Expanding substrate specificity of salicylate decarboxylase by site-directed mutagenesis for expansion of the entrance region connecting to the substrate access tunnel

Kotaro Kirimura, Masahiro Araki, Mana Ishihara, Yoshitaka Ishii

    研究成果: Article査読

    抄録

    Salicylate decarboxylase (Sdc, EC 4.1.1.91) from the yeast Trichosporon moniliiforme WU-0401 catalyzes the carboxylation of phenol to salicylic acid and is applicable to enzymatic Kolbe-Schmitt reaction. Based on the 3D-modeling of Sdc, we generated a Sdc mutant, K23A-Sdc, by site-directed mutagenesis for expansion of the entrance region connecting to the substrate access tunnel. K23A-Sdc catalyzed the carboxylation of o-cresol to 3-methyl salicylic acid (3-MS), whereas Sdc showed negligible and slight activity toward o-cresol and 3-MS, respectively. Simultaneously, K23A-Sdc showed approximately 5.8-fold more decarboxylation activity toward 3-MS than Sdc. These results clearly indicate that K23A-Sdc acquired novel substrate specificity by substitution of only one amino acid residue (23rd lysine residue to alanine residue), around the substrate entrance region but not at the active center of Sdc.

    本文言語English
    ページ(範囲)58-61
    ページ数4
    ジャーナルChemistry Letters
    48
    1
    DOI
    出版ステータスPublished - 2019 1 1

    ASJC Scopus subject areas

    • Chemistry(all)

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