| abstract |
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 152 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 74 and threonine at position 209 in addition to the position 152 were further substituted with different amino acids, respectively, also had the high catalytic activity. |