Comparative CO and SiO hydratase activity of an enzyme from the siliceous demosponge Suberitesdomuncula.

Silicase, an enzyme that catalyzes the hydrolysis of silicon-oxygen bonds, is a crucial player in breaking down silicates into silicic acid, particularly in organisms like aquatic sponges with siliceous skeletons. Despite its significance, our understanding of silicase remains limited. This study comprehensively examines silicase from the demosponge Suberites domuncula, focusing on its kinetics toward CO as a substrate, as well as its silicase and esterase activity. It investigates inhibition and activation profiles with a range of inhibitors and activators belonging to various classes. By comparing its esterase activity to human carbonic anhydrase II, we gain insights into its enzymatic properties. Moreover, we investigate silicase's inhibition and activation profiles, providing valuable information for potential applications. We explore the evolutionary relationship of silicase with related enzymes, revealing potential functional roles in biological systems. Additionally, we propose a biochemical mechanism through three-dimensional modeling, shedding light on its catalytic mechanisms and structural features for both silicase activity and CO hydration. We highlight nature's utilization of enzymatic expertise in silica metabolism. This study enhances our understanding of silicase and contributes to broader insights into ecosystem functioning and Earth's geochemical cycles, emphasizing the intricate interplay between biology and the environment.