Identification of a novel Baeyer-Villiger monooxygenase from Acinetobacter radioresistens: close relationship to the Mycobacterium tuberculosis prodrug activator EtaA.
Bottom Line: Phylogenetic analysis placed the sequence of this novel BVMO in the same clade of the prodrug activator ethionamide monooxygenase (EtaA) and it bears only a distant relation to the other known class I BVMO proteins.In silico analysis of the 3D model of the S13 BVMO generated by homology modelling also supports the similarities with EtaA by binding ethionamide to the active site.In vitro experiments carried out with the purified enzyme confirm that this novel BVMO is indeed capable of typical Baeyer-Villiger reactions as well as oxidation of the prodrug ethionamide.
Affiliation: Department of Life Sciences and Systems Biology, University of Torino, via Accademia Albertina 13, 10123 Torino, Italy.Show MeSH
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Mentions: A good stereochemical quality of the model was found by analysis of the geometrical parameters using the Ramachandran plot (Fig. 7A), which shows how the distribution of the ϕ and ψ angles is well comprised in the allowed regions. 86.1% of the residues are in the most favoured regions and 10.2% are in the additional allowed regions, placing the majority (96.3%) of the residues in the most favoured regions. The carbon‐α ribbon presentation of the 3D model of Ar‐BVMO is shown in Fig. 7B.
Affiliation: Department of Life Sciences and Systems Biology, University of Torino, via Accademia Albertina 13, 10123 Torino, Italy.