Carbonic anhydrase versatility: from pH regulation to CO2 sensing and metabolism
Open accessAbstract
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. CO 2 , 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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Other unique COGs are associated with host-immune interactions and osmotic and pH regulation.
“Specifically, 25 unique COGs are implicated in the import and processing of human milk sugars [84] , while others are associated with host-immune interactions [85] and osmotic and pH regulation [86] , i.e., functions that support survival in the infant gut [23,87,88] .”
From Genome-scale insights into the metabolic landscape and evolutionary development of Bifidobacterium bifidum (2026) · cites this paper as [86]
Section 2, “CAs and pH regulation” (page unavailable), says carbonic anhydrases help buffer and control pH. It does not link that function to unique COGs or address osmotic regulation; searches for COGs, osmotic regulation, and the infant gut found no such passage. (LLM, conf=0.82)
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- Authors
- Supuran, C. T.
- Affiliations
- University of Florence (IT)
- Corresponding author
- Supuran, Claudiu T.
- ORCID
- Supuran, Claudiu T.
- Venue
- Frontiers in Molecular Biosciences
- Publisher
- Frontiers Media SA
- Published
- 2023-11-10
- Volume
- 10
- Pages
- 1326633-1326633
- ISSN
- 2296-889X (ISSN-L)
- PMC
- PMC10676200
- OpenAlex
- W4388638493
- Cited by
- 71
- References
- 54
- Citations by year
- 2026: 28 · 2025: 25 · 2024: 18
- FWCI
- 6.33
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Frontiers in Molecular Biosciences (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme function and inhibition
- Physical Sciences › Chemical Engineering › Process Chemistry and Technology › Carbon dioxide utilization in catalysis
- Health Sciences › Medicine › Nephrology › Renal function and acid-base balance
- Keywords
- carbonic anhydrase, pH control, carbon dioxide detection, bicarbonate, proton transport, carbonic anhydrase inhibitors, carbonic anhydrase activators, enzyme modulators, buffering systems, biomedical applications, environmental applications
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