Structural, kinetic, and computational studies of enzymes that are perturbed by site-directed amino acid substitutions can provide fundamental information about the roles of protein motions in catalysis.
The role of the enzyme's dynamic motions in catalysis is at the center of heated contemporary debates among both theoreticians and experimentalists.
Taken together, the results of these inquiries highlight the importance of electrostatic interactions and motions in enzyme catalysis.
The role of protein motions in enzyme catalysis has been demonstrated in a wide variety of enzymes, including cyclophilin A, α-amylase, adenylate kinase, and dihydrofolate reductase (DHFR).
The role of protein motions in enzymatic catalysis is a research area of great interest where much remains to be understood (e.g., refs (1− 4)).
Among them, dihydrofolate reductase (DHFR) is a paradigm system for the study of the role of protein motions in enzyme catalysis, both experimentally and theoretically, because of the well-characterized conformational changes and the measured T dependence of the KIEs.
According to Kramers theory, solvent viscosity results in friction against proteins in solution, and this should result in decreased motion, inhibiting catalysis in motile enzymes.
Serine repeats may form a hinge structure of a protein and hinge bending motions play an important role in catalysis and protein-ligand interactions [ 61].
