Carbonic anhydrase versatility: from pH regulation to CO2 sensing and metabolism

While the carbonic anhydrase (CA, EC 4.2.1.1) superfamily of enzymes has been described primarily as involved only in pH regulation for decades, it also has many other important functions. CO2, bicarbonate, and protons, the physiological substrates of CA, are indeed the main buffering system in orga...

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Main Author: Claudiu T. Supuran
Format: Article
Language:English
Published: Frontiers Media S.A. 2023-11-01
Series:Frontiers in Molecular Biosciences
Subjects:
Online Access:https://www.frontiersin.org/articles/10.3389/fmolb.2023.1326633/full
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author Claudiu T. Supuran
author_facet Claudiu T. Supuran
author_sort Claudiu T. Supuran
collection DOAJ
description While the carbonic anhydrase (CA, EC 4.2.1.1) superfamily of enzymes has been described primarily as involved only in pH regulation for decades, it also has many other important functions. CO2, bicarbonate, and protons, the physiological substrates of CA, are indeed the main buffering system in organisms belonging to all life kingdoms; however, in the last period, relevant progress has been made in the direction of elucidating the involvement of the eight genetically distinct CA families in chemical sensing, metabolism, and several other crucial physiological processes. Interference with CA activity, both by inhibiting and activating these enzymes, has thus led to novel applications for CA inhibitors and activators in the field of innovative biomedicine and environment and health. In this perspective article, I will discuss the recent advances which have allowed for a deeper understanding of the biochemistry of these versatile enzymes and various applications of their modulators of activity.
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spelling doaj.art-26b700862adf4b9e8a9f439993c98ba12023-11-13T11:45:10ZengFrontiers Media S.A.Frontiers in Molecular Biosciences2296-889X2023-11-011010.3389/fmolb.2023.13266331326633Carbonic anhydrase versatility: from pH regulation to CO2 sensing and metabolismClaudiu T. SupuranWhile the carbonic anhydrase (CA, EC 4.2.1.1) superfamily of enzymes has been described primarily as involved only in pH regulation for decades, it also has many other important functions. CO2, bicarbonate, and protons, the physiological substrates of CA, are indeed the main buffering system in organisms belonging to all life kingdoms; however, in the last period, relevant progress has been made in the direction of elucidating the involvement of the eight genetically distinct CA families in chemical sensing, metabolism, and several other crucial physiological processes. Interference with CA activity, both by inhibiting and activating these enzymes, has thus led to novel applications for CA inhibitors and activators in the field of innovative biomedicine and environment and health. In this perspective article, I will discuss the recent advances which have allowed for a deeper understanding of the biochemistry of these versatile enzymes and various applications of their modulators of activity.https://www.frontiersin.org/articles/10.3389/fmolb.2023.1326633/fullcarbonic anhydrasepH regulationCO2/bicarbonate sensingmetabolisminhibitor
spellingShingle Claudiu T. Supuran
Carbonic anhydrase versatility: from pH regulation to CO2 sensing and metabolism
Frontiers in Molecular Biosciences
carbonic anhydrase
pH regulation
CO2/bicarbonate sensing
metabolism
inhibitor
title Carbonic anhydrase versatility: from pH regulation to CO2 sensing and metabolism
title_full Carbonic anhydrase versatility: from pH regulation to CO2 sensing and metabolism
title_fullStr Carbonic anhydrase versatility: from pH regulation to CO2 sensing and metabolism
title_full_unstemmed Carbonic anhydrase versatility: from pH regulation to CO2 sensing and metabolism
title_short Carbonic anhydrase versatility: from pH regulation to CO2 sensing and metabolism
title_sort carbonic anhydrase versatility from ph regulation to co2 sensing and metabolism
topic carbonic anhydrase
pH regulation
CO2/bicarbonate sensing
metabolism
inhibitor
url https://www.frontiersin.org/articles/10.3389/fmolb.2023.1326633/full
work_keys_str_mv AT claudiutsupuran carbonicanhydraseversatilityfromphregulationtoco2sensingandmetabolism