Fig. 9 in Site-directed mutagenesis of β sesquiphellandrene synthase enhances enzyme promiscuity

Fig. 9. The homology modelling illustration of the active site of PmSTSΔ24WT and PmSTSΔ24L454G. The residue L454 and Y418 are shown as stick and coloured in purple and orange, respectively. (A) The side chain of the L454 provides steric hindrance, preventing the rotation of the Y418 toward the interior of the active site. (B) The mutation of L454G provide sufficient space to allow the Y418 to undergo rotation toward the interior of the active site and (C) thus allowing interaction with other amino acid in the active site. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)