High-throughput identification of catalytic redox-active cystein residues

Dmitri E. Fomenko, Weibing Xing, Blakely M. Adair, David J. Thomas, Vadim N. Gladyshev

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Abstract

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.

Original languageEnglish (US)
Pages (from-to)387-389
Number of pages3
JournalScience
Volume315
Issue number5810
DOIs
StatePublished - Jan 19 2007

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Cite this

Fomenko, D. E., Xing, W., Adair, B. M., Thomas, D. J., & Gladyshev, V. N. (2007). High-throughput identification of catalytic redox-active cystein residues. Science, 315(5810), 387-389. https://doi.org/10.1126/science.1133114