High-throughput identification of catalytic redox-active cysteine residues.
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.
Fomenko
Dmitri E
DE
Department of Biochemistry, University of Nebraska, Lincoln, NE 68588, USA.
Xing
Weibing
W
Adair
Blakely M
BM
Thomas
David J
DJ
Gladyshev
Vadim N
VN
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D019843:Archaeal Proteins / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry; D001483:Base Sequence; D002384:Catalysis; D019295:Computational Biology; D003545:Cysteine / Q000032:analysis / Q000737:chemistry*; D030561:Databases, Nucleic Acid; D030562:Databases, Protein; D004798:Enzymes / Q000737:chemistry*; D005057:Eukaryotic Cells; D019143:Evolution, Molecular; D008780:Methyltransferases / Q000737:chemistry; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D017279:Selenocysteine / Q000737:chemistry; D051140:Selenoproteins / Q000737:chemistry*
D019843:Archaeal Proteins; D001426:Bacterial Proteins; D004798:Enzymes; D011506:Proteins; D051140:Selenoproteins; D017279:Selenocysteine; D010088:Oxidoreductases; D008780:Methyltransferases; D003545:Cysteine