Carbonic Anhydrase: Mechanism, Regulation, Links to Disease, by Susan C. Frost, Robert McKenna

By Susan C. Frost, Robert McKenna

The examine of carbonic anhydrase has spanned a number of generations of scientists. Carbonic anhydrase used to be first stumbled on in 1932 via Meldrum and Roughton. Inhibition by means of sulfanilamide was once proven in 1940 via Mann and Keilin. Even Hans Krebs contributed to early experiences with a paper in 1948 exhibiting the connection of 25 assorted sulfonamides to CA inhibition. It was once he who mentioned the significance of either the charged and uncharged personality of those compounds for physiological experiments. the sector of research that makes a speciality of carbonic anhydrase (CA) has exploded lately with the identity of latest households and isoforms. The CAs are metalloenzymes that are constituted of five structurally various households: the alpha, beta, gamma, and delta, and epsilon periods. The alpha category is located essentially in animals with numerous isoforms linked to human sickness. The beta CAs are expressed essentially in vegetation and are the main divergent. The gamma CAs are the main historic. those are structurally concerning the beta CAs, yet have a mechanism extra just like the alpha CAs. The delta CAs are present in marine algae and diflagellates. The epsilon category is located in prokaryotes within which it's a part of the carboxysome shell might be offering RuBisCO with CO2 for carbon fixation. With the buzz surrounding the invention of disease-related CAs, scientists have redoubled their efforts to raised comprehend structure-function relationships, to layout excessive affinity, isotype-specific inhibitors, and to delineate signaling platforms that play regulatory roles over expression and job. now we have designed the ebook to hide easy details of mechanism, constitution, and serve as of the CA households. The authors incorporated during this e-book carry to gentle the most recent facts in regards to the function of CA in body structure and pathology, throughout phylums, and in designated environmental niches.

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Additional info for Carbonic Anhydrase: Mechanism, Regulation, Links to Disease, and Industrial Applications

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Formation of bicarbonate promotes a bidentate interaction with the zinc metal, resulting in a penta-coordinated metal ion with trigonal bipyramidal geometry. A water molecule displaces the zinc-bound bicarbonate which is then deprotonated via the proton transfer water network for the subsequent round of catalysis. A previously unidentified water molecule was observed in both the apoand holo-CO2 bound HCA II structures which may play the role of displacing bicarbonate [96, 98]. This water molecule is located between the side chain of Thr200 and the CO2 molecule and could allow for easier access to the bicarbonate molecule and increased catalytic activity (as compared to random diffusion of water from the bulk solvent into the active site).

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Schwartz GL, Kittelberger AM, Watkins RH, O’Reilly MA (2003) Carbonic anhydrase XII mRNA encodes a hydratase that is differentially expressed along the rabbit nephron. Am J Physiol 284:F399–F410 152. Sterling D, Alvarez BV, Casey JR (2002) The extracellular component of a transport metabolon: extracellular loop 4 of the human AE1 Cl /HCO3 exchanger binds carbonic anhydrase IV. J Biol Chem 277:25239–25246 153. Yang Z, Alvarez B, Chakarova C, Jiang L, Karan G, Frederick JM, Zhao Y, Sauve Y, Zrenner E, Wissinger B, Den Hollander AI, Katz B, Baehr W, Cremers FP, Casey JR, Bhattacharya SS, Zhang K (2005) Mutant carbonic anhydrase 4 impairs pH regulation and causes retinal photoreceptor degeneration.

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