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Function(s) and Biological Relevance

Benzylisoquinoline alkaloids (BIAs), plant-specialized metabolites, is the organism that forms TNMT. Tetrahydroprotoberberine N-methyltransferase (TNMT) catalyzes the N-methylation of (S)-stylopine in the pathway leading to protopines and benzo [c] phenanthridines. Also acts on (S)-canadine in a different pathway that leads to the production of phthalideisoquinolines. The substrate specificity of TNMT enzymes appears to arise from the arrangement of subgroup-specific stereospecific recognition elements relative to catalytic elements that are more widely-conserved.

Broader Implications

Structural highlights and structure-function relationships

GfTNMT was co-crystallized with the cofactor S-adenosyl-L-methionine (dmin = 1.6 A), product S-adenosyl-L-homocysteine (dmin = 1.8 A), or in complex with S-adenosyl-L-homocysteine and (S)-cis-N-methylstylopine (dmin = 1.8 A), These structures reveal for the first time how a mostly hydrophobic L-shaped substrate recognition pocket selects for the (S)-cis configuration of the two central six-membered rings in protoberberine BIA compounds.

Energy Transformation

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