Boosting the enzymatic activity of CxxC motif-containing PDI family members
Tsubura Kuramochi, Yukino Yamashita, Kenta Arai, Shingo Kanemura, Takahiro Muraoka, Masaki Okumura
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.
Topics & Concepts
ChemistryEnzymeGlutathioneThiolOxidative phosphorylationProtein foldingDisulfide bondBoosting (machine learning)RedoxBiochemistryOxidative foldingFolding (DSP implementation)Combinatorial chemistryCysteineOrganic chemistryComputer scienceMachine learningElectrical engineeringEngineeringPhotosynthetic Processes and MechanismsEndoplasmic Reticulum Stress and DiseaseEnzyme Structure and Function