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Isolation and characterization of a novel metagenomic enzyme capable of degrading bacterial phytotoxin toxoflavin
Toxoflavin, a 7-azapteridine phytotoxin produced by the bacterial pathogens such as Burkholderia glumae and Burkholderia gladioli, has been known as one of the key virulence factors in crop diseases. Because the toxoflavin had an antibacterial activity, a metagenomic E. coli clone capable of growing...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Public Library of Science
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5749703/ https://www.ncbi.nlm.nih.gov/pubmed/29293506 http://dx.doi.org/10.1371/journal.pone.0183893 |
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author | Choi, Ji-Eun Nguyen, Cuong Mai Lee, Boyoung Park, Ji Hyun Oh, Joon Young Choi, Jung Sup Kim, Jin-Cheol Song, Jae Kwang |
author_facet | Choi, Ji-Eun Nguyen, Cuong Mai Lee, Boyoung Park, Ji Hyun Oh, Joon Young Choi, Jung Sup Kim, Jin-Cheol Song, Jae Kwang |
author_sort | Choi, Ji-Eun |
collection | PubMed |
description | Toxoflavin, a 7-azapteridine phytotoxin produced by the bacterial pathogens such as Burkholderia glumae and Burkholderia gladioli, has been known as one of the key virulence factors in crop diseases. Because the toxoflavin had an antibacterial activity, a metagenomic E. coli clone capable of growing well in the presence of toxoflavin (30 μg/ml) was isolated and the first metagenome-derived toxoflavin-degrading enzyme, TxeA of 140 amino acid residues, was identified from the positive E. coli clone. The conserved amino acids for metal-binding and extradiol dioxygenase activity, Glu-12, His-8 and Glu-130, were revealed by the sequence analysis of TxeA. The optimum conditions for toxoflavin degradation were evaluated with the TxeA purified in E. coli. Toxoflavin was totally degraded at an initial toxoflavin concentration of 100 μg/ml and at pH 5.0 in the presence of Mn(2+), dithiothreitol and oxygen. The final degradation products of toxoflavin and methyltoxoflavin were fully identified by MS and NMR as triazines. Therefore, we suggested that the new metagenomic enzyme, TxeA, provided the clue to applying the new metagenomic enzyme to resistance development of crop plants to toxoflavin-mediated disease as well as to biocatalysis for Baeyer-Villiger type oxidation. |
format | Online Article Text |
id | pubmed-5749703 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-57497032018-01-26 Isolation and characterization of a novel metagenomic enzyme capable of degrading bacterial phytotoxin toxoflavin Choi, Ji-Eun Nguyen, Cuong Mai Lee, Boyoung Park, Ji Hyun Oh, Joon Young Choi, Jung Sup Kim, Jin-Cheol Song, Jae Kwang PLoS One Research Article Toxoflavin, a 7-azapteridine phytotoxin produced by the bacterial pathogens such as Burkholderia glumae and Burkholderia gladioli, has been known as one of the key virulence factors in crop diseases. Because the toxoflavin had an antibacterial activity, a metagenomic E. coli clone capable of growing well in the presence of toxoflavin (30 μg/ml) was isolated and the first metagenome-derived toxoflavin-degrading enzyme, TxeA of 140 amino acid residues, was identified from the positive E. coli clone. The conserved amino acids for metal-binding and extradiol dioxygenase activity, Glu-12, His-8 and Glu-130, were revealed by the sequence analysis of TxeA. The optimum conditions for toxoflavin degradation were evaluated with the TxeA purified in E. coli. Toxoflavin was totally degraded at an initial toxoflavin concentration of 100 μg/ml and at pH 5.0 in the presence of Mn(2+), dithiothreitol and oxygen. The final degradation products of toxoflavin and methyltoxoflavin were fully identified by MS and NMR as triazines. Therefore, we suggested that the new metagenomic enzyme, TxeA, provided the clue to applying the new metagenomic enzyme to resistance development of crop plants to toxoflavin-mediated disease as well as to biocatalysis for Baeyer-Villiger type oxidation. Public Library of Science 2018-01-02 /pmc/articles/PMC5749703/ /pubmed/29293506 http://dx.doi.org/10.1371/journal.pone.0183893 Text en © 2018 Choi et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Choi, Ji-Eun Nguyen, Cuong Mai Lee, Boyoung Park, Ji Hyun Oh, Joon Young Choi, Jung Sup Kim, Jin-Cheol Song, Jae Kwang Isolation and characterization of a novel metagenomic enzyme capable of degrading bacterial phytotoxin toxoflavin |
title | Isolation and characterization of a novel metagenomic enzyme capable of degrading bacterial phytotoxin toxoflavin |
title_full | Isolation and characterization of a novel metagenomic enzyme capable of degrading bacterial phytotoxin toxoflavin |
title_fullStr | Isolation and characterization of a novel metagenomic enzyme capable of degrading bacterial phytotoxin toxoflavin |
title_full_unstemmed | Isolation and characterization of a novel metagenomic enzyme capable of degrading bacterial phytotoxin toxoflavin |
title_short | Isolation and characterization of a novel metagenomic enzyme capable of degrading bacterial phytotoxin toxoflavin |
title_sort | isolation and characterization of a novel metagenomic enzyme capable of degrading bacterial phytotoxin toxoflavin |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5749703/ https://www.ncbi.nlm.nih.gov/pubmed/29293506 http://dx.doi.org/10.1371/journal.pone.0183893 |
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