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HIGH-THROUGHPUT IDENTIFICATION OF CATALYTIC REDOX-ACTIVE CYSTEINE RESIDUES
Citation:
FOMENKO, D. E., W. XING, B. ADAIR, D. J. THOMAS, AND V. N. GLADYSHEV. HIGH-THROUGHPUT IDENTIFICATION OF CATALYTIC REDOX-ACTIVE CYSTEINE RESIDUES . SCIENCE. American Association for the Advancement of Science (AAAS), Washington, DC, 315:387-389, (2007).
Impact/Purpose:
to develop a procedure for high-throughput identification of catalytic redox-active Cys in proteins
Description:
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 protein family-, structure- and taxa-independent method selectively detected the majority of known proteins with redox-active Cys, and made 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.