Boosting the enzymatic activity of CxxC motif-containing PDI family members.

Autor: Kuramochi, Tsubura, Yamashita, Yukino, Arai, Kenta, Kanemura, Shingo, Muraoka, Takahiro, Okumura, Masaki
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Zdroj: Chemical Communications; 6/18/2024, Vol. 60 Issue 48, p6134-6137, 4p
Abstrakt: Compounds harboring high acidity and oxidizability of thiol groups permit tuning the redox equilibrium constants of CxxC sites of members of the protein disulphide isomerase (PDI) family and thus can be used to accelerate folding processes and increase the production of native proteins by minimal loading in comparison to glutathione. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index