Structural basis for the selective addition of an oxygen atom to cyclic ketones by Baeyer-Villiger monooxygenase from Parvibaculum lavamentivorans
- 주제(키워드) Baeyer-villiger monooxygenase , BVMOParvi , BVMOOcean , Bulge
- 주제(기타) Biochemistry & Molecular Biology; Biophysics
- 설명문(일반) [Tien Duc Nguyen; Gu, Do-Heon; Seo, Pil-Won; Kim, Ji-Won; Kim, Jeong-Sun] Chonnam Natl Univ, Dept Chem, Gwangju 61186, South Korea; [Choi, Go-Eun; Park, Jin-Byung] Ewha Womans Univ, Dept Food Sci & Engn, Seoul 03760, South Korea
- 등재 SCIE, SCOPUS
- 발행기관 ACADEMIC PRESS INC ELSEVIER SCIENCE
- 발행년도 2019
- URI http://www.dcollection.net/handler/ewha/000000160061
- 본문언어 영어
- Published As http://dx.doi.org/10.1016/j.bbrc.2019.03.114
- PubMed https://pubmed.ncbi.nlm.nih.gov/30914200
초록/요약
Baeyer-Villiger monooxygenase (BVMO) catalyzes insertion of an oxygen atom into aliphatic or cyclic ketones with high regioselectivity. The BVMO5 from Parvibaculum lavamentivorans (BVMOParvi) and Oceanicola batsensis (BVMOOcean) 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 BVMOParvi structure shows that BVMOParvi forms a two-domain structure like other BVMOs. It has two inserted residues, compared with BVMOOcean, that form a bulge near the bound flavin adenine dinucleotide in the active site. Furthermore, this bulge is linked to a nearby alpha-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 BVMOParvi, and Ser-Thr in BVMOOcean) allows a large volume in BVMOParvi 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. (C) 2019 Elsevier Inc. All rights reserved.
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