5o3n

Crystal structure of E. cloacae 3,4-dihydroxybenzoic acid decarboxylase (AroY) reconstituted with prFMN

spinqualitylabelsall models 5o3n, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5o3n is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 4LU, GOL, MN, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The utilization of CO2 as carbon source for organic syntheses meets the urgent demand of more sustainability in chemical production. Here we report on the enzyme-catalyzed para-carboxylation of catechols, employing 3,4-dihydroxybenzoic acid decarboxylases (AroY) that belong to the UbiD enzyme family. Crystal structures and accompanying solution data confirm that AroY utilizes the recently discovered prenylated FMN (prFMN) cofactor, and requires oxidative maturation to form the catalytically competent prFMNiminium species. This study reports on the in vitro reconstitution and activation of a prFMN-dependent enzyme that is capable of directly carboxylating aromatic catechol substrates under ambient conditions. A reaction mechanism for the reversible decarboxylation involving a monocovalent quinoid-cofactor intermediate is proposed, which is distinct from the prFMN associated 1,3 dipolar cycloaddition mechanism in related enzymes. Regioselective para-Carboxylation of Catechols by a Prenylated Flavin Dependent Decarboxylase.,Payer S, Marshall SA, Barland N, Sheng X, Reiter T, Dordic A, Steinkellner G, Wuensch C, Kaltwasser S, Fisher K, Rigby SEJ, Macheroux P, Vonck J, Gruber K, Faber K, Himo F, Leys D, Pavkov-Keller T, Glueck SM Angew Chem Int Ed Engl. 2017 Aug 30. doi: 10.1002/anie.201708091. PMID:28857436 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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