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• W2766402435 startingPage "15556" @default.
• W2766402435 abstract "The synthesis, photophysics, and biochemical utility of a fluorescent NAD+ analogue based on an isothiazolo[4,3-d]pyrimidine core (NtzAD+) are described. Enzymatic reactions, photophysically monitored in real time, show NtzAD+ and NtzADH to be substrates for yeast alcohol dehydrogenase and lactate dehydrogenase, respectively, with reaction rates comparable to that of the native cofactors. A drop in fluorescence is seen as NtzAD+ is converted to NtzADH, reflecting a complementary photophysical behavior to that of the native NAD+/NADH. NtzAD+ and NtzADH serve as substrates for NADase, which selectively cleaves the nicotinamide's glycosidic bond yielding tzADP-ribose. NtzAD+ also serves as a substrate for ribosyl transferases, including human adenosine ribosyl transferase 5 (ART5) and Cholera toxin subunit A (CTA), which hydrolyze the nicotinamide and transfer tzADP-ribose to an arginine analogue, respectively. These reactions can be monitored by fluorescence spectroscopy, in stark contrast to the corresponding processes with the nonemissive NAD+." @default.
• W2766402435 created "2017-11-10" @default.
• W2766402435 creator A5014322047 @default.
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• W2766402435 date "2017-10-27" @default.
• W2766402435 modified "2023-10-18" @default.
• W2766402435 title "Emissive Synthetic Cofactors: An Isomorphic, Isofunctional, and Responsive NAD⁺ Analogue" @default.
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• W2766402435 doi "https://doi.org/10.1021/jacs.7b05852" @default.
• W2766402435 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5766281" @default.
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• W2766402435 hasPublicationYear "2017" @default.
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