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Homology modeling, docking studies and functional analysis of various azoreductase accessory interacting proteins of Nostoc sp.PCC7120

机译:Nostoc sp.PCC7120的各种偶氮还原酶辅助相互作用蛋白的同源性建模,对接研究和功能分析

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摘要

Azo dyes have become a threat to public health because of its toxicity and carcinogenicity. Azoreductase enzyme plays a pivotalrole in the degradation of azodyes released by industrial effluents and other resources. The degradation pathway has to be studiedin detail for increasing the activity of azoreductase and for better degradation of azo dyes. But the data available on cyanobacterialazoreductase enzyme and its degradation pathway are still very less. Therefore the present work explored the azoreductasepathway of the cyanobacterium Nostoc sp. PCC7120 for better understanding of the degradation pathway and the other accessoryinteracting proteins involved. The accessory interacting proteins of azoreductase from cyanobacterium Nostoc sp. PCC7120 wereobtained from STRING database. The proteins do not have a comprehensive three dimensional structure and are hypothetical. Thesecondary structure and functional analysis indicated that the proteins are all soluble proteins, without disulphide bonds and havealpha helices only. The structural prediction and docking study showed that alr2106, alr1063 and alr2326 have best docking resultwhich tally with the STRING database confidence score and thus these proteins could possibly enhance the azoreductase activityand better dye degradation. These results will pave way for further increase in azoreductase activity and for better understandingof the dye degradation pathway.
机译:偶氮染料由于其毒性和致癌性而已成为对公共健康的威胁。偶氮还原酶在工业废水和其他资源释放的偶氮染料的降解中起关键作用。为了增加偶氮还原酶的活性和更好地降解偶氮染料,必须详细研究降解途径。但是有关蓝细菌偶氮还原酶及其降解途径的可用数据仍然很少。因此,本工作探索了蓝细菌Nostoc sp。的偶氮还原酶途径。 PCC7120用于更好地了解降解途径和所涉及的其他辅助相互作用蛋白。蓝细菌Nostoc sp。的偶氮还原酶的辅助相互作用蛋白。从STRING数据库获得PCC7120。这些蛋白质没有全面的三维结构,并且是假设的。二级结构和功能分析表明,这些蛋白均为可溶蛋白,没有二硫键,仅具有α螺旋。结构预测和对接研究表明,alr2106,alr1063和alr2326具有最佳的对接结果,与STRING数据库的置信度一致,因此这些蛋白可能会增强偶氮还原酶的活性并改善染料的降解。这些结果将为进一步提高偶氮还原酶活性和更好地理解染料降解途径铺平道路。

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