DIPHOSPHOMEVALONATE DECARBOXYLASE VARIANT AND METHOD FOR PRODUCING OLEFIN COMPOUND BY USING THE SAME

摘要

Mutations involving amino acid substitution were introduced into various sites of diphosphomevalonate decarboxylase (MVD), thus preparing a large number of MVD variants. Then, the variants were each evaluated in terms of a catalytic activity for production of olefin compounds such as isoprene. As a result, it was found that substitution of glycine at position with a different amino acid resulted in improvement in the catalytic activity. In addition, it was found that the MVD in which arginine at position and threonine at position in addition to the position were further substituted with different amino acids, respectively, also had the high catalytic activity.