A structure-based approach for detection of thiol oxidoreductases and their catalytic redox-active cysteine residues.

ABSTRACT: Cysteine (Cys) residues often play critical roles in proteins, for example, in the formation of structural disulfide bonds, metal binding, targeting proteins to the membranes, and various catalytic functions. However, the structural determinants for various Cys functions are not clear. Thiol oxidoreductases, which are enzymes containing catalytic redox-active Cys residues, have been extensively studied, but even for these proteins there is little understanding of what distinguishes their catalytic redox Cys from other Cys functions. Herein, we characterized thiol oxidoreductases at a structural level and developed an algorithm that can recognize these enzymes by (i) analyzing amino acid and secondary structure composition of the active site and its similarity to known active sites containi

SUBMITTER: Marino SM 

PROVIDER: S-EPMC2673044 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature