Carbonic anhydrases are metalloenzymes catalyzing the reversible hydration of carbon dioxide to bicarbonate (CO2 + H2O ⇆ HCO3−+ H+). The enzymes are widely distributed among metabolically diverse species from all three domains of life (Eucarya, Bacteria and Archaea) reflecting the importance of this enzyme in biology. Five independently evolved classes (α, β, γ, δ, and ζ) of carbonic anhydrases have been identified that have no significant sequence or structural identity, save the active site. Thus, Nature has repeatedly invented carbonic anhydrase which further underscores the broad physiological importance of this enzyme. Although diverse and widespread, the current understanding of the biochemistry and biological roles of carbonic anhydrases are based largely on several α and β class enzymes from mammals and plants. Only one each from the δ and ζ classes have been characterized, both isolated from a marine diatom of the Eucarya domain. The γ class is widely distributed in diverse species from all three domains of life however, only Cam has been characterized biochemically and shown to have carbonic anhydrase activity. Here you can see the crystal structure of a gamma carbonic anhydrase from Methanosarcina thermophila (PDB code: 1QRE)
#molecularart ... #immolecular ... #anhydrase ... #carbonic ... #enzymeclass ... #crystal ... #methanosarcina ... #xray
Structure of the gamma carbonic anhydrase rendered with @proteinimaging and depicted with @corelphotopaint
#molecularart ... #immolecular ... #anhydrase ... #carbonic ... #enzymeclass ... #crystal ... #methanosarcina ... #xray
Structure of the gamma carbonic anhydrase rendered with @proteinimaging and depicted with @corelphotopaint
