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• W2010018654 abstract "Adenylation/adenylate-forming enzymes catalyze the activation of a carboxylic acid at the expense of ATP to form an acyl-adenylate intermediate and pyrophosphate (PPi). In a second half-reaction, adenylation enzymes catalyze the transfer of the acyl moiety of the acyl-adenylate onto an acceptor molecule, which can be either a protein or a small molecule. We describe the design, development, and validation of a coupled continuous spectrophotometric assay for adenylation enzymes that employs hydroxylamine as a surrogate acceptor molecule, leading to the formation of a hydroxamate. The released pyrophosphate from the first half-reaction is measured using the pyrophosphatase–purine nucleoside phosphorylase coupling system with the chromogenic substrate 7-methylthioguanosine (MesG). The coupled hydroxamate–MesG assay is especially useful for characterizing the activity and inhibition of adenylation enzymes that acylate a protein substrate and/or fail to undergo rapid ATP–PPi exchange." @default.
• W2010018654 created "2016-06-24" @default.
• W2010018654 creator A5021345648 @default.
• W2010018654 creator A5042757158 @default.
• W2010018654 date "2010-09-01" @default.
• W2010018654 modified "2023-10-17" @default.
• W2010018654 title "A continuous kinetic assay for adenylation enzyme activity and inhibition" @default.
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• W2010018654 doi "https://doi.org/10.1016/j.ab.2010.04.033" @default.
• W2010018654 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2900519" @default.
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