Calcineurin Hydrolysis of Para-Nitrophenyl Phosphorothioate

Donna   J.   Spannaus-Martin; Bruce   L.   Martin

doi:10.2174/0929866043478338

Abstract

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 specificity,, Substrate analog.

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Protein & Peptide Letters

Title: Calcineurin Hydrolysis of Para-Nitrophenyl Phosphorothioate

Volume: 11 Issue: 2

Author(s): Donna J. Spannaus-Martin and Bruce L. Martin

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Keywords: Calcineurin,, Metal-activated enzyme,, Substrate specificity,, Substrate analog.

Abstract: 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+.

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Spannaus-Martin J. Donna and Martin L. Bruce, Calcineurin Hydrolysis of Para-Nitrophenyl Phosphorothioate, Protein & Peptide Letters 2004; 11 (2) . https://dx.doi.org/10.2174/0929866043478338