Genome mining reveals new bacterial type I Baeyer-Villiger monooxygenases with (bio)synthetic potential

• Published in: Molecular catalysis Vol. 486; p. 110875
• Main Authors: Ceccoli, Romina D., Bianchi, Dario A., Carabajal, María Ayelén, Rial, Daniela V.
• Format: Journal Article
• Language: English
• Published: Elsevier B.V 01.05.2020
• Subjects: Baeyer-Villiger monooxygenases; Biocatalysis; Biotransformations; Flavoenzymes; Ketone biooxidation; Biocatalysis; Baeyer-Villiger monooxygenases; Ketone biooxidation; Flavoenzymes; Biotransformations
• ISSN: 2468-8231; 2468-8231
• DOI: 10.1016/j.mcat.2020.110875

[Display omitted] •Seven putative type I BVMOs were identified in Bradyrhizobium diazoefficiens.•Phylogenetic relationships were established with available BVMOs.•Three of them were functionally expressed in Escherichia coli for the first time.•The activity and the stability of the three pure BVMOs were investigated.•They showed different substrate profile and particular regioselectivity. Baeyer-Villiger monooxygenases (BVMOs) are oxidorreductases that catalyze the oxidation of ketones in a very selective manner. By genome mining we detected seven putative type I BVMOs in Bradyrhizobium diazoefficiens USDA 110. As we established the phylogenetic relationships among them and with other type I BVMOs, we found out that they belong to different clades of the phylogenetic tree. Thus, we decided to clone and heterologously express five of them. Three of them, each one from a divergent phylogenetic group, were obtained as soluble proteins, allowing us to proceed with their biocatalytic assessment and enzymatic characterization. As to substrate scope and selectivity, we observed a complementary behavior among the three BVMOs. BVMO2 was the more versatile biocatalyst in whole-cell systems while BVMO4 and BVMO5 showed a narrow substrate profile with preference for linear ketones and particular regioselectivity for (±)-cis-bicyclo[3.2.0]hept-2-en-6-one.