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Carbonic Anhydrases and Their Physiological Roles MOL2NET, 2019, 5, http://sciforum.net/conference/mol2net-05 ISSN: 2624-5078 1 DOI : 10.3390/mol2net-05-xxxxx MOL2NET, International Conference on Multidisciplinary Sciences, 5th Edition MDPI USINEWS-03: US-IN-EU Worldwide Science Workshop Series, UMN, Duluth, USA, 2019 Carbonic Anhydrases and their Physiological Roles Tanya Agarwal, Rajeev K Singla *, Arun Garg Drug Design and Discovery Laboratory, School of Medical and Allied Sciences, KR Mangalam University, Sohna Road, Gurugram-122103, India * Address for Correspondence: Rajeev K Singla, [email protected] Graphical Abstract Abstract. Carbonic anhydrase is an omnipresent zinc- containing metalloenzyme which is essential for a lot of physiological activities because of its property to convert CO2 to HCO3- reversibly. It is one of the fastest enzymes known for hydrating 106 molecules of CO2 per second. The rate of reaction of this enzyme is typically limited by the rate of diffusion of its substrates. There are six types of carbonic anhydrases- alpha, beta, gamma, delta, epsilon and zeta, named by greek letters. Carbonic anhydrase is often arranged in clusters along membranes or localised in extracellular spaces, which may contribute to the ability of carbonic anhydrase to facilitate the intracellular diffusion of carbon dioxide and protons (H+). By increasing the movement of protons, carbonic anhydrase can dissipate intracellular pH gradients, thereby helping the cell to maintain a uniform cellular pH. Overall, the uses of Carbonic anhydrase are multifold which will be later discussed in this paper. Introduction carbon dioxide. This enzyme was first identified Carbonic anhydrase (EC-4.2.1.1), also known as in 1933, in red blood cells of cows (Dutta, 2004) carbonate dehydratases (Almanza, 2012), is a by Meldrum and Roughton in 1933 and Neish zinc containing metalloenzyme that catalyses the accidentally discovered the first β carbonic inter-conversion of dissolved bicarbonates and anhydrase as a component of the chloroplast of MOL2NET, 2019, 5, http://sciforum.net/conference/mol2net-05 ISSN: 2624-5078 2 DOI : 10.3390/mol2net-05-xxxxx the plant leaf in 1939 (Almanza, 2012). Carbonic first class, the α-CA, was discovered in the anhydrase is one of the fastest enzymes known 1930′s in vertebrates. The second class, the beta- for hydrating 106 molecules of CO2 per second. CA, was discovered in the 1990′s in plants The rate of reaction of this enzyme is typically (DiMario et al, 2018). A third group was limited by the rate of diffusion of its substrates identified in archaebacteria in 1994. The latest (Bhat et al, 2017). The carbonic anhydrase CA families, the η-CAs and the θ-CAs, were reaction is involved in many physiological and discovered in 2015 and 2016 respectively. Each pathological processes, including respiration and protein family is phylogenetically unrelated to transport of CO2 and bicarbonate between the others (DiMario et al, 2018). metabolizing tissues and lungs, pH and CO2 homeostasis, electrolyte secretion in various 1. ALPHA TYPE tissues and organs, biosynthetic reactions (such The α-class is found throughout the animal as gluconeogenesis, lipogenesis and kingdom, in the periplasm (Bhat et al, 2017). The ureagenesis), bone resorption and calcification ɑ-carbonic anhydrases are widely identified in (Supuran, 2018). Species can produce many vertebrates, algae and in eubacteria (Bhat et al, different carbonic anhydrase isozymes, some of 2017). They were the first class of carbonic which act in the cytosol, while others are anhydrases which were isolated from membrane-bound. For instance, in humans there erythrocytes. They are distinct from all other are five cytosolic isozymes (I, II, III, VII and carbonic anhydrase classes in both protein XIII) (Supuran, 2018), five membrane-bound structure and amino acid sequence (DiMario et isozymes (IV, VII, IX, XII and XIV), two al, 2018). The protein structure includes a central mitochondrial isozymes (VA and VB), and a β-sheet consisting of ten β-strands surrounded by secreted salivary isozyme (VI), as well as several seven peripheral α-helices. The β-sheet acts as related proteins that lack catalytic the active site of carbonic anhydrase. It activity. Carbonic anhydrases are often arranged coordinates the zinc atom with three histidine in clusters along membranes or localised in residues and a water molecule (DiMario et al, extracellular spaces, which may contribute to the 2018). ability of carbonic anhydrase to facilitate the The CA enzymes found in mammals are divided intracellular diffusion of carbon dioxide and + into four broad subgroups, which, in turn consist protons (H ). By increasing the movement of of several isoforms: protons, carbonic anhydrase can dissipate intracellular pH