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Characterization of a Linuron-Specific Amidohydrolase from the Newly Isolated Bacterium Sphingobium sp. Strain SMB
- Source :
- Journal of Agricultural and Food Chemistry. 68:4335-4345
- Publication Year :
- 2020
- Publisher :
- American Chemical Society (ACS), 2020.
-
Abstract
- The phenylurea herbicide linuron is globally used and has caused considerable concern because it leads to environmental pollution. In this study, a highly efficient linuron-transforming strain Sphingobium sp. SMB was isolated, and a gene (lahB) responsible for the hydrolysis of linuron to 3,4-dichloroaniline and N,O-dimethylhydroxylamine was cloned from the genome of strain SMB. The lahB gene encodes an amidohydrolase, which shares 20-53% identity with other biochemically characterized amidohydrolases, except for the newly reported linuron hydrolase Phh (75%). The optimal conditions for the hydrolysis of linuron by LahB were determined to be pH 7.0 and 30 °C, and the Km value of LahB for linuron was 37.3 ± 1.2 μM. Although LahB and Phh shared relatively high identity, LahB exhibited a narrow substrate spectrum (specific for linuron) compared to Phh (active for linuron, diuron, chlortoluron, etc.). Sequence analysis and site-directed mutagenesis revealed that Ala261 of Phh was the key amino acid residue affecting the substrate specificity. Our study provides a new amidohydrolase for the specific hydrolysis of linuron.
- Subjects :
- 0106 biological sciences
Strain (chemistry)
Amidohydrolase
biology
010401 analytical chemistry
Environmental pollution
General Chemistry
biology.organism_classification
01 natural sciences
0104 chemical sciences
Hydrolysis
chemistry.chemical_compound
chemistry
Biochemistry
Hydrolase
Chlortoluron
General Agricultural and Biological Sciences
Site-directed mutagenesis
Bacteria
010606 plant biology & botany
Subjects
Details
- ISSN :
- 15205118 and 00218561
- Volume :
- 68
- Database :
- OpenAIRE
- Journal :
- Journal of Agricultural and Food Chemistry
- Accession number :
- edsair.doi...........c09a413a185e13a1823e4a713bd6cdec