Cloning and characterization of a pyrethroid pesticide decomposing esterase gene, Est3385, from Rhodopseudomonas palustris PSB-S
Full length open reading frame of pyrethroid detoxification gene, Est3385 , contains 963 nucleotides. This gene was identified and cloned based on the genome sequence of Rhodopseudomonas palustris PSB-S available at the GneBank. The predicted amino acid sequence of Est3385 shared moderate identities...
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| Published in | Scientific reports Vol. 8; no. 1; pp. 7384 - 8 |
|---|---|
| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
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London
Nature Publishing Group UK
09.05.2018
Nature Publishing Group Nature Portfolio |
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| Abstract | Full length open reading frame of pyrethroid detoxification gene,
Est3385
, contains 963 nucleotides. This gene was identified and cloned based on the genome sequence of
Rhodopseudomonas palustris
PSB-S available at the GneBank. The predicted amino acid sequence of Est3385 shared moderate identities (30–46%) with the known homologous esterases. Phylogenetic analysis revealed that Est3385 was a member in the esterase family I. Recombinant Est3385 was heterologous expressed in
E. coli
, purified and characterized for its substrate specificity, kinetics and stability under various conditions. The optimal temperature and pH for Est3385 were 35 °C and 6.0, respectively. This enzyme could detoxify various pyrethroid pesticides and degrade the optimal substrate fenpropathrin with a
K
m and
V
max value of 0.734 ± 0.013 mmol·l
−1
and 0.918 ± 0.025 U·µg
−1
, respectively. No cofactor was found to affect Est3385 activity but substantial reduction of enzymatic activity was observed when metal ions were applied. Taken together, a new pyrethroid degradation esterase was identified and characterized. Modification of Est3385 with protein engineering toolsets should enhance its potential for field application to reduce the pesticide residue from agroecosystems. |
|---|---|
| AbstractList | Full length open reading frame of pyrethroid detoxification gene,
Est3385
, contains 963 nucleotides. This gene was identified and cloned based on the genome sequence of
Rhodopseudomonas palustris
PSB-S available at the GneBank. The predicted amino acid sequence of Est3385 shared moderate identities (30–46%) with the known homologous esterases. Phylogenetic analysis revealed that Est3385 was a member in the esterase family I. Recombinant Est3385 was heterologous expressed in
E. coli
, purified and characterized for its substrate specificity, kinetics and stability under various conditions. The optimal temperature and pH for Est3385 were 35 °C and 6.0, respectively. This enzyme could detoxify various pyrethroid pesticides and degrade the optimal substrate fenpropathrin with a
K
m and
V
max value of 0.734 ± 0.013 mmol·l
−1
and 0.918 ± 0.025 U·µg
−1
, respectively. No cofactor was found to affect Est3385 activity but substantial reduction of enzymatic activity was observed when metal ions were applied. Taken together, a new pyrethroid degradation esterase was identified and characterized. Modification of Est3385 with protein engineering toolsets should enhance its potential for field application to reduce the pesticide residue from agroecosystems. Full length open reading frame of pyrethroid detoxification gene, Est3385, contains 963 nucleotides. This gene was identified and cloned based on the genome sequence of Rhodopseudomonas palustris PSB-S available at the GneBank. The predicted amino acid sequence of Est3385 shared moderate identities (30–46%) with the known homologous esterases. Phylogenetic analysis revealed that Est3385 was a member in the esterase family I. Recombinant Est3385 was heterologous expressed in E. coli, purified and characterized for its substrate specificity, kinetics and stability under various conditions. The optimal temperature and pH for Est3385 were 35 °C and 6.0, respectively. This enzyme could detoxify various pyrethroid pesticides and degrade the optimal substrate fenpropathrin with a Km and Vmax value of 0.734 ± 0.013 mmol·l−1 and 0.918 ± 0.025 U·µg−1, respectively. No cofactor was found to affect Est3385 activity but substantial reduction of enzymatic activity was observed when metal ions were applied. Taken together, a new pyrethroid degradation esterase was identified and characterized. Modification of Est3385 with protein engineering toolsets should enhance its potential for field application to reduce the pesticide residue from agroecosystems. Abstract Full length open reading frame of pyrethroid detoxification gene, Est3385 , contains 963 nucleotides. This gene was identified and cloned based on the genome sequence of Rhodopseudomonas palustris PSB-S available at the GneBank. The predicted amino acid sequence of Est3385 shared moderate identities (30–46%) with the known homologous esterases. Phylogenetic analysis revealed that Est3385 was a member in the esterase family I. Recombinant Est3385 was heterologous expressed in E. coli , purified and characterized for its substrate specificity, kinetics and stability under various conditions. The optimal temperature and pH for Est3385 were 35 °C and 6.0, respectively. This enzyme could detoxify various pyrethroid pesticides and degrade the optimal substrate fenpropathrin with a K m and V max value of 0.734 ± 0.013 mmol·l −1 and 0.918 ± 0.025 U·µg −1 , respectively. No cofactor was found to affect Est3385 activity but substantial reduction of enzymatic activity was observed when metal ions were applied. Taken together, a new pyrethroid degradation esterase was identified and characterized. Modification of Est3385 with protein engineering toolsets should enhance its potential for field application to reduce the pesticide residue from agroecosystems. Full length open reading frame of pyrethroid detoxification gene, Est3385, contains 963 nucleotides. This gene was identified