6gkz

Crystal structure of Coclaurine N-Methyltransferase (CNMT) bound to N-methylheliamine and SAH

spinqualitylabelsall models 6gkz, resolution 2.43Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6gkz is a 4 chain structure with sequence from Coptis japonica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.43Å Ligands: MSE, SAH Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q948P7_COPJA Publication Abstract from PubMed Benzylisoquinoline alkaloids (BIAs) are a structurally diverse family of plant secondary metabolites which have been exploited to develop analgesics, antibiotics, antitumor agents and other therapeutic agents. Biosynthesis of BIAs proceeds via a common pathway from tyrosine to (S)-reticulene at which point the pathway diverges. Coclaurine N-methyltransferase (CNMT) is a key enzyme in the pathway to (S)-reticulene, installing the N-methyl substituent that is essential for the bioactivity of many BIAs. In this paper, we describe the first crystal structure of CNMT which, along with mutagenesis studies, defines the enzymes active site architecture. The specificity of CNMT was also explored with a range of natural and synthetic substrates as well as co-factor analogues. Knowledge from this study could be used to generate improved CNMT variants required to produce BIAs or synthetic derivatives. Structure and Biocatalytic Scope of Coclaurine N-Methyltransferase.,Bennett M, Thompson M, Shepherd S, Dunstan M, Herbert A, Smith D, Cronin V, Menon B, Levy C, Micklefield J Angew Chem Int Ed Engl. 2018 May 23. doi: 10.1002/anie.201805060. PMID:29791083 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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