Abstract: A method enables olefin compound production with a high productivity, and an enzyme is used in the method. Mutations involving amino acid substitution are introduced into various sites of diphosphomevalonate decarboxylase (MVD) to prepare multiple MVD variants. Then, these variants are evaluated in terms of catalytic activity for producing an olefin compound such as isoprene, and have found as a result that the catalytic activity is improved when serine at position 153 and threonine at position 209 are each substituted with a different amino acid. In addition, the catalytic activity of the variants is further improved when glycine at position 152 is further substituted with a different amino acid.

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 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.

Abstract: A method which enables olefin compound production with a high productivity and an enzyme used in the method, a mutation involving amino acid substitution has been introduced into various sites of diphosphomevalonate decarboxylase (MVD), thus preparing a large number of MVD variants. Next, the result of evaluating the variants for the catalytic activity related to the production of olefin compounds such as isoprene has revealed that MVD whose threonine at position 209 is substituted with a different amino acid has the catalytic activity, and that MVD whose arginine at position 74 is further substituted with a different amino acid in addition to position 209 has the catalytic activity at higher levels.

Abstract: A method enables olefin compound production with a high productivity, and an enzyme is used in the method. Mutations involving amino acid substitution are introduced into various sites of diphosphomevalonate decarboxylase (MVD) to prepare multiple MVD variants. Then, these variants are evaluated in terms of catalytic activity for producing an olefin compound such as isoprene, and have found as a result that the catalytic activity is improved when serine at position 153 and threonine at position 209 are each substituted with a different amino acid. In addition, the catalytic activity of the variants is further improved when glycine at position 152 is further substituted with a different amino acid.

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 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.

Abstract: A method which enables olefin compound production with a high productivity and an enzyme used in the method, a mutation involving amino acid substitution has been introduced into various sites of diphosphomevalonate decarboxylase (MVD), thus preparing a large number of MVD variants. Next, the result of evaluating the variants for the catalytic activity related to the production of olefin compounds such as isoprene has revealed that MVD whose threonine at position 209 is substituted with a different amino acid has the catalytic activity, and that MVD whose arginine at position 74 is further substituted with a different amino acid in addition to position 209 has the catalytic activity at higher levels.