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: RTâPCR experiments were performed on the total RNA extracted from A.âradioresistens S13 grown in minimal medium supplemented with C14, C16 (mediumâchainâlength alkanes) and C24, C36 (longâchainâlength alkanes) as the sole energy and carbon source and from bacteria grown in the presence of sodium acetate. Using the two sets of almaâ and alkBâspecific primers an amplified product of the expected size (499 and 466âbp respectively) was obtained only with RNA extracted from S13 grown with mediumâchain alkanes in the case of ALK primers (Fig.â6), and on RNA extracted from bacteria grown on longâchain alkanes when BVMO primers were used. No amplified product was obtained from the RNA of bacteria grown with sodium acetate or from the RTânegative controls. An amplified fragment of the expected size was also obtained using the A.âradioresistens S13 16S rDNAâspecific primers on the RNA of the bacterium grown in the presence of mediumâ and longâchainâlength alkanes and sodium acetate.
Affiliation: Department of Life Sciences and Systems Biology, University of Torino, via Accademia Albertina 13, 10123 Torino, Italy.