The molecular mechanism of the open–closed protein conformational cycle transitions and coupled substrate binding, activation and product release events in lysine 5,6-aminomutase

Abstract

How a protein domain motion is coupled to the catalytic cycle is a current subject in enzymology. We render down a complicated domain motion in the 5′-deoxyadenosylcobalamin and pyridoxal-5′-phosphate codependent radical enzyme, lysine 5,6-aminomutase, into dominant contributions from Lys370α and Asp298α to the critical Co–C bond cleavage trigger and open–closed cycle transitions.