酿酒酵母NCIM 3458中蝶呤脱氨酶的分子结构

IF 0.5 4区医学 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY

Pteridines Pub Date : 2017-12-20 DOI:10.1515/pterid-2017-0011

Thandeeswaran Murugesan, Karuppuswamy Velliayadevar, Murugesh Easwaran, Kiran kG, A. Ka, M. Ramasamy, Palaniswamy Muthusamy, A. Jayaraman

{"title":"酿酒酵母NCIM 3458中蝶呤脱氨酶的分子结构","authors":"Thandeeswaran Murugesan, Karuppuswamy Velliayadevar, Murugesh Easwaran, Kiran kG, A. Ka, M. Ramasamy, Palaniswamy Muthusamy, A. Jayaraman","doi":"10.1515/pterid-2017-0011","DOIUrl":null,"url":null,"abstract":"Abstract As early as 1974, reports have confirmed the anticancer activity of pterin deaminase isolated from fungi. The enzyme has also been reported in bacteria, fungi and slime mold genera, but the enzyme characterization was effetely done. The present study attempted to purify and characterize pterin deaminase enzyme from Saccharomyces cerevisiae NCIM 3458. The protein was extracted from the extracellular extract by using the ethanol precipitation method. Partial purification of pterin deaminase enzyme was achieved by ion exchange chromatography (Hi-Trap QFF) by fast protein liquid chromatography (AKTA purifier). The molecular weight of the protein was apparently determined by SDS-PAGE, and the presence of pterin deaminase was confirmed by activity staining. The purified enzyme was further biochemically characterized. Molecular docking studies showed higher binding affinity towards folic acid interaction. The structural characterization of this protein may open the windows for new drug targets for cancer therapy.","PeriodicalId":20792,"journal":{"name":"Pteridines","volume":"28 1","pages":"141 - 151"},"PeriodicalIF":0.5000,"publicationDate":"2017-12-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/pterid-2017-0011","citationCount":"2","resultStr":"{\"title\":\"Molecular architecture of pterin deaminase from Saccharomyces cerevisiae NCIM 3458\",\"authors\":\"Thandeeswaran Murugesan, Karuppuswamy Velliayadevar, Murugesh Easwaran, Kiran kG, A. Ka, M. Ramasamy, Palaniswamy Muthusamy, A. Jayaraman\",\"doi\":\"10.1515/pterid-2017-0011\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Abstract As early as 1974, reports have confirmed the anticancer activity of pterin deaminase isolated from fungi. The enzyme has also been reported in bacteria, fungi and slime mold genera, but the enzyme characterization was effetely done. The present study attempted to purify and characterize pterin deaminase enzyme from Saccharomyces cerevisiae NCIM 3458. The protein was extracted from the extracellular extract by using the ethanol precipitation method. Partial purification of pterin deaminase enzyme was achieved by ion exchange chromatography (Hi-Trap QFF) by fast protein liquid chromatography (AKTA purifier). The molecular weight of the protein was apparently determined by SDS-PAGE, and the presence of pterin deaminase was confirmed by activity staining. The purified enzyme was further biochemically characterized. Molecular docking studies showed higher binding affinity towards folic acid interaction. The structural characterization of this protein may open the windows for new drug targets for cancer therapy.\",\"PeriodicalId\":20792,\"journal\":{\"name\":\"Pteridines\",\"volume\":\"28 1\",\"pages\":\"141 - 151\"},\"PeriodicalIF\":0.5000,\"publicationDate\":\"2017-12-20\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1515/pterid-2017-0011\",\"citationCount\":\"2\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Pteridines\",\"FirstCategoryId\":\"3\",\"ListUrlMain\":\"https://doi.org/10.1515/pterid-2017-0011\",\"RegionNum\":4,\"RegionCategory\":\"医学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Pteridines","FirstCategoryId":"3","ListUrlMain":"https://doi.org/10.1515/pterid-2017-0011","RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}

引用次数: 2

摘要

摘要早在1974年，就有报道证实了从真菌中分离的蝶呤脱氨酶具有抗癌活性。在细菌、真菌和黏菌属中也有这种酶的报道，但对酶的鉴定效果不佳。本研究试图从酿酒酵母NCIM3458中纯化并鉴定蝶呤脱氨酶。采用乙醇沉淀法从细胞外提取物中提取蛋白质。采用离子交换色谱法（Hi-Trap QFF）和快速蛋白液相色谱法（AKTA纯化器）对蝶呤脱氨酶进行部分纯化。SDS-PAGE对蛋白质的分子量进行了测定，活性染色证实了蝶呤脱氨酶的存在。对纯化的酶进行了进一步的生化表征。分子对接研究显示，叶酸相互作用具有更高的结合亲和力。该蛋白的结构特征可能为癌症治疗的新药物靶点打开窗口。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

查看原文本刊更多论文

Molecular architecture of pterin deaminase from Saccharomyces cerevisiae NCIM 3458

Abstract As early as 1974, reports have confirmed the anticancer activity of pterin deaminase isolated from fungi. The enzyme has also been reported in bacteria, fungi and slime mold genera, but the enzyme characterization was effetely done. The present study attempted to purify and characterize pterin deaminase enzyme from Saccharomyces cerevisiae NCIM 3458. The protein was extracted from the extracellular extract by using the ethanol precipitation method. Partial purification of pterin deaminase enzyme was achieved by ion exchange chromatography (Hi-Trap QFF) by fast protein liquid chromatography (AKTA purifier). The molecular weight of the protein was apparently determined by SDS-PAGE, and the presence of pterin deaminase was confirmed by activity staining. The purified enzyme was further biochemically characterized. Molecular docking studies showed higher binding affinity towards folic acid interaction. The structural characterization of this protein may open the windows for new drug targets for cancer therapy.

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

Pteridines 生物-生化与分子生物学

CiteScore

1.20

自引率

25.00%

发文量

审稿时长

>12 weeks

期刊介绍： Pteridines is an open acess international quarterly journal dealing with all aspects of pteridine research. Pteridines are heterocyclic fused ring compounds involved in a wide range of biological functions from the color on butterfly wings to cofactors in enzyme catalysis to essential vitamins. Of the pteridines, 5,6,7,8-tetrahydrobiopterin is the necessary cofactor of several aromatic amino acid monoxygenases, the nitric oxide synthases and glyceryl ether monoxygenase (GEMO). Neopterin plays an essential role in the immune system and is an important biomarker in laboratory medicine for diseases such as HIV, cardiovascular disease, malignant tumors, among others. Topics: -Neopterin, dihydroneopterin, monapterin- Biopterin, tetrahydrobiopterin- Folates, antifolates, riboflavin- Phenylalanine, tyrosine, phenylketonuria, serotonin, adrenalin, noradrenalin, L-DOPA, dopamine, related biogenic amines- Phenylalanine hydroxylase, tyrosine hydroxylase, tryptophan hydroxylase, nitric oxide synthases (iNOS), alkylglycerol monooxygenase (AGMO), dihydropterin reductase, sepiapterin reductase- Homocysteine, mediators of inflammation, redox systems, iron.