Browse by author
Lookup NU author(s): Professor Paul RaceORCiD
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
© 2015 The Royal Society of Chemistry. Achieving regio-specific hydroxylation of aromatic compounds remains a major challenge in synthetic chemistry. By contrast, this transformation is readily accomplished in nature through the action of FAD-dependant monooxygenase enzymes. Here, we report the kinetic characterisation of one such enzyme, TropB, from the stipitatic acid biosynthetic pathway. Analogues of the TropB natural substrate, 3-methyl-orcinaldehyde, were synthesised and used to examine the substrate selectivity of this enzyme. TropB displays broad substrate tolerance, for instance accepting single-ring aromatic substrates containing a range of C-1 substituents with varying electronic and steric properties. These include nitro, nitrosyl, alkyl, and aryl keto groups. Bicyclic substrates, however, were rejected by TropB. Additionally, C-5 substituents on single-ring aromatic substrates were not tolerated whereas the presence of a 6-methyl group was found to be important for substrate binding. Docking studies were employed to investigate and understand the broad substrate selectivity of TropB and identifies the key structural elements of its substrates. Our work has shown that TropB is an attractive target for biocatalyst engineering and industrial aromatic hydroxylation.
Author(s): Abood A, Al-Fahad A, Scott A, Hosny AE-DMS, Hashem AM, Fattah AMA, Race PR, Simpson TJ, Cox RJ
Publication type: Article
Publication status: Published
Journal: RSC Advances
Year: 2015
Volume: 5
Issue: 62
Pages: 49987-49995
Online publication date: 29/05/2015
Acceptance date: 27/05/2015
ISSN (electronic): 2046-2069
Publisher: Royal Society of Chemistry
URL: https://doi.org/10.1039/c5ra06693j
DOI: 10.1039/c5ra06693j
Altmetrics provided by Altmetric
