Mechanism-based Inhibition Reveals Transitions between Two Conformational States in the Action of Lysine 5,6-Aminomutase: A Combination of Electron Paramagnetic Resonance Spectroscopy, Electron Nuclear Double Resonance Spectroscopy, and Density Functional Theory Study

An "open"-state crystal structure of lysine 5,6-aminomutase suggests that transition to a hypothetical "closed"-state is required to bring the cofactors adenosylcobalamin (AdoCbl) and pyridoxal-5′-phosphate (PLP) and the substrate into proximity for the radical-mediated 1,2-amino group migration. Th...

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Publicado en:	Journal of the American Chemical Society Vol. 135; no. 2; pp. 788 - 795
Autores principales:	Yung-Han Chen, Maity, Amarendra N., Frey, Perry A., Shyue-Chu Ke
Formato:	Artículo
Publicado:	American Chemical Society 1/16/2013
Materias:	Lysine Electron paramagnetic resonance spectroscopy Electron nuclear double resonance spectroscopy Density functionals Conformational analysis
Acceso en línea:	Ver este registro en EBSCOhost