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念珠藻属PCC7120各种偶氮还原酶辅助相互作用蛋白的同源建模、对接研究及功能分析

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

作者信息

Philem Priyadarshini Devi, Adhikari Samrat

机构信息

Bioinformatics Infrastructure Facility, Department of Biotechnology, St Edmund's College, Shillong- 793003, Meghalaya, India.

出版信息

Bioinformation. 2012;8(7):296-300. doi: 10.6026/97320630008296. Epub 2012 Apr 13.

DOI:10.6026/97320630008296
PMID:22553385
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3338972/
Abstract

Azo dyes have become a threat to public health because of its toxicity and carcinogenicity. Azoreductase enzyme plays a pivotal role in the degradation of azodyes released by industrial effluents and other resources. The degradation pathway has to be studied in detail for increasing the activity of azoreductase and for better degradation of azo dyes. But the data available on cyanobacterial azoreductase enzyme and its degradation pathway are still very less. Therefore the present work explored the azoreductase pathway of the cyanobacterium Nostoc sp. PCC7120 for better understanding of the degradation pathway and the other accessory interacting proteins involved. The accessory interacting proteins of azoreductase from cyanobacterium Nostoc sp. PCC7120 were obtained from STRING database. The proteins do not have a comprehensive three dimensional structure and are hypothetical. The secondary structure and functional analysis indicated that the proteins are all soluble proteins, without disulphide bonds and have alpha helices only. The structural prediction and docking study showed that alr2106, alr1063 and alr2326 have best docking result which tally with the STRING database confidence score and thus these proteins could possibly enhance the azoreductase activity and better dye degradation. These results will pave way for further increase in azoreductase activity and for better understanding of the dye degradation pathway.

摘要

偶氮染料因其毒性和致癌性已对公众健康构成威胁。偶氮还原酶在工业废水和其他来源释放的偶氮染料降解中起关键作用。为了提高偶氮还原酶的活性并更好地降解偶氮染料,必须详细研究其降解途径。但是,关于蓝藻偶氮还原酶及其降解途径的现有数据仍然非常少。因此,本研究探索了蓝藻 Nostoc sp. PCC7120 的偶氮还原酶途径,以更好地了解其降解途径以及其他参与相互作用的辅助蛋白。来自蓝藻 Nostoc sp. PCC7120 的偶氮还原酶的辅助相互作用蛋白是从 STRING 数据库获得的。这些蛋白质没有完整的三维结构,是假设的。二级结构和功能分析表明,这些蛋白质都是可溶性蛋白质,没有二硫键,并且仅具有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,这与 STRING 数据库置信度得分相符,因此这些蛋白质可能会增强偶氮还原酶的活性并更好地降解染料。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。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f8c0/3338972/c3f5353f0532/97320630008296F3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f8c0/3338972/e226948c5d7e/97320630008296F1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f8c0/3338972/79961b737020/97320630008296F2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f8c0/3338972/c3f5353f0532/97320630008296F3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f8c0/3338972/e226948c5d7e/97320630008296F1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f8c0/3338972/79961b737020/97320630008296F2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f8c0/3338972/c3f5353f0532/97320630008296F3.jpg

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