Issue 48, 2024

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

Abstract

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.

Graphical abstract: Boosting the enzymatic activity of CxxC motif-containing PDI family members

Supplementary files

Article information

Article type
Communication
Submitted
11 Apr 2024
Accepted
09 May 2024
First published
13 May 2024
This article is Open Access
Creative Commons BY license

Chem. Commun., 2024,60, 6134-6137

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

T. Kuramochi, Y. Yamashita, K. Arai, S. Kanemura, T. Muraoka and M. Okumura, Chem. Commun., 2024, 60, 6134 DOI: 10.1039/D4CC01712A

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