关的行为（Romling等人，《微生物学与分子生物学综述》77(1):1 - 52，2013年）。生物信息学工具能够轻松预测二鸟苷酸环化酶GGDEF结构域，或与磷酸二酯酶活性相关的EAL和HD - GYP结构域的存在。然而，酶活性的实验确认仍然是必要的，因为许多蛋白质含有退化结构域，这些结构域缺乏催化活性，但仍可作为c-di-GMP受体发挥作用。
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