Arco, Jon delPerona Requena, AlmudenaGonzález, LeticiaFernández-Lucas, JesúsGago, FedericoSánchez-Murcia, Pedro A.2024-02-012024-02-012019Org. Biomol. Chem., 2019, 17, 7891–78991477-052010.1039/c9ob01315fhttps://hdl.handle.net/20.500.14352/97640Insight into the catalytic mechanism of Lactobacillus leichmannii nucleoside 2’-deoxyribosyltransferase (LlNDT) has been gained by calculating a quantum mechanics–molecular mechanics (QM/MM) freeenergy landscape of the reaction within the enzyme active site. Our results support an oxocarbenium species as the reaction intermediate and thus an SN1 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.engAttribution 4.0 Internationalhttp://creativecommons.org/licenses/by/4.0/journal article1477-0539https://doi.org/10.1039/c9ob01315fopen access577.154Ciencias Biomédicas23 Química2306 Química Orgánica2302 Bioquímica