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Article Dans Une Revue Cell Chemical Biology Année : 2018

Structural Insights into the Forward and Reverse Enzymatic Reactions in Human Adenine Phosphoribosyltransferase

Résumé

Highlights d Human APRT catalyzes the transformation of adenine into AMP and vice versa d Complexes with substrates in both directions of the reaction highlight key residues d The catalytic flexible loop dynamic is revealed by an in crystallo activity d Tyr105 is essential for cell growth by facilitating the forward reaction In Brief APRT is a key enzyme in the purine salvage pathway in prokaryotes and eukaryotes. Huyet et al., by using in vitro, cellular, and in crystallo enzymatic analyses, reveal that a hydroxyl group in a conserved tyrosine controls the protein dynamics and the catalytic efficiencies of the forward and reverse reactions.
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hal-02346886 , version 1 (05-11-2019)

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Jessica Huyet, Mohammad Ozeir, Marie-Claude Burgevin, Anne Olivier-Bandini, Franck Auge, et al.. Structural Insights into the Forward and Reverse Enzymatic Reactions in Human Adenine Phosphoribosyltransferase. Cell Chemical Biology, 2018, 25 (6), pp.666-676.e4. ⟨10.1016/j.chembiol.2018.02.011⟩. ⟨hal-02346886⟩
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