Baeyer-Villiger monooxygenase (BVMO) catalyzes insertion of an oxygen atom into aliphatic or cyclic ketones with high regioselectivity. The BVMOs from Parvibaculum lavamentivorans (BVMO Parvi ) and Oceanicola batsensis (BVMO Ocean ) are interesting because of their homologies, with >40% sequence identity, and reaction with the same cyclic ketones with a methyl moiety to give different products. The revealed BVMO Parvi structure shows that BVMO Parvi forms a two-domain structure like other BVMOs. It has two inserted residues, compared with BVMO Ocean , that form a bulge near the bound flavin adenine dinucleotide in the active site. Furthermore, this bulge is linked to a nearby α-helix via a disulfide bond, probably restricting access of the bulky methyl group of the substrate to this bulge. Another sequence motif at the entrance of the active site (Ala-Ser in BVMO Parvi and Ser-Thr in BVMO Ocean ) allows a large volume in BVMO Parvi . These minute differences may discriminate a substrate orientation in both BVMOs from the initial substrate binding pocket to the final oxygenation site, resulting in the inserted oxygen atom being in different positions of the same substrate.
|Number of pages
|Biochemical and Biophysical Research Communications
|Published - 7 May 2019
Bibliographical noteFunding Information:
The X-ray diffraction experiments were performed with Beamline 11C at the Pohang Accelerator in Korea. This work was supported by Basic Science Research programs (NRF Grant Number: 2017R1D1A3B03032278 ) of the National Research Foundation of Korea funded by the Ministry of Education, Science and Technology of Korea (MEST).
© 2019 Elsevier Inc.
- Baeyer-villiger monooxygenase