3gsy

Structure of berberine bridge enzyme in complex with dehydroscoulerine

spinqualitylabelsall models 3gsy, resolution 1.63Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3gsy is a 1 chain structure with sequence from Eschscholzia californica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BMA, DEH, FAD, MG, NAG Related: 3d2d, 3d2h, 3d2j, 3fw9, 3fw7, 3fw8 Gene: BBE1 (Eschscholzia californica) Activity: Reticuline oxidase, with EC number 1.21.3.3 Resources: FirstGlance, OCA, RCSB, PDBsum Function [RETO_ESCCA] Essential to the formation of benzophenanthridine alkaloids in the response of plants to pathogenic attack. Catalyzes the stereospecific conversion of the N-methyl moiety of (S)-reticuline into the berberine bridge carbon of (S)-scoulerine. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Berberine bridge enzyme catalyzes the stereospecific oxidation and carbon-carbon bond formation of (S)-reticuline to (S)-scoulerine. In addition to this type of reactivity the enzyme can further oxidize (S)-scoulerine to the deeply red protoberberine alkaloid dehydroscoulerine albeit with a much lower rate of conversion. In the course of the four electron oxidation, no dihydroprotoberberine species intermediate was detectable suggesting that the second oxidation step leading to aromatization proceeds at a much faster rate. Performing the reaction in the presence of oxygen and under anoxic conditions did not affect the kinetics of the overall reaction suggesting no strict requirement for oxygen in the oxidation of the unstable dihydroprotoberberine intermediate. In addition to the kinetic characterization of this reaction we also present a structure of the enzyme in complex with the fully oxidized product. Combined with information available for the binding modes of (S)-reticuline and (S)-scoulerine a possible mechanism for the additional oxidation is presented. This is compared to previous reports of enzymes ((S)-tetrahydroprotoberberine oxidase and canadine oxidase) showing a similar type of reactivity in different plant species. Berberine bridge enzyme catalyzes the six electron oxidation of (S)-reticuline to dehydroscoulerine.,Winkler A, Puhl M, Weber H, Kutchan TM, Gruber K, Macheroux P Phytochemistry. 2009 Jun;70(9):1092-7. Epub 2009 Jun 29. PMID:19570558 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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