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Structural and Functional Studies of Pavine N-Methyltransferase from Thalictrum flavum Reveal Novel Insights into Substrate Recognition and Catalytic Mechanism.

J Biol Chem. 2016; 
Torres MA,, Hoffarth E,, Eugenio L,, Savtchouk J,, Chen X, Morris JS, Facchini PJ, Ng KK,.
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Mutagenesis Services Site-Directed Mutagenesis – Synthetic genes (Genscript) encoding three PavNMT mutants (E205A, H206A and E205A-H206A) were individually ligated into the PstI and KpnI restriction sites of the pRSETC vector for expression in E.... Synthetic genes (Genscript) encoding two additional PavNMT mutants (Y79A and E80A) were prepared using wild-type pRSET-TfPavNMT plasmid as a template. Get A Quote

摘要

Benzylisoquinoline alkaloids (BIAs) are produced in a wide variety of plants and include many common analgesic, antitussive, and anticancer compounds. Several members of a distinct family of S-adenosylmethionine (SAM)-dependent N-methyltransferases (NMTs) play critical roles in BIA biosynthesis, but the molecular basis of substrate recognition and catalysis is not known for NMTs involved in BIA metabolism. To address this issue, the crystal structure of pavine NMT from Thalictrum flavum was solved using selenomethionine-substituted protein (dmin = 2.8 Å). Additional structures were determined for the native protein (dmin = 2.0 Å) as well as binary complexes with SAM (dmin = 2.3 Å) or the reaction product S-a... More

关键词

Benzylisoquinoline alkaloid biosynthesis; enzyme kinetics; enzyme mechanism; protein structure; secondary metabolism; x-ray crystallography