Regiospecificity and kinetic properties of a plant natural product O-methyltransferase are determined by its N-terminal domain.

A recently discovered, S-adenosyl-L-methionine and bivalent cation-dependent O-methyltransferase from the ice plant, Mesembryanthemum crystallinum, is involved in the methylation of various flavonoid and phenylpropanoid conjugates. Differences in regiospecificity as well as altered kinetic properties of the recombinant as compared to the native plant O-methyltransferase can be attributed to differences in the N-terminal part of the protein. Upon cleavage of the first 11 amino acids, the recombinant protein displays essentially the same substrate specificity as observed earlier for the native plant enzyme. Product formation of the newly designed, truncated recombinant enzyme is consistent with light-induced accumulation of methylated flavonoid conjugates in the ice plant. Therefore, substrate affinity and regiospecificity of an O-methyltransferase in vivo and in vitro can be controlled by cleavage of an N-terminal domain.