ORCID Profile
0000-0003-3138-066X
Current Organisations
University of Sydney
,
University of Oxford
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Publisher: Elsevier BV
Date: 03-2023
Publisher: American Chemical Society (ACS)
Date: 17-02-2021
Publisher: Springer Science and Business Media LLC
Date: 17-06-2015
DOI: 10.1038/NATURE14559
Publisher: Springer Science and Business Media LLC
Date: 20-08-2021
DOI: 10.1038/S41467-021-25278-Z
Abstract: The widespread UbiD enzyme family utilises the prFMN cofactor to achieve reversible decarboxylation of acrylic and (hetero)aromatic compounds. The reaction with acrylic compounds based on reversible 1,3-dipolar cycloaddition between substrate and prFMN occurs within the confines of the active site. In contrast, during aromatic acid decarboxylation, substantial rearrangement of the substrate aromatic moiety associated with covalent catalysis presents a molecular dynamic challenge. Here we determine the crystal structures of the multi-subunit vanillic acid decarboxylase VdcCD. We demonstrate that the small VdcD subunit acts as an allosteric activator of the UbiD-like VdcC. Comparison of distinct VdcCD structures reveals domain motion of the prFMN-binding domain directly affects active site architecture. Docking of substrate and prFMN-adduct species reveals active site reorganisation coupled to domain motion supports rearrangement of the substrate aromatic moiety. Together with kinetic solvent viscosity effects, this establishes prFMN covalent catalysis of aromatic (de)carboxylation is afforded by UbiD dynamics.
Publisher: Springer Science and Business Media LLC
Date: 16-09-2019
Publisher: Elsevier BV
Date: 10-2020
Publisher: Elsevier BV
Date: 08-2023
Publisher: Coventry University, Lanchester Library
Date: 31-07-2019
Location: United Kingdom of Great Britain and Northern Ireland
Location: United Kingdom of Great Britain and Northern Ireland
No related grants have been discovered for Laura Di Michele.