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Review
. 2019 Dec;34(1):1652-1659.
doi: 10.1080/14756366.2019.1664501.

Activation of α-, β-, γ- δ-, ζ- and η- class of carbonic anhydrases with amines and amino acids: a review

Affiliations
Review

Activation of α-, β-, γ- δ-, ζ- and η- class of carbonic anhydrases with amines and amino acids: a review

Suleyman Akocak et al. J Enzyme Inhib Med Chem. 2019 Dec.

Abstract

Eight genetically distinct carbonic anhydrase (EC 4.2.1.1) enzyme families (α-, β-, γ- δ-, ζ-, η-, θ- and ι-CAs) were described to date. On the other hand, 16 mammalian α-CA isoforms are known to be involved in many diseases such as glaucoma, edema, epilepsy, obesity, hypoxic tumors, neuropathic pain, arthritis, neurodegeneration, etc. Although CA inhibitors were investigated for the management of a variety of such disorders, the activators just started to be investigated in detail for their in vivo effects. This review summarizes the activation profiles of α-, β, γ-, δ-, ζ- and η- CAs from various organisms (animals, fungi, protozoan, bacteria and archaea) with the most investigated classes of activators, the amines and the amino acids.

Keywords: Carbonic anhydrase; activator; isoforms; neurodegenerative; proton shuttle.

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Figures

Figure 1.
Figure 1.
Catalytic mechanism of α-CAs [3]. A. The zinc hydroxide form of the enzyme. B. The bucleophilic attack on CO2 bound in the hydrophobic pocket. C. Bicarbonate bound to the active site metal ion. D. Acidic form of the enzyme. B in the last step of the cycle is a buffer molecule or the imidazole moiety of a His64 residue from the enzyme active site, acting as proton shuttle.
Chart 1.
Chart 1.
Amino acids 1–11 and amines 12–19.

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