5ny5
The apo structure of 3,4-dihydroxybenzoic acid decarboxylases from Enterobacter cloacaeThe apo structure of 3,4-dihydroxybenzoic acid decarboxylases from Enterobacter cloacae
Structural highlights
FunctionPublication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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