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Título: | Reaction mechanism of nucleoside 2′-deoxyribosyltransferases: Free-energy landscape supports an oxocarbenium ion as the reaction intermediate |
Autor: | Del Arco, J.; Perona, Almudena CSIC ORCID CVN; González, L.; Fernández-Lucas, J.; Gago, Federico CSIC ORCID; Sánchez-Murcia, Pedro A. CSIC ORCID | Fecha de publicación: | 2019 | Editor: | Royal Society of Chemistry (UK) | Citación: | Organic and Biomolecular Chemistry 17: 7891-7899 (2019) | Resumen: | Insight into the catalytic mechanism of Lactobacillus leichmannii nucleoside 2′-deoxyribosyltransferase (LlNDT) has been gained by calculating a quantum mechanics-molecular mechanics (QM/MM) free-energy landscape of the reaction within the enzyme active site. Our results support an oxocarbenium species as the reaction intermediate and thus an S1 reaction mechanism in this family of bacterial enzymes. Our mechanistic proposal is validated by comparing experimental kinetic data on the impact of the single amino acid replacements Tyr7, Glu98 and Met125 with Ala, Asp and Ala/norLeu, respectively, and accounts for the specificity shown by this enzyme on a non-natural substrate. This work broadens our understanding of enzymatic C-N bond cleavage and C-N bond formation. | Versión del editor: | http://dx.doi.org/10.1039/c9ob01315f | URI: | http://hdl.handle.net/10261/200973 | DOI: | 10.1039/c9ob01315f | Identificadores: | doi: 10.1039/c9ob01315f issn: 1477-0520 e-issn: 1477-0539 |
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