The exceptional properties of Plasmodium deoxyguanylate pathways as a potential area for metabolic and drug discovery studies.

Mahmoud Kandeel, Yoshiaki Kitamura, Yukio Kitade
{"title":"The exceptional properties of Plasmodium deoxyguanylate pathways as a potential area for metabolic and drug discovery studies.","authors":"Mahmoud Kandeel,&nbsp;Yoshiaki Kitamura,&nbsp;Yukio Kitade","doi":"10.1093/nass/nrp020","DOIUrl":null,"url":null,"abstract":"<p><p>In Plasmodium falciparum, deoxyguanylate was found to be a substrate for several DNA metabolizing enzymes. Guanylate kinase utilizes dGMP with very low specificity, which is estimated to be the lowest among well-known prokaryotic and eukaryotic enzymes. Furthermore, thymidylate kinase, which is a pyrimidine specific enzyme, was found to phosphorylate dGMP with a surprisingly high specificity similar to that of the natural substrate. The above mentioned distinctions are specific for the Plasmodium protozoa and provide an interesting method for tracking dGMP metabolism during development and a starting point for drug development.</p>","PeriodicalId":87448,"journal":{"name":"Nucleic acids symposium series (2004)","volume":" 53","pages":"39-40"},"PeriodicalIF":0.0000,"publicationDate":"2009-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1093/nass/nrp020","citationCount":"15","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Nucleic acids symposium series (2004)","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1093/nass/nrp020","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 15

Abstract

In Plasmodium falciparum, deoxyguanylate was found to be a substrate for several DNA metabolizing enzymes. Guanylate kinase utilizes dGMP with very low specificity, which is estimated to be the lowest among well-known prokaryotic and eukaryotic enzymes. Furthermore, thymidylate kinase, which is a pyrimidine specific enzyme, was found to phosphorylate dGMP with a surprisingly high specificity similar to that of the natural substrate. The above mentioned distinctions are specific for the Plasmodium protozoa and provide an interesting method for tracking dGMP metabolism during development and a starting point for drug development.

脱氧鸟苷疟原虫途径的特殊性质作为代谢和药物发现研究的潜在领域。
在恶性疟原虫中,脱氧鸟苷酸被发现是几种DNA代谢酶的底物。鸟苷酸激酶利用dGMP的特异性非常低,估计是已知的原核和真核酶中最低的。此外,胸苷激酶(thymidylate kinase)是一种嘧啶特异性酶,可以磷酸化dGMP,具有与天然底物相似的高特异性。上述差异是疟原虫原生动物所特有的,为在发育过程中追踪dGMP代谢提供了一种有趣的方法,也为药物开发提供了一个起点。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
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