当前位置: X-MOL 学术J. Enzyme Inhib. Med. Chem. › 论文详情
Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)
Human carbonic anhydrases and post-translational modifications: a hidden world possibly affecting protein properties and functions.
Journal of Enzyme inhibition and Medicinal Chemistry ( IF 5.6 ) Pub Date : 2020-07-10 , DOI: 10.1080/14756366.2020.1781846
Anna Di Fiore 1 , Claudiu T Supuran 2 , Andrea Scaloni 3 , Giuseppina De Simone 1
Affiliation  

Abstract

Human carbonic anhydrases (CAs) have become a well-recognized target for the design of inhibitors and activators with biomedical applications. Accordingly, an enormous amount of literature is available on their biochemical, functional and structural aspects. Nevertheless post-translational modifications (PTMs) occurring on these enzymes and their functional implications have been poorly investigated so far. To fill this gap, in this review we have analysed all PTMs occurring on human CAs, as deriving from the search in dedicated databases, showing a widespread occurrence of modification events in this enzyme family. By combining these data with sequence alignments, inspection of 3 D structures and available literature, we have summarised the possible functional implications of these PTMs. Although in some cases a clear correlation between a specific PTM and the CA function has been highlighted, many modification events still deserve further dedicated studies.



中文翻译:

人碳酸酐酶和翻译后修饰:一个可能影响蛋白质特性和功能的隐藏世界。

摘要

人碳酸酐酶(CAs)已成为设计用于生物医学应用的抑制剂和活化剂的公认目标。因此,关于其生化,功能和结构方面的文献很多。然而,到目前为止,对这些酶上发生的翻译后修饰(PTM)及其功能含义的研究很少。为了填补这一空白,在这篇综述中,我们分析了在人类CA上发生的所有PTM,这些PTM来自于专用数据库中的搜索,显示了该酶家族中广泛发生的修饰事件。通过将这些数据与序列比对,3D结构检查和现有文献相结合,我们总结了这些PTM的可能功能含义。

更新日期:2020-07-10
down
wechat
bug