In vivo bioconversion of tetrahydroisoquinoline by recombinant coclaurine N-methyltransferase.
Coclaurine N-methyltransferase from Coptis japonica catalyzes 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. coli successfully N-methylated the substrate added to the medium and excreted the product. Limitation of bioconversion by the supply of methyl-group donor is discussed.
Morishige
Takashi
T
Division of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Japan.
Choi
Kum-Boo
KB
Sato
Fumihiko
F
D001711:Biotransformation; D039323:Coptis / Q000201:enzymology* / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics; D013058:Mass Spectrometry; D008780:Methyltransferases / Q000235:genetics / Q000378:metabolism*; D015394:Molecular Structure; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D044005:Tetrahydroisoquinolines / Q000737:chemistry / Q000378:metabolism*
D011994:Recombinant Proteins; D044005:Tetrahydroisoquinolines; D008780:Methyltransferases; C430217:S-adenosyl-L-methionine coclaurine N-methyltransferase