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

Author:

Kuramochi Tsubura12,Yamashita Yukino3,Arai Kenta45ORCID,Kanemura Shingo1ORCID,Muraoka Takahiro36ORCID,Okumura Masaki12ORCID

Affiliation:

1. Frontier Research Institute for Interdisciplinary Sciences, Tohoku University, 6-3 Aramaki-Aza-Aoba, Aoba-ku, Sendai, Miyagi, 980-8578, Japan

2. Department of Molecular and Chemical Life Sciences, Graduate School of Life Sciences, Tohoku University, 2-1-1 Katahira, Aoba-ku, Sendai, Miyagi, 980-8577, Japan

3. Department of Applied Chemistry, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei, Tokyo 184-8588, Japan

4. Department of Chemistry, School of Science, Tokai University, Kitakaname, Hiratsuka-shi, Kanagawa 259-1292, Japan

5. Institute of Advanced Biosciences, Tokai University, Kitakaname, Hiratsuka-shi, Kanagawa 259-1292, Japan

6. Kanagawa Institute of Industrial Science and Technology, 3-2-1 Sakato, Takatsu-ku, Kawasaki, Kanagawa 213-0012, Japan

Abstract

Compounds harboring high acidity and oxidizability of thiol groups permit tuning the redox equilibrium constants of CxxC sites of the PDI family enzymes and thus can be used to promote oxidative folding and increase the native protein productions by minimal loading as compared to glutathione.

Funder

Japan Society for the Promotion of Science

Fusion Oriented REsearch for disruptive Science and Technology

Takeda Science Foundation

Mochida Memorial Foundation for Medical and Pharmaceutical Research

Naito Foundation

Uehara Memorial Foundation

Terumo Foundation for Life Sciences and Arts

Astellas Foundation for Research on Metabolic Disorders

Asahi Glass Foundation

Daiichi Sankyo Foundation of Life Science

Sumitomo Foundation

Japan Science and Technology Agency

Publisher

Royal Society of Chemistry (RSC)

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