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Calcineurin Hydrolysis of Para-Nitrophenyl Phosphorothioate

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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+.

Keywords: Calcineurin; Metal-activated enzyme; Substrate analog; Substrate specificity

Document Type: Review Article


Affiliations: Department of Laboratory Medicine and Pathology, University of Minnesota 420 Delaware Street, SE; Mayo Mail Code 609; Minneapolis, MN 55455

Publication date: April 1, 2004

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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