Carbonic anhydrases
Metalloenzymes, Page: 139-156
2024
- 4Citations
- 95Captures
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Book Chapter Description
The metalloenzyme carbonic anhydrase (CA, EC 4.2.1.1) is an effective catalyst for the hydration of CO 2 to bicarbonate and protons, acting also on other substrates such as COS, CS 2, cyanamide, aldehydes, ester, thioesters, and selenoesters. CAs are widespread in both prokaryotes and eukaryotes, with eight genetic families encoding them, the α-, β-, γ-, δ-, ζ-, η-, θ-, and ι-classes. All these proteins except ι-CAs are metalloenzymes, with Zn(II) being the prevalent metal ion present in their active site. The catalytic mechanism and structural organization are well known for many representatives of the α-, β-, γ-, ζ-, θ-, and ι-CAs. A large number of inhibitor and activator classes are known, with vertebrate α-CAs being the most investigated such enzymes. The human 15 CA (hCA) isoforms are drug targets for diuretics, antiglaucoma, antiepileptic, antiobesity, and antitumor agents, and recent research showed their involvement in neuropathic pain, arthritis, cerebral ischemia, and other neurological disorders. Pathogenic organism CAs present in bacteria, fungi, protozoans, and platyhelminths started to be investigated in the search of antiinfectives devoid of drug resistance problems common to the clinically used such drugs. CA activators show promise for memory therapy and might be thus useful for improving cognition or in therapeutic areas such as phobias, obsessive-compulsive disorder, generalized anxiety, posttraumatic stress disorders, for which few drugs are available. There are at least 30 clinically used CA inhibitor drugs, and many others are in advanced clinical trials for the management of many diseases in which the activity of CAs is dysregulated.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/B9780128239742000140; http://dx.doi.org/10.1016/b978-0-12-823974-2.00014-0; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85176836829&origin=inward; https://linkinghub.elsevier.com/retrieve/pii/B9780128239742000140; https://dx.doi.org/10.1016/b978-0-12-823974-2.00014-0
Elsevier BV
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