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High-Throughput Identification of Catalytic Redox-Active Cysteine Residues

机译:高通量鉴定催化活性的半胱氨酸残基

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Cysteine (Cys) residues often play critical roles in proteins; however, identification of their specific functions has been limited to case-by-case experimental approaches. We developed a procedure for high-throughput identification of catalytic redox-active Cys in proteins by searching for sporadic selenocysteine-Cys pairs in sequence databases. This method is independent of protein family, structure, and taxon. We used it to selectively detect the majority of known proteins with redox-active Cys and to make additional predictions, one of which was verified. Rapid accumulation of sequence information from genomic and metagenomic projects should allow detection of many additional oxidoreductase families as well as identification of redox-active Cys in these proteins.
机译:半胱氨酸(Cys)残基通常在蛋白质中起关键作用。但是,对它们特定功能的识别仅限于个案实验方法。我们通过在序列数据库中搜索散发的硒代半胱氨酸-Cys对,开发了一种用于蛋白质中催化氧化还原活性Cys的高通量鉴定的程序。此方法与蛋白质家族,结构和分类单元无关。我们使用它来选择性地检测具有氧化还原活性的Cys的大多数已知蛋白质,并做出其他预测,其中一项已得到验证。来自基因组和宏基因组计划的序列信息的快速积累,应允许检测许多其他的氧化还原酶家族,以及鉴定这些蛋白中的氧化还原活性Cys。

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