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Review
. 2020 Oct 6;119(7):1275-1280.
doi: 10.1016/j.bpj.2020.08.020. Epub 2020 Aug 27.

Perspectives on the Classical Enzyme Carbonic Anhydrase and the Search for Inhibitors

Bengt-Harald Jonsson  1 , Anders Liljas  2
Affiliations
Review

Perspectives on the Classical Enzyme Carbonic Anhydrase and the Search for Inhibitors

Bengt-Harald Jonsson et al. Biophys J. .

Abstract

Carbonic anhydrase (CA) is a thoroughly studied enzyme. Its primary role is the rapid interconversion of carbon dioxide and bicarbonate in the cells, where carbon dioxide is produced, and in the lungs, where it is released from the blood. At the same time, it regulates pH homeostasis. The inhibitory function of sulfonamides on CA was discovered some 80 years ago. There are numerous physiological-therapeutic conditions in which inhibitors of carbonic anhydrase have a positive effect, such as glaucoma, or act as diuretics. With the realization that several isoenzymes of carbonic anhydrase are associated with the development of several types of cancer, such as brain and breast cancer, the development of inhibitor drugs specific to those enzyme forms has exploded. We would like to highlight the breadth of research on the enzyme as well as draw the attention to some problems in recent published work on inhibitor discovery.

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Figures

Figure 1
Figure 1
The binding of a competitive inhibitor to an enzyme ((25), Chapter 5).
Figure 2
Figure 2
Theoretical inhibition curves for inhibitors of various strengths at an enzyme concentration of 50 nM ((25), chapter 7).
Figure 3
Figure 3
Typical inhibition curves from (32), using compound 10 and carbonic anhydrase isoenzymes II and XII.
See this image and copyright information in PMC

Comment in

References

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