Human carbonic anhydrases and post-translational modifications: a hidden world possibly affecting protein properties and functions. (1st January 2020)

• Record Type: Journal Article
• Authors: Di Fiore, Anna; Supuran, Claudiu T.; Scaloni, Andrea; De Simone, Giuseppina
• Is Part Of: Journal of enzyme inhibition and medicinal chemistry. Volume 35:Number 1(2020)
• Page Start: 1450
• Page End: 1461
• Publication Date: 2020-01-01
• Subjects: Carbonic anhydrase -- post-translational modifications -- proteomics; Enzyme inhibitors -- Periodicals; Enzyme Inhibitors -- periodicals; Biochemistry -- periodicals; 572.7
• DOI: 10.1080/14756366.2020.1781846
• Languages: English
• ISSNs: 1475-6366

Abstract

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.