Publications by authors named "Liege A Kawai"
Article Synopsis
- The thioredoