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. 2022 Feb 28;23(5):2682. doi: 10.3390/ijms23052682

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© 2022 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

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Effect of protein post-translational modifications (PTMs) on ALDH activity. Ethanol (acute/low-dose), isoflurane, heat shock factor 1 (HSF1), and melatonin can lead to phosphorylation and activation of aldehyde dehydrogenase 2 (ALDH2) by activating phosphatidylinositol protein kinase C epsilon (PKCε). ALDH2 can also be activated by its acetylation increased by the inactivation of sirtuin 3 (SIRT3) stimulated by ethanol (acute/low-dose). The phosphorylation of ALDH2 promoted by c-Jun NH₂-terminal kinase (JNK) under carbon tetrachloride (CCl₄) exposure as well as the S-nitrosylation and tyrosine nitration of ALDH2 stimulated by ethanol (chronic or excessive abuse), acetaminophen (N-acetyl-p-aminophenol [APAP]), nitric oxide (NO) donor, and ischemia/reperfusion (I/R) injury can inhibit ALDH2 activity. P = phosphorylation; Ac = acetylation; SNO = S-nitrosylation; NO₂ = nitration.