Human carbonic anhydrases and post-translational modifications: a hidden world possibly affecting protein properties and functions.
Carbonic anhydrase
post-translational modifications
proteomics
Journal
Journal of enzyme inhibition and medicinal chemistry
ISSN: 1475-6374
Titre abrégé: J Enzyme Inhib Med Chem
Pays: England
ID NLM: 101150203
Informations de publication
Date de publication:
Dec 2020
Dec 2020
Historique:
entrez:
11
7
2020
pubmed:
11
7
2020
medline:
9
2
2021
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 32648529
doi: 10.1080/14756366.2020.1781846
pmc: PMC7470082
doi:
Substances chimiques
Carbonic Anhydrases
EC 4.2.1.1
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
1450-1461Références
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