In silico studies based on homology modeling, docking and MD simulations predicted ( S)-norlaudanine as the potential substrate forming a stable complex with Ps3′OMT.
Comparison of transcript and metabolite profiles of high and low papaverine producing cultivar revealed the occurrence of a 3′ O-methyltransferase, Ps3′OMT, which was abundant in aerial organs and shared 72% identity with the GfLOMT7 predicted to have 3′OMT activity. In this study, we report the identification and functional characterization of 3′ O-methyltransferase (Ps3′OMT) which might participate in the 3′ O-methylation of the intermediates in the papaverine biosynthesis. In addition, there are several intermediate steps in both the proposed pathways that are not very well characterized in terms of specific enzymes. Papaverine biosynthesis has remained debatable as two different pathways, NH (involving N-desmethylated intermediates) and the NCH 3 (involving N-methylated intermediates), have been proposed. Papaverine, one of the benzylisoquinoline alkaloids (BIA) synthesized in the medicinally important plant, Papaver somniferum, is known for the potent pharmacological properties. Using, in silico, in vitro and in planta functional assays, we demonstrate that Ps3′OMT, an 3′- O methyl transferase is linked to papaverine biosynthesis in opium poppy.
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