» Articles » PMID: 26161776

The Origin and Evolution of Baeyer-Villiger Monooxygenases (BVMOs): An Ancestral Family of Flavin Monooxygenases

Overview
Journal PLoS One
Date 2015 Jul 11
PMID 26161776
Citations 25
Authors
Affiliations
Soon will be listed here.
Abstract

The Baeyer-Villiger Monooxygenases (BVMOs) are enzymes belonging to the "Class B" of flavin monooxygenases and are capable of performing exquisite selective oxidations. These enzymes have been studied from a biotechnological perspective, but their physiological substrates and functional roles are widely unknown. Here, we investigated the origin, taxonomic distribution and evolutionary history of the BVMO genes. By using in silico approaches, 98 BVMO encoding genes were detected in the three domains of life: Archaea, Bacteria and Eukarya. We found evidence for the presence of these genes in Metazoa (Hydra vulgaris, Oikopleura dioica and Adineta vaga) and Haptophyta (Emiliania huxleyi) for the first time. Furthermore, a search for other "Class B" monooxygenases (flavoprotein monooxygenases--FMOs--and N-hydroxylating monooxygenases--NMOs) was conducted. These sequences were also found in the three domains of life. Phylogenetic analyses of all "Class B" monooxygenases revealed that NMOs and BVMOs are monophyletic, whereas FMOs form a paraphyletic group. Based on these results, we propose that BVMO genes were already present in the last universal common ancestor (LUCA) and their current taxonomic distribution is the result of differential duplication and loss of paralogous genes.

Citing Articles

Towards biotechnological production of bio-based low molecular weight esters: a patent review.

Zago M, Branduardi P, Serra I RSC Adv. 2024; 14(40):29472-29489.

PMID: 39297040 PMC: 11409443. DOI: 10.1039/d4ra04131c.


Bioenzymatic detoxification of mycotoxins.

Liu M, Zhang X, Luan H, Zhang Y, Xu W, Feng W Front Microbiol. 2024; 15:1434987.

PMID: 39091297 PMC: 11291262. DOI: 10.3389/fmicb.2024.1434987.


A bird's-eye view: exploration of the flavin-containing monooxygenase superfamily in common wheat.

Sun S, Bakkeren G Front Plant Sci. 2024; 15:1369299.

PMID: 38681221 PMC: 11046709. DOI: 10.3389/fpls.2024.1369299.


The dynamics of the flavin, NADPH, and active site loops determine the mechanism of activation of class B flavin-dependent monooxygenases.

Pierdominici-Sottile G, Palma J, Ferrelli M, Sobrado P Protein Sci. 2024; 33(4):e4935.

PMID: 38501462 PMC: 10962481. DOI: 10.1002/pro.4935.


Investigating the biochemical signatures and physiological roles of the FMO family using molecular phylogeny.

Nicoll C, Mascotti M BBA Adv. 2023; 4:100108.

PMID: 38034983 PMC: 10682829. DOI: 10.1016/j.bbadva.2023.100108.


References
1.
Choi I, Kim S . Global extent of horizontal gene transfer. Proc Natl Acad Sci U S A. 2007; 104(11):4489-94. PMC: 1815472. DOI: 10.1073/pnas.0611557104. View

2.
Weiss M, Denger K, Huhn T, Schleheck D . Two enzymes of a complete degradation pathway for linear alkylbenzenesulfonate (LAS) surfactants: 4-sulfoacetophenone Baeyer-Villiger monooxygenase and 4-sulfophenylacetate esterase in Comamonas testosteroni KF-1. Appl Environ Microbiol. 2012; 78(23):8254-63. PMC: 3497377. DOI: 10.1128/AEM.02412-12. View

3.
Forterre P . The common ancestor of archaea and eukarya was not an archaeon. Archaea. 2013; 2013:372396. PMC: 3855935. DOI: 10.1155/2013/372396. View

4.
Nasir A, Kim K, Caetano-Anolles G . Global patterns of protein domain gain and loss in superkingdoms. PLoS Comput Biol. 2014; 10(1):e1003452. PMC: 3907288. DOI: 10.1371/journal.pcbi.1003452. View

5.
Furnham N, Sillitoe I, Holliday G, Cuff A, Laskowski R, Orengo C . Exploring the evolution of novel enzyme functions within structurally defined protein superfamilies. PLoS Comput Biol. 2012; 8(3):e1002403. PMC: 3291543. DOI: 10.1371/journal.pcbi.1002403. View