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. 2021 Mar 22;22(6):3232. doi: 10.3390/ijms22063232

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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 (http://creativecommons.org/licenses/by/4.0/).

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Mechanistic details of threonine protease catalysis. (A) The six step mechanism according to Wei et al., 2013 [175]. (B) Free energy profile of the six-step reaction. (C) Inhibitor structures of the yeast 20S proteasome. Upper panel: The epoxide Ac-Ala-Pro-Leu-Leu-ep covalently bound to the Thr1 Oγ atom of the β5 subunit corresponds to the tetrahedral intermediate INT2. The αN-C bond is not shown for clarity in the upper panel (PDB 4QBY). Lower panel: The tBu-Ala-Ala-Ala-aldehyde bound to Thr1 represents the acyl intermediate INT3 (PDB 4Y8L).