Version 1
: Received: 11 May 2024 / Approved: 13 May 2024 / Online: 14 May 2024 (08:20:30 CEST)
How to cite:
Wierzchowski, J. .-.; Stachelska-Wierzchowska, A. .-. Chemo-Enzymatic Generation of Highly Fluorescent Nucleoside Analogs Using Purine-Nucleoside Phosphorylase – A Mini-Review. Preprints2024, 2024050891. https://doi.org/10.20944/preprints202405.0891.v1
Wierzchowski, J. .-.; Stachelska-Wierzchowska, A. .-. Chemo-Enzymatic Generation of Highly Fluorescent Nucleoside Analogs Using Purine-Nucleoside Phosphorylase – A Mini-Review. Preprints 2024, 2024050891. https://doi.org/10.20944/preprints202405.0891.v1
Wierzchowski, J. .-.; Stachelska-Wierzchowska, A. .-. Chemo-Enzymatic Generation of Highly Fluorescent Nucleoside Analogs Using Purine-Nucleoside Phosphorylase – A Mini-Review. Preprints2024, 2024050891. https://doi.org/10.20944/preprints202405.0891.v1
APA Style
Wierzchowski, J. . ., & Stachelska-Wierzchowska, A. . . (2024). Chemo-Enzymatic Generation of Highly Fluorescent Nucleoside Analogs Using Purine-Nucleoside Phosphorylase – A Mini-Review. Preprints. https://doi.org/10.20944/preprints202405.0891.v1
Chicago/Turabian Style
Wierzchowski, J.-. and Alicja - Stachelska-Wierzchowska. 2024 "Chemo-Enzymatic Generation of Highly Fluorescent Nucleoside Analogs Using Purine-Nucleoside Phosphorylase – A Mini-Review" Preprints. https://doi.org/10.20944/preprints202405.0891.v1
Abstract
Reviewed are recent efforts leading to chemo-enzymatic syntheses of strongly fluorescent ribosides of nucleobase analogs, potentially applicable in analytical biochemistry and cell biology. Described are syntheses and properties of fluorescent purine, 8-azapurine and etheno-purine ribosides, obtained using various types of the purine nucleoside phosphorylase (PNP) as catalysts of ribosylation, and -ribose-1-phosphate (r1P) as a second substrate. In several instances, the ribosylation sites were different than the canonical purine N9. Some of the obtained ribosides show fluorescence yields close to 100%. Their main applications are assays of PNP, nucleoside hydrolases, and other enzyme activities both in vitro and, possibly, within the living cells, using fluorescence microscopy.
Copyright:
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