Kinetic characterisation of the FAD dependent monooxygenase TropB and investigation of its biotransformation potential

Abood, Amira, Al-Fahad, Ahmed, Scott, Alan, Hosny, Alaa El-Dein M. S., Hashem, Amal M., Fattah, Azza M. A., Race, Paul R., Simpson, Thomas J. and Cox, Russell J. 2015. Kinetic characterisation of the FAD dependent monooxygenase TropB and investigation of its biotransformation potential. RSC Advances 5 (62) , pp. 49987-49995. 10.1039/C5RA06693J

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Abstract

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 FADdependant 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-methylorcinaldehyde, 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.

Item Type:	Article
Date Type:	Published Online
Status:	Published
Schools:	Chemistry
Publisher:	Royal Society of Chemistry
ISSN:	2046-2069
Date of Acceptance:	27 May 2015
Last Modified:	05 Nov 2021 02:51
URI:	https://orca.cardiff.ac.uk/id/eprint/122790

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