Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0075450
Title: Monooxygenase, a Novel Beta-Cypermethrin Degrading Enzyme from Streptomyces sp
Authors: Chen S.
Lin Q.
Xiao Y.
Deng Y.
Chang C.
Zhong G.
Hu M.
Zhang L.-H. 
Keywords: aluminum
beta cypermethrin
cipermethrin
cupric ion
ferrous ion
hydrolase
pyrethroid
silver
unclassified drug
unspecific monooxygenase
amino acid sequence
amino terminal sequence
article
catalysis
chemical modification
controlled study
degradation
detoxification
enzyme activation
enzyme activity
enzyme purification
enzyme structure
fungus growth
fungus isolation
hydroxylation
microorganism
molecular weight
nonhuman
pH
protein family
Streptomyces
temperature
Base Sequence
Environmental Pollution
Hydrogen-Ion Concentration
Insecticides
Metals, Heavy
Mixed Function Oxygenases
Molecular Sequence Data
Molecular Weight
Pyrethrins
Sequence Analysis, DNA
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Streptomyces
Temperature
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
Elements

Show full item record
Files in This Item:
File Description SizeFormatAccess SettingsVersion 
10_1371_journal_pone_0075450.pdf557.37 kBAdobe PDF

OPEN

PublishedView/Download

SCOPUSTM   
Citations

14
checked on Jan 21, 2020

Page view(s)

25
checked on Jan 23, 2020

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.