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. 2023 Mar 28;13:5029. doi: 10.1038/s41598-023-31900-5

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© The Author(s) 2023

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/.

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Proximal hyperacylation is specific to CoA-binding sites. (a) Illustration of the structural similarities between CoA and ADP, ATP, NAD, and NADP. CoA shares a core ADP moiety with ATP, NAD, and NADP, but its added 3′ phosphoryl group may prevent it from fitting in binding sites of those species. (b) Table comparing the relative odds ratios of CoA-reachable lysines being glutarylated by CoA-binding protein and NAD[P]-binding proteins. (c) Relative probability of lysine acylation as a function of a lysine’s distance from the CoA ensemble built into [acyl-]CoA, NAD, and NADP binding sites, showing a lack of acylation enrichment near NAD and NADP binding sites.