Fig. 1 in Site-directed mutagenesis of β sesquiphellandrene synthase enhances enzyme promiscuity

Fig. 1. Superimposition of PmSTS homology model (green) with the crystal structure of Nicotiana tabacum 5-epi-aristolochene synthase (NtEAS, PDB ID:3M01). NtEAS has a FPP ligand analog (2-trans, 6-trans)-2- fluorofarnesyl diphosphate (FPF) bound in the active site (pink) shows an RMSD of 1.4 Å over 518 aligned Cα atoms. The Mg2+ ions in the active site of NtEAS are shown in yellow spheres. PmSTS and NtEAS share ~38% sequence identify. The putative active residues of PmSTS (W286, Y390, L454 and V466) shown heavier sticks were selected for mutagenesis studies. The structure superimposition was carried out using SSM in COOT (Emsley et al., 2010). (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)Published as part of Ker, De-Sheng, Chan, Kok Gan, Othman, Roohaida, Hassan, Maizom & Ng, Chyan Leong, 2020, Site-directed mutagenesis of β sesquiphellandrene synthase enhances enzyme promiscuity, pp. 1-10 in Phytochemistry (112286) 173 on page 2, DOI: 10.1016/j.phytochem.2020.112286, http://zenodo.org/record/829441