Direct Screening for Phosphatase Activity by Turnover-Based Capture of Protein Catalysts This work was supported by BBSRC studentships (to J.B. and H.D.), by an EPSRC studentship (to J.H.R.), and by an EC TMR studentship (to S.C.-T.).

Abstract

Disulfide exchange leads to the attachment of phosphate ester 1 to a solid surface, which can then be used in turnover selection to screen a large library of proteins for phosphate monoester hydrolysis activity. This ester hydrolysis leads to formation of an electrophilic quinone methide 2, which bonds covalently to the protein catalyst and links it to the surface for selection.