In VivoBioconversion of Tetrahydroisoquinoline by Recombinant Coclaurine N-Methyltransferase

Coclaurine N-methyltransferase from Coptis japonicacatalyzes the N-methylation of coclaurine as well as simple tetrahydroisoquinoline. We examined the possibility of converting 6,7-dimethoxy-1,2,3,4-tetrahydroisoquinoline into its N-methylated product using transgenic Escherichia coli, which expressed recombinant coclaurine N-methyltransferase, without the addition of a methyl-group donor. Transgenic E. colisuccessfully N-methylated the substrate added to the medium and excreted the product. Limitation of bioconversion by the supply of methyl-group donor is discussed.