Human carbonic anhydrases and post-translational modifications: a hidden world possibly affecting protein properties and functions(244 views) Di Fiore A, Supuran CT, Scaloni A, De Simone G
Istituto di Biostrutture e Bioimmagini-National Research Council, Napoli, Italy.
NEUROFARBA Department, Pharmaceutical and Nutraceutical Section, University of Firenze, Sesto Fiorentino, Italy.
Proteomics and Mass Spectrometry Laboratory, ISPAAM, National Research Council, Napoli, Italy.
References: Not available.
Human carbonic anhydrases and post-translational modifications: a hidden world possibly affecting protein properties and functions
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.
Human carbonic anhydrases and post-translational modifications: a hidden world possibly affecting protein properties and functions