Catalysis of the cleavage of uridine 3'-2, 2, 2-trichloroethylphosphate by a designed Helix-Loop-Helix motif peptide

J Razkin, H Nilsson, L Baltzer

Index: Razkin, Jesus; Nilsson, Helena; Baltzer, Lars Journal of the American Chemical Society, 2007 , vol. 129, # 47 p. 14752 - 14758

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Citation Number: 21

Abstract

A 42-residue peptide that folds into a helix-loop-helix motif and dimerizes to form a four-helix bundle has been designed to catalyze the hydrolysis of phosphodiesters. The active site on the surface of the folded catalyst is composed of two histidine and four arginine residues, with the capacity to provide general acid, general base, and/or nucleophilic catalysis as well as transition state stabilization. Uridine 3'-2, 2, 2 trichloroethylphosphate (2) is a mimic of ...