Structure-function studies of tetrahydroprotoberberine N-methyltransferase reveal the molecular basis of stereoselective substrate recognition.

ABSTRACT: Benzylisoquinoline alkaloids (BIAs) are a structurally diverse class of plant-specialized metabolites that have been particularly well-studied in the order Ranunculales. The N-methyltransferases (NMTs) in BIA biosynthesis can be divided into three groups according to substrate specificity and amino acid sequence. Here, we report the first crystal structures of enzyme complexes from the tetrahydroprotoberberine NMT (TNMT) subclass, specifically for GfTNMT from the yellow horned poppy (Glaucium flavum). GfTNMT was co-crystallized with the cofactor S-adenosyl-l-methionine (d_min = 1.6 Å), the product S-adenosyl-l-homocysteine (d_min = 1.8 Å), or in complex with S-adenosyl-l-homocysteine and (S)-cis-N<

SUBMITTER: Lang DE 

PROVIDER: S-EPMC6779432 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature