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. 2018 Feb 14;8:3042. doi: 10.1038/s41598-018-19991-x

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© The Author(s) 2018

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Schematic of the amino acid deglycation reaction catalyzed by Amadoriase I. The enzyme catalyzes the oxidation of the C-N bond between the nitrogen of the amino acid moiety of the Amadori product and C1 of the fructosyl portion. The reaction results in the Schiff base which is hydrolyzed to yield glucosone and a free amino acid. The reduced FAD is oxidized by an oxygen molecule with the release of hydrogen peroxide. Only relevant hydrogen atoms are shown. Blue font highlights the products of the enzymatic catalysis.