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. 2021 Nov 12;10(11):1165. doi: 10.3390/biology10111165

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© 2021 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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Diversification of glutathione peroxidases. The ancestral GPx protein was a promiscuous enzyme, regarding its substrate and reducing agent, and it contained a peroxidatic (SH_P) and resolving cysteines (SH_R). Throughout evolution, it has independently evolved to use specific substrates and reducing agents. Further information is described within the “Discussion” section. Reducing agents and substrates displayed indicate preferences, not necessarily exclusivity. GSH: reduced glutathione; Trx: thioredoxin; PDI: protein disulfide isomerase; n: several substrates/reducing agents; LOOH: lipid peroxides; H₂O₂: hydrogen peroxide; SeH and SeCys: selenocysteine; CysR: resolving cysteine; CysP: peroxidatic cysteine.