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. 2020 Sep 1;8:822. doi: 10.3389/fcell.2020.00822

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Copyright © 2020 Xu, Gan, Gao, Huang, Wu, Zhang, Wang and Sheng.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Caffeine directly binds to SIRT3 to enhance its substrate binding affinity. (A) Enzymatic reaction involving SIRT3. (B) Caffeine binds to SIRT3, with K_D = 6.858 × 10^{– 7} M. (C) NAD⁺ does not directly interact with SIRT3. (D) The acetylated substrate p53-Ac binds to SIRT3, with K_D = 2.434 × 10^{– 5} M. (E) NAD⁺ is the coenzyme for the SIRT3 deacetylation reaction, and its presence enhances the binding affinity of p53-Ac to SIRT3, with K_D = 2.800 × 10^{– 6} M. (F) Addition of caffeine enhances the binding affinity between SIRT3 and its substrate, with K_D = 2.696 × 10^{– 6} M. (G) The binding affinity between SIRT3 and its substrate is increased in the presence of caffeine and NAD⁺, with K_D = 4.076 × 10^{– 7} M. All SPR experiments were carried out using a Biacore S200 instrument (Biacore, GE Healthcare). The data represented here represent one of three independent experiments with similar results.