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Protein & Peptide Letters


ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Calcineurin Hydrolysis of Para-Nitrophenyl Phosphorothioate

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

Volume 11, Issue 2, 2004

Page: [149 - 158] Pages: 10

DOI: 10.2174/0929866043478338

Price: $65


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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