Please use this identifier to cite or link to this item: https://dspace.ctu.edu.vn/jspui/handle/123456789/5299
Title: Expanded insecticide catabolic activity gained by a single nucleotide substitution in a bacterial carbamate hydrolase gene
Authors: Ozturk, Basak
Nguyễn, Thị Phi Oanh
Ghequire, Maarten
Mot, Rene De
Springael, Dirk
Wattiez, Ruddy
Issue Date: 2016
Series/Report no.: Environmental Microbiology;18 .- p.4878–4887
Abstract: Carbofuran-mineralizing strain Novosphingobium sp. KN65.2 produces the CfdJ enzyme that converts the N-methylcarbamate insecticide to carbofuran phenol. Purified CfdJ shows a remarkably low KM towards carbofuran. Together with the carbaryl hydrolase CehA of Rhizobium sp. strain AC100, CfdJ represents a new protein family with several uncharacterized bacterial members outside the proteobacteria. Although both enzymes differ by only four amino acids, CehA does not recognize carbofuran as a substrate whereas CfdJ also hydrolyzes carbaryl. None of the CfdJ amino acids that differ from CehA were shown to be silent regarding carbofuran hydrolytic activity but one particular amino acid substitution, i.e., L152 to F152, proved crucial. CfdJ is more efficient in degrading methylcarbamate pesticides with an aromatic side chain whereas CehA is more efficient in degrading the oxime carbamate nematicide oxamyl. The presence of common flanking sequences suggest that the cfdJ gene is located on a remnant of the mobile genetic element Tnceh carrying cehA. Our results suggest that these enzymes can be acquired through horizontal gene transfer and can evolve to degrade new carbamate substrates by limited amino acid substitutions. We demonstrate that a carbaryl hydrolase can gain the additional capacity to degrade carbofuran by a single nucleotide transversion.
URI: http://localhost:8080//jspui/handle/123456789/5299
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