Calcineurin hydrolysis of para-nitrophenyl phosphorothioate.
para-Nitrophenyl phosphorothioate (pNPT) was hydrolyzed by calcineurin at initial rates slightly, but comparable to rates for para-nitrophenyl phosphate (pNPP). Kinetic characterization yielded higher estimates for both Km and Vmax compared to pNPP. Metal ion activation of phosphorothioate hydrolysis was more promiscuous. Unlike the hydrolysis of with pNPP, Ca2+, Mg2+, and Ba2+ activated calcineurin as well as Mn2+.
Spannaus-Martin
Donna J
DJ
Department of Laboratory Medicine and Pathology, University of Minnesota, 420 Delaware Street, SE, Mayo Mail Code 609, Minneapolis, MN 55455, USA.
Martin
Bruce L
BL
D000818:Animals; D019703:Calcineurin / Q000737:chemistry* / Q000378:metabolism; D002417:Cattle; D004789:Enzyme Activation; D004793:Enzyme Reactivators / Q000737:chemistry* / Q000378:metabolism; D006868:Hydrolysis; D007700:Kinetics; D008670:Metals / Q000737:chemistry* / Q000378:metabolism; D009943:Organophosphorus Compounds / Q000737:chemistry* / Q000378:metabolism; D013379:Substrate Specificity
D004793:Enzyme Reactivators; D008670:Metals; D009943:Organophosphorus Compounds; D019703:Calcineurin