Structural highlights
Function
C1DTU5_SULAA
Publication Abstract from PubMed
Two thermostable alpha-carbonic anhydrases (alpha-CAs) isolated from thermophilic Sulfurihydrogenibium spp., namely SspCA (from S. yellowstonensis) and SazCA (from S. azorense), were shown in a previous work to possess interesting complementary properties. SspCA was shown to have an exceptional thermal stability, whereas SazCA demonstrated to be the most active alpha-CA known to date for the CO2 hydration reaction. Here we report the crystallographic structure of SazCA and the identification of the structural features responsible for its high catalytic activity, by comparing it with SspCA structure. These data are of relevance for the design of engineered proteins showing higher stability and catalytic activity than other alpha-CAs known to date.
Crystal structure of the most catalytically effective carbonic anhydrase enzyme known, SazCA from the thermophilic bacterium Sulfurihydrogenibium azorense.,De Simone G, Monti SM, Alterio V, Buonanno M, De Luca V, Rossi M, Carginale V, Supuran CT, Capasso C, Di Fiore A Bioorg Med Chem Lett. 2015 May 1;25(9):2002-6. doi: 10.1016/j.bmcl.2015.02.068., Epub 2015 Mar 6. PMID:25817590[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ De Simone G, Monti SM, Alterio V, Buonanno M, De Luca V, Rossi M, Carginale V, Supuran CT, Capasso C, Di Fiore A. Crystal structure of the most catalytically effective carbonic anhydrase enzyme known, SazCA from the thermophilic bacterium Sulfurihydrogenibium azorense. Bioorg Med Chem Lett. 2015 May 1;25(9):2002-6. doi: 10.1016/j.bmcl.2015.02.068., Epub 2015 Mar 6. PMID:25817590 doi:http://dx.doi.org/10.1016/j.bmcl.2015.02.068