and cloned based on the genome sequence of Rhodopseudomonas palustris PSB-S available at the GneBank. The predicted amino acid sequence of Est3385 shared moderate identities (30-46%) with the known homologous esterases. Phylogenetic analysis revealed that Est3385 was a member in the esterase family I. Recombinant Est3385 was heterologous expressed in E. coli, purified and characterized for its substrate specificity, kinetics and stability under various conditions. The optimal temperature and pH for Est3385 were 35 °C and 6.0, respectively. This enzyme could detoxify various pyrethroid pesticides and degrade the optimal substrate fenpropathrin with a Km and Vmax value of 0.734 ± 0.013 mmol·l and 0.918 ± 0.025 U·µg , respectively. No cofactor was found to affect Est3385 activity but substantial reduction of enzymatic activity was observed when metal ions were applied. Taken together, a new pyrethroid degradation esterase was identified and characterized. Modification of Est3385 with protein engineering toolsets should enhance its potential for field application to reduce the pesticide residue from agroecosystems. Abstract Full length open reading frame of pyrethroid detoxification gene, Est3385, contains 963 nucleotides. This gene was identified and cloned based on the genome sequence of Rhodopseudomonas palustris PSB-S available at the GneBank. The predicted amino acid sequence of Est3385 shared moderate identities (30–46%) with the known homologous esterases. Phylogenetic analysis revealed that Est3385 was a member in the esterase family I. Recombinant Est3385 was heterologous expressed in E. coli, purified and characterized for its substrate specificity, kinetics and stability under various conditions. The optimal temperature and pH for Est3385 were 35 °C and 6.0, respectively. This enzyme could detoxify various pyrethroid pesticides and degrade the optimal substrate fenpropathrin with a Km and Vmax value of 0.734 ± 0.013 mmol·l−1 and 0.918 ± 0.025 U·µg−1, respectively. No cofactor was found to affect Est3385 activity but substantial reduction of enzymatic activity was observed when metal ions were applied. Taken together, a new pyrethroid degradation esterase was identified and characterized. Modification of Est3385 with protein engineering toolsets should enhance its potential for field application to reduce the pesticide residue from agroecosystems. |
| ArticleNumber | 7384 |
| Author | Zhou, Xuguo Liu, Yong Luo, Xiangwen Du, Jiao Zhang, Deyong Zhang, Songbai |
| Author_xml | – sequence: 1 givenname: Xiangwen surname: Luo fullname: Luo, Xiangwen organization: Key Laboratory of Pest Management of Horticultural Crop of Hunan Province, Hunan Plant Protection Institute, Hunan Academy of Agricultural Science – sequence: 2 givenname: Deyong surname: Zhang fullname: Zhang, Deyong organization: Key Laboratory of Pest Management of Horticultural Crop of Hunan Province, Hunan Plant Protection Institute, Hunan Academy of Agricultural Science – sequence: 3 givenname: Xuguo surname: Zhou fullname: Zhou, Xuguo organization: Department of Entomology, University of Kentucky – sequence: 4 givenname: Jiao surname: Du fullname: Du, Jiao organization: Key Laboratory of Pest Management of Horticultural Crop of Hunan Province, Hunan Plant Protection Institute, Hunan Academy of Agricultural Science – sequence: 5 givenname: Songbai surname: Zhang fullname: Zhang, Songbai email: zsongb@hotmail.com organization: Key Laboratory of Pest Management of Horticultural Crop of Hunan Province, Hunan Plant Protection Institute, Hunan Academy of Agricultural Science – sequence: 6 givenname: Yong surname: Liu fullname: Liu, Yong email: haoasliu@163.com organization: Key Laboratory of Pest Management of Horticultural Crop of Hunan Province, Hunan Plant Protection Institute, Hunan Academy of Agricultural Science |
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| Cites_doi | 10.1016/j.toxlet.2015.08.658 10.1038/s41598-017-03561-8 10.1016/j.jhazmat.2016.10.056 10.1016/j.jhazmat.2012.04.031 10.1016/j.cmpb.2015.12.013 10.1007/s10532-010-9444-y 10.1186/1475-2859-7-38 10.1093/molbev/mst197 10.1021/jf052691u 10.1074/jbc.M403673200 10.1016/j.scitotenv.2015.10.131 10.1128/AEM.01298-09 10.1038/srep08784 10.1016/j.chemosphere.2014.12.077 10.1016/j.chemosphere.2015.03.091 10.1016/j.bpj.2015.11.660 10.1016/j.ibmb.2012.01.004 10.1006/pest.1996.0022 10.1016/j.procbio.2010.04.009 10.1016/0003-2697(76)90527-3 10.1021/jf051460k 10.1093/toxsci/kfh027 10.1371/journal.pone.0077329 10.18474/0749-8004-37.1.83 10.1007/s11356-015-5831-6 10.1186/1475-2859-11-33 10.1016/j.molcatb.2013.07.022 10.1128/aem.59.7.2007-2013.1993 |
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| Snippet | Full length open reading frame of pyrethroid detoxification gene,
Est3385
, contains 963 nucleotides. This gene was identified and cloned based on the genome... Full length open reading frame of pyrethroid detoxification gene, Est3385, contains 963 nucleotides. This gene was identified and cloned based on the genome... Abstract Full length open reading frame of pyrethroid detoxification gene, Est3385 , contains 963 nucleotides. This gene was identified and cloned based on the... Abstract Full length open reading frame of pyrethroid detoxification gene, Est3385, contains 963 nucleotides. This gene was identified and cloned based on the... |
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| SubjectTerms | 13/1 38/23 38/77 631/61/168 704/172 82/29 82/80 82/83 Amino acid sequence Detoxification Enzymatic activity Esterase Genomes Humanities and Social Sciences Metal ions multidisciplinary Nucleotide sequence Pesticide residues Pesticides Phylogeny Protein engineering Rhodopseudomonas palustris Science Science (multidisciplinary) Substrate specificity |
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| Title | Cloning and characterization of a pyrethroid pesticide decomposing esterase gene, Est3385, from Rhodopseudomonas palustris PSB-S |
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