Istituto di Biostrutture e Bioimmagini-National Research Council, Napoli, Italy.
NEUROFARBA Department, Pharmaceutical and Nutraceutical Section, University of Firenze, Sesto Fiorentino, Italy.
J Enzyme Inhib Med Chem. 2020 Dec;35(1):1450-1461. doi: 10.1080/14756366.2020.1781846.
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.
人类碳酸酐酶(CA)已成为设计具有生物医学应用的抑制剂和激活剂的公认靶标。因此,大量文献可用于研究其生化、功能和结构方面。然而,迄今为止,这些酶上发生的翻译后修饰(PTM)及其功能意义还没有得到充分的研究。为了填补这一空白,在这篇综述中,我们分析了所有在人类 CA 上发生的 PTM,这些信息源自于对专用数据库的搜索,显示了这种酶家族中广泛存在的修饰事件。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 可能具有的功能意义。尽管在某些情况下,已经强调了特定 PTM 与 CA 功能之间的明确相关性,但许多修饰事件仍需要进一步的专门研究。