Abstract
A novel strategy for enhancing the activity and stability of metal-activated enzymes by allosteric control and confinement of metal-nulceobase hybrid coordination was reported in this study. Despite the lack of active Mg2+ ions, methionine adenosyltransferase (MAT) immobilized by Zn2(adenine) still exhibited robust catalytic activity and stability at pH 3 and 80 °C.
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