76318-96-2Relevant academic research and scientific papers
PURIFICATION AND CHARACTERIZATION OF THREE ISOFORMS OF S-ADENOSYL-L-METHIONINE: (R,S)-TETRAHYDROBENZYLISOQUINOLINE-N-METHYLTRANSFERASE FROM BERBERIS KOETINEANA CELL CULTURES
Frenzel, Thomas,Zenk, Meinhart H.
, p. 3491 - 3497 (2007/10/02)
Three distinctly different isoforms of S-adenosyl-L-methionine-(R,S)-tetrahydroisoquinoline-N-methyltransferases could be isolated from cell suspension cultures of Berberis koetineana.These isoforms were designated NMT-I, -II and -III.The three enzymes have different molecular weights (60-78 * 103), pH optima (6.8/7.4), kinetic properties and substrate specificities.NMT-I showed maximal activity with (R)-tetrahydropapaverine as substrate, NMT-II and -III were most active against (R)-coclaurine.The mixture of all three NMT's was immobilized on CH-Sepharose or CPG-10 glass beads.The enzymes under these conditions retained their properties and represent a useful tool for the preparative synthesis of isotopically labelled N-methylated benzylisoquinoline alkaloids.
