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  • Substrate specificity characterization for eight putative nudix hydrolases. Evaluation of criteria for substrate identification within the Nudix family.

Substrate specificity characterization for eight putative nudix hydrolases. Evaluation of criteria for substrate identification within the Nudix family.

Proteins (2016-09-13)
Vi N Nguyen, Annsea Park, Anting Xu, John R Srouji, Steven E Brenner, Jack F Kirsch
ABSTRACT

The nearly 50,000 known Nudix proteins have a diverse array of functions, of which the most extensively studied is the catalyzed hydrolysis of aberrant nucleotide triphosphates. The functions of 171 Nudix proteins have been characterized to some degree, although physiological relevance of the assayed activities has not always been conclusively demonstrated. We investigated substrate specificity for eight structurally characterized Nudix proteins, whose functions were unknown. These proteins were screened for hydrolase activity against a 74-compound library of known Nudix enzyme substrates. We found substrates for four enzymes with k

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Sigma-Aldrich
Guanosine 5′-monophosphomorpholidate 4-morpholine-N,N′-dicyclohexylcarboxamidine salt, ≥90%