Characterization of a Linuron-Specific Amidohydrolase from the Newly Isolated Bacterium Sphingobium sp. Strain SMB.

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ID: 101142
2020
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Abstract
The phenylurea herbicide linuron is globally used and has caused considerable concern due to its 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 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.
Reference Key
zhang2020characterizationjournal Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Zhang, Long;Hu, Qiang;Liu, Bin;Li, Feng;Jiang, Jian-Dong;
Journal Journal of agricultural and food chemistry
Year 2020
DOI
10.1021/acs.jafc.0c00597
URL
Keywords
Epidemiology fungi field crops disease warning systems oilseeds and legumes

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