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. 2022 Jan 27;12:1536. doi: 10.1038/s41598-022-05195-x

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© The Author(s) 2022

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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Structural mapping of important individual residues onto hOTC monomeric structure. A structure of the hOTC monomer (white cartoon) bound to a substrate analog (N-phosphonoacetyl-L-ornithine, cyan sticks) (PDB: 1OTH) is used to highlight amino acid positions mutated in the VAE-sampled sequences (magenta sticks). (A) Amino acid positions of mutations that have a beneficial/positive effect on T_m and specific activity. (B) Amino acid positions of mutations that have a beneficial/positive effect on either T_m or specific activity, but not both. (C) Amino acid positions of mutations that negatively affect T_m and specific activity. (D–G) Close-up views of A217, A135 and G83, the small beta-sheet consisting of I159 and I160 and the three important lysines at K68, K70 and K353.