通过分子对接比较分析从大肠杆菌中获得的酶对硫化染料毒性的降解潜力

Muhammad Naveed, Maida Salah Ud Din, Tariq Aziz, Tayyab Javed, Sana Miraj Khan, Rida Naveed, Ayaz Ali Khan, Metab Alharbi
{"title":"通过分子对接比较分析从大肠杆菌中获得的酶对硫化染料毒性的降解潜力","authors":"Muhammad Naveed, Maida Salah Ud Din, Tariq Aziz, Tayyab Javed, Sana Miraj Khan, Rida Naveed, Ayaz Ali Khan, Metab Alharbi","doi":"10.1515/znc-2024-0072","DOIUrl":null,"url":null,"abstract":"The common bacterium <jats:italic>Escherichia coli</jats:italic> has demonstrated potential in the field of biodegradation. <jats:italic>E. coli</jats:italic> is naturally capable of biodegradation because it carries a variety of enzymes that are essential for the breakdown of different substances. The degradation process is effectively catalyzed by these enzymes. The collaborative effects of <jats:italic>E. coli</jats:italic>’s aryl sulfotransferase, alkanesulfonate moonoxygenase, and azoreductase enzymes on the breakdown of sulfur dyes from industrial effluents are investigated in this work. ExPASY ProtParam was used to confirm the stability of the enzyme, showing an instability index less than 40. We determined the maximum binding affinities of these enzymes with sulfur dye pollutants – 1-naphthalenesulfonic acid, sulfogene, sulfur green 3, sulfur red 6, sulfur red 1, sulfur yellow 2, thianthrene, thiazone, and thional – using comparative molecular docking. Significantly, the highest binding affinity was shown by monooxygenase (−12.1), whereas aryl sulfotransferase and azoreductase demonstrated significant energies of −11.8 and −11.4, respectively. The interactions between proteins and ligands in the docked complexes were examined. To evaluate their combined effects, co-expression analysis of genes and enzyme bioengineering were carried out. Using aryl sulfotransferase, alkanesulfonate monooxygenase, and azoreductase, this study investigates the enzymatic degradation of sulfur dye pollutants, thereby promoting environmentally friendly and effective sulfur dye pollutant management.","PeriodicalId":23894,"journal":{"name":"Zeitschrift für Naturforschung C","volume":"48 1","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2024-04-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Comparative analysis among the degradation potential of enzymes obtained from Escherichia coli against the toxicity of sulfur dyes through molecular docking\",\"authors\":\"Muhammad Naveed, Maida Salah Ud Din, Tariq Aziz, Tayyab Javed, Sana Miraj Khan, Rida Naveed, Ayaz Ali Khan, Metab Alharbi\",\"doi\":\"10.1515/znc-2024-0072\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"The common bacterium <jats:italic>Escherichia coli</jats:italic> has demonstrated potential in the field of biodegradation. <jats:italic>E. coli</jats:italic> is naturally capable of biodegradation because it carries a variety of enzymes that are essential for the breakdown of different substances. The degradation process is effectively catalyzed by these enzymes. The collaborative effects of <jats:italic>E. coli</jats:italic>’s aryl sulfotransferase, alkanesulfonate moonoxygenase, and azoreductase enzymes on the breakdown of sulfur dyes from industrial effluents are investigated in this work. ExPASY ProtParam was used to confirm the stability of the enzyme, showing an instability index less than 40. We determined the maximum binding affinities of these enzymes with sulfur dye pollutants – 1-naphthalenesulfonic acid, sulfogene, sulfur green 3, sulfur red 6, sulfur red 1, sulfur yellow 2, thianthrene, thiazone, and thional – using comparative molecular docking. Significantly, the highest binding affinity was shown by monooxygenase (−12.1), whereas aryl sulfotransferase and azoreductase demonstrated significant energies of −11.8 and −11.4, respectively. The interactions between proteins and ligands in the docked complexes were examined. To evaluate their combined effects, co-expression analysis of genes and enzyme bioengineering were carried out. Using aryl sulfotransferase, alkanesulfonate monooxygenase, and azoreductase, this study investigates the enzymatic degradation of sulfur dye pollutants, thereby promoting environmentally friendly and effective sulfur dye pollutant management.\",\"PeriodicalId\":23894,\"journal\":{\"name\":\"Zeitschrift für Naturforschung C\",\"volume\":\"48 1\",\"pages\":\"\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2024-04-25\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Zeitschrift für Naturforschung C\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1515/znc-2024-0072\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Zeitschrift für Naturforschung C","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1515/znc-2024-0072","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0

摘要

常见的大肠杆菌在生物降解领域具有巨大潜力。大肠杆菌具有天然的生物降解能力,因为它携带多种分解不同物质所必需的酶。降解过程由这些酶有效催化。这项工作研究了大肠杆菌的芳基磺基转移酶、烷磺酸月氧合酶和偶氮还原酶对分解工业废水中的硫化染料的协同作用。我们使用 ExPASY ProtParam 来确认酶的稳定性,结果显示其不稳定指数小于 40。我们利用比较分子对接法测定了这些酶与硫化染料污染物--1-萘磺酸、砜基、硫绿 3、硫红 6、硫红 1、硫黄 2、噻蒽、噻酮和噻吩--的最大结合亲和力。值得注意的是,单氧化酶的结合亲和力最高(-12.1),而芳基磺基转移酶和偶氮还原酶的结合能量分别为-11.8和-11.4。研究还考察了对接复合物中蛋白质和配体之间的相互作用。为了评估它们的综合效应,对基因和酶的生物工程进行了共表达分析。本研究利用芳基磺基转移酶、烷磺酸单加氧酶和偶氮还原酶,研究了硫化染料污染物的酶降解,从而促进环境友好和有效的硫化染料污染物治理。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Comparative analysis among the degradation potential of enzymes obtained from Escherichia coli against the toxicity of sulfur dyes through molecular docking
The common bacterium Escherichia coli has demonstrated potential in the field of biodegradation. E. coli is naturally capable of biodegradation because it carries a variety of enzymes that are essential for the breakdown of different substances. The degradation process is effectively catalyzed by these enzymes. The collaborative effects of E. coli’s aryl sulfotransferase, alkanesulfonate moonoxygenase, and azoreductase enzymes on the breakdown of sulfur dyes from industrial effluents are investigated in this work. ExPASY ProtParam was used to confirm the stability of the enzyme, showing an instability index less than 40. We determined the maximum binding affinities of these enzymes with sulfur dye pollutants – 1-naphthalenesulfonic acid, sulfogene, sulfur green 3, sulfur red 6, sulfur red 1, sulfur yellow 2, thianthrene, thiazone, and thional – using comparative molecular docking. Significantly, the highest binding affinity was shown by monooxygenase (−12.1), whereas aryl sulfotransferase and azoreductase demonstrated significant energies of −11.8 and −11.4, respectively. The interactions between proteins and ligands in the docked complexes were examined. To evaluate their combined effects, co-expression analysis of genes and enzyme bioengineering were carried out. Using aryl sulfotransferase, alkanesulfonate monooxygenase, and azoreductase, this study investigates the enzymatic degradation of sulfur dye pollutants, thereby promoting environmentally friendly and effective sulfur dye pollutant management.
求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信