Evolution study of the Baeyer-Villiger monooxygenases enzyme family: functional importance of the highly conserved residues.

Baeyer-Villiger monooxygenases (BVMOs) catalyze the transformation of linear and cyclic ketones into their corresponding esters and lactones by introducing an oxygen atom into a C-C bond. This bioreaction has numerous advantages compared to its chemical version; it does not induce the use of potentially harmful reagents (i.e., green chemistry) and displays significant better enantio- and regio-selectivity. New potential BVMOs were searched using sequence homology for type I BVMO proteins. 116 new sequences were identified as new putative BVMOs respecting the defined selection criteria. Multiple sequence alignments were carried out on the selected sequences to study the conservation of structurally and/or functionally important amino acids during evolution. Type I BVMO signature motif was found to be conserved in 94.8% of the sequences. We noticed also the highly conserved - but previously unnoticed - Threonine 167 (93.1%), located in the signature motif; this position could be added in the pattern used to characterize specific Type I enzymes. Amino acids at the vicinity of the FAD and NADPH cofactors were found also to be highly conserved and the details of the interactions were emphasized. Interestingly, residues at the enzyme binding site were found less conserved in terms of sequence evolution, leading sometimes to some important amino acid changes. These behaviors could explain the enzyme selectivity and specificity for different ligands.

Keywords

sequence alignment phylogeny protein structure function interactions enentioselectivity stereoselectivity lactones ketones esters lactones.

Domains

Life Sciences [q-bio] Biochemistry, Molecular Biology Life Sciences [q-bio] Biotechnology Computer Science [cs] Biotechnology Life Sciences [q-bio] Quantitative Methods [q-bio.QM] Life Sciences [q-bio] Pharmaceutical sciences Life Sciences [q-bio] Toxicology Chemical Sciences Catalysis Chemical Sciences Organic chemistry Computer Science [cs] Bioinformatics [q-bio.QM]

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https://www.hal.inserm.fr/inserm-00926584

Submitted on : Thursday, January 9, 2014-6:30:43 PM

Last modification on : Saturday, June 25, 2022-8:27:22 PM

Long-term archiving on: Thursday, April 10, 2014-12:01:26 PM

Dates and versions

inserm-00926584 , version 1 (09-01-2014)

Identifiers

HAL Id : inserm-00926584 , version 1
DOI : 10.1016/j.biochi.2013.03.005
PUBMED : 23523772

Cite

Joseph Rebehmed, Véronique Alphand, Véronique de Berardinis, Alexandre de Brevern. Evolution study of the Baeyer-Villiger monooxygenases enzyme family: functional importance of the highly conserved residues.. Biochimie, 2013, 95 (7), pp.1394-402. ⟨10.1016/j.biochi.2013.03.005⟩. ⟨inserm-00926584⟩

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