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Structural basis for the selective addition of an oxygen atom to cyclic ketones by Baeyer-Villiger monooxygenase from Parvibaculum lavamentivorans

Title
Structural basis for the selective addition of an oxygen atom to cyclic ketones by Baeyer-Villiger monooxygenase from Parvibaculum lavamentivorans
Authors
Tien Duc NguyenChoi, Go-EunGu, Do-HeonSeo, Pil-WonKim, Ji-WonPark, Jin-ByungKim, Jeong-Sun
Ewha Authors
박진병
SCOPUS Author ID
박진병scopus
Issue Date
2019
Journal Title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
ISSN
0006-291XJCR Link

1090-2104JCR Link
Citation
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS vol. 512, no. 3, pp. 564 - 570
Keywords
Baeyer-villiger monooxygenaseBVMOParviBVMOOceanBulge
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Indexed
SCIE; SCOPUS WOS scopus
Document Type
Article
Abstract
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.
DOI
10.1016/j.bbrc.2019.03.114
Appears in Collections:
공과대학 > 식품생명공학과 > Journal papers
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