Abstract
Biological molecular motors use chemical free energy to drive mechanical motion in a specific direction. This function appears to require high molecular complexity, and it is interesting to consider how the evolutionary leap from non-motor enzymes to molecular motors occurred. Here, atomistic simulations coupled with kinetic modeling show that conformational switching of non-motor enzymes, induced by substrate binding and catalysis, induces motor-like, directional torsional motions, as well as oar-like, reciprocating motions, which should be detectable experimentally. Such directional motions in the earliest enzymes would have been starting point for the evolution of motor proteins. Additionally, driven molecular motions in catalytically active enzymes may help explain why the apparent diffusion constants of some enzymes increase with enzyme velocity (1–3).
One Sentence Summary Analysis of protein simulations shows that catalytically active nonmotor enzymes can execute motor-like motions.