gradients, thereby helping the • The cytosolic CAs (CA-I, CA-II, CA-III, CA- cell to maintain a uniform cellular pH. Carbonic VII and CA XIII) anhydrases can also create localised gradients, • Mitochondrial CAs (CA-VA and CA-VB) which may aid in processes such as facilitated diffusion across a membrane. • secreted CAs (CA-VI) • Membrane-associated CAs (CA-IV, CA-IX, Types of Carbonic Anhydrase CA-XII, CA-XIV and CA-XV) There is a wide variety of carbonic anhydrase proteins that fall into a number of protein There are three additional acatalytic CA isoforms families. These families are named by Greek (CA-VIII, CA-X, and CA-XI) whose functions letters and roughly follow the order in which are unclear (Hunter, 2018). they were discovered (DiMario et al, 2018). The MOL2NET, 2019, 5, http://sciforum.net/conference/mol2net-05 ISSN: 2624-5078 3 DOI : 10.3390/mol2net-05-xxxxx calcification (Mutat and GN, 2004). Other features include developmental delay, short 1.1 CARBONIC ANHYDRASE I (CAI) stature, cognitive defects, and a history of multiple fractures by adolescence (Mutat and Carbonic anhydrase I belongs to α-CA sub- GN, 2004). family and is localized in the cytosol of red blood cell, GI tract, cardiac tissues and other organs or 1.3 CARBONIC ANHYDRASE III (CAIII) tissues (Cedar101, 2018). The human CAI protein contains an N-terminus active site, zinc Carbonic anhydrase III (CA III) is a cytosolic binding site, and substrate-binding site. The enzyme which is known to be highly expressed crystal structure of the human CA1-bicarbonate in the skeletal muscle, (Harju et al, 2013), tissues anion complex has two H-bonds between the that synthesize and/or store fat: liver, white Glu106-Thr199 pair and the Glu117-His119 pair, adipose tissue and brown adipose tissue (Renner, and one pi H-bond between a water molecule and 2017). It is nutritionally regulated at both the the phenyl ring of the Tyr114 residue (Cedar101, mRNA and protein level (Renner, 2017). It helps 2018). The catalytic rate of CAI is only about in reversible hydration of carbon dioxide 10% that of CAII (Cedar101, 2018). It is used in (Anonymous, 2018). It is activated by proton reversible hydration of carbon dioxide and it can donors such as imidazole and the dipeptide hydrate cyanamide to urea (Anonymous, 2018). histidyl-histidine and inhibited by coumarins and In a human zinc-activated variant of CA1, the sulfonamide derivatives such as acetazolamide Michigan Variant, a single point mutation (Anonymous, 2018). changes His 67 to Arg in a critical region of the active site. This variant of the zinc 1.4 CARBONIC ANHYDRASE IV (CAIV) metalloenzyme appears to be unique in that it possesses esterase activity that is specifically CA IV is a glycosylphosphatidyl-inositol- enhanced by added free zinc ions (Cedar101, anchored membrane isozyme expressed on the 2018). CAI is activated by histamine, imidazole, luminal surfaces of pulmonary (and certain L-adrenaline, L and D-histidine, and L and D- other) capillaries and of proximal renal tubules phenylalanine (Anonymous, 2018). (Bot, 2018). It is identified in pulmonary epithelium of many mammalian species and may 1.2 CARBONIC ANHYDRASE II (CAII) be uniquely adaptive for gas exchange necessary for the high metabolic requirements of mammals Human carbonic anhydrase II is one of the most (Bot, 2018). It is essential for acid overload efficient one in carbonic anhydrase isozymes, removal from the retina and retina epithelium, which catalyzes the reversible and acid release in the choriocapillaris in the hydration/dehydration of CO2 and water choroid (Anonymous, 2018). Carbonic anhydrase (Anonymous, 2013). It is widely found in IV is activated by histamine, L-adrenaline, D- human’s kidney, brain, Pancreas, gastric mucosa, phenylalanine, L and D-histidine and inhibited skeletal muscle, retina and lens and other by coumarins, saccharin, sulfonamide derivatives organizations organs (Anonymous, 2013). It is such as acetazolamide and Foscarnet involved in many pathological and physiological (Anonymous, 2018). processes such as acid-base balance, cancer, osteoporosis, glaucoma (Anonymous, 2013), 1.5 CARBONIC ANHYDRASE V (CAV) regulation of fluid secretion into the anterior chamber of the eye (Anonymous, 2018). It is Carbonic anhydrase V is of two types CAVA and activated by X-ray, histamine, L-adrenaline, L CAVB. CAVB is localized in the mitochondria and D-phenylalanine, L and D-histidine, L-His- and shows the highest sequence similarity to the OMe and beta-Ala-His (carnosine) (Anonymous, other mitochondrial CA, CAVA. It has a wider 2018) and competitively inhibited by saccharin, tissue distribution than CAVA (Anonymous, thioxolone, coumarins, 667-coumate, celecoxib 2018). The carbonic anhydrase VA enzyme is (Celebrex), valdecoxib (Bextra) etc particularly
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