Biomolecules, Volume 10, Issue 4 (April 2020) – 169 articles
Cover Story (view full-size image): Carbonic Anhydrase II (CAII) is a ubiquitously expressed zinc-metalloenzyme highly expressed in red blood cells. This enzyme catalyzes the reversible hydration/dehydration of CO2/ HCO3-, while also having an innate carboxylesterase activity. Aspirin (acetyl-salicylic acid), one of the most commonly used drugs globally, has been shown to have a short half-life in the blood of ~15 minutes. Here, we report that CAII, and specifically its carboxylesterase activity, is responsible for aspirin’s short half-life. Furthermore, the esterase product, salicylic acid, acts as an inhibitor of CAII once formed, blocking the active site. Thus, CAII not only degrades aspirin but, in turn, aspirin also acts as a suicide inhibitor of CAII within red blood cells. View this paper.
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