title: 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.
authors.affiliation: Physics Department, National Dong Hwa University, Hualien, Taiwan 97401. ke@mail.ndhu.edu.tw.
authors.forename: Hsin-Hsi
authors.initials: HH
authors.lastname: Lo
authors.forename: Hsin-Hua
authors.initials: HH
authors.lastname: Lin
authors.forename: Amarendra Nath
authors.initials: AN
authors.lastname: Maity
authors.forename: Shyue-Chu
authors.initials: SC
authors.lastname: Ke
mesh_terms: D001665:Binding Sites; D055162:Biocatalysis; D047991:Acetoanaerobium sticklandii / Q000201:enzymology; D019751:Intramolecular Transferases / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D011789:Quantum Theory
chemical_list: D019751:Intramolecular Transferases; C403167:D-lysine 5,6-aminomutase