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. 2024 Jul 29;22:697. doi: 10.1186/s12967-024-05507-x

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© The Author(s) 2024

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 5 — R101G and R114W variants cause inefficient acetaldehyde metabolism. (A) The Michaelis–Menten plot showing rate of reaction (y-axis) against NAD⁺ concentration for proteins expressed with petDuet-1 plasmid. These in vitro results support inefficient acetaldehyde metabolism for WT/R101G and WT/R114W. (B) V_max of WT/R101G and WT/R114W are significantly different from WT/E504K and wild type ALDH2. K_m of WT/R101G is significantly different from WT/R114W, WT/E504K and wild type ALDH2. n = 5/group, ^*p < 0.01 versus wild type ALDH2 enzyme