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|Title:||Monooxygenase, a Novel Beta-Cypermethrin Degrading Enzyme from Streptomyces sp||Authors:||Chen S.
amino acid sequence
amino terminal sequence
Mixed Function Oxygenases
Molecular Sequence Data
Sequence Analysis, DNA
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
|Issue Date:||2013||Citation:||Chen S., Lin Q., Xiao Y., Deng Y., Chang C., Zhong G., Hu M., Zhang L.-H. (2013). Monooxygenase, a Novel Beta-Cypermethrin Degrading Enzyme from Streptomyces sp. PLoS ONE 8 (9) : e75450. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0075450||Abstract:||The widely used insecticide beta-cypermethrin has become a public concern because of its environmental contamination and toxic effects on mammals. In this study, a novel beta-cypermethrin degrading enzyme designated as CMO was purified to apparent homogeneity from a Streptomyces sp. isolate capable of utilizing beta-cypermethrin as a growth substrate. The native enzyme showed a monomeric structure with a molecular mass of 41 kDa and pI of 5.4. The enzyme exhibited the maximal activity at pH 7.5 and 30°C. It was fairly stable in the pH range from 6.5-8.5 and at temperatures below 10°C. The enzyme activity was significantly stimulated by Fe2+, but strongly inhibited by Ag+, Al3+, and Cu2+. The enzyme catalyzed the degradation of beta-cypermethrin to form five products via hydroxylation and diaryl cleavage. A novel beta-cypermethrin detoxification pathway was proposed based on analysis of these products. The purified enzyme was identified as a monooxygenase by matrix-assisted laser desorption/ionization time-of-flight/time-of-flight mass spectrometry analysis (MALDI-TOF-MS) and N-terminal protein sequencing. Given that all the characterized pyrethroid-degrading enzymes are the members of hydrolase family, CMO represents the first pyrethroid-degrading monooxygenase identified from environmental microorganisms. Taken together, our findings depict a novel pyrethroid degradation mechanism and indicate that the purified enzyme may be a promising candidate for detoxification of beta-cypermethrin and environmental protection. © 2013 Chen et al.||Source Title:||PLoS ONE||URI:||https://scholarbank.nus.edu.sg/handle/10635/161463||ISSN:||1932-6203||DOI:||10.1371/journal.pone.0075450|
|Appears in Collections:||Staff Publications|
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