The higher activity of VvROMT and its variants towards the larger phenolic styrenes can be attributed to different reasons. VvROMT wildtype and the seven variants thereof show striking differences in substrate acceptance (Scheme 3). The effects of the mutations differ between the two stilbenes, the two larger 2c and 2d and the catecholic 2b. These three groups constitute very different substrates for the enzyme. Both stilbenes have the methylated hydroxy group in meta-position. While the para-hydroxy group of 2c and 2d attacks the reactive methyl group of SAM, 2b is methylated first in meta-position.