Targeted metabolite and transcript profiling for elucidating enzyme function: isolation of novel N-methyltransferases from three benzylisoquinoline alkaloid-producing species.
Broad substrate specificity for (RS)-1-benzyl-1,2,3,4-tetrahydroisoquinolines; including coclaurine, norcoclaurine, isococlaurine, norarmepavine, norreticuline and tetrahydropapaverine. Both R- and S-enantiomers are methylated. The enzyme participates in the pathway leading to benzylisoquinoline alkaloid synthesis in plants. The physiological substrate is likely to be coclaurine. The enzyme was earlier termed norreticuline N-methyltransferase. However, norreticuline has not been found to occur in nature and that name does not reflect the broad specificity of the enzyme for (RS)-1-benzyl-1,2,3,4-tetrahydroisoquinolines.
Purification and characterization of three isoforms of S-adenosyl-L-methionine: (R,S)-tetrahydrobenzyl-isoquinoline N-methyltransferase from Berberis koetineana cell cultures.
