Protein Flexibility and Stiffness Enable Efficient Enzymatic Catalysis.

ABSTRACT: The enormous rate accelerations observed for many enzyme catalysts are due to strong stabilizing interactions between the protein and reaction transition state. The defining property of these catalysts is their specificity for binding the transition state with a much higher affinity than substrate. Experimental results are presented which show that the phosphodianion-binding energy of phosphate monoester substrates is used to drive conversion of their protein catalysts from flexible and entropically rich ground states to stiff and catalytically active Michaelis complexes. These results are generalized to other enzyme-catalyzed reactions. The existence of many enzymes in flexible, entropically rich, and inactive ground states provides a mechanism for utilization of ligand-binding energy to

SUBMITTER: Richard JP 

PROVIDER: S-EPMC6396832 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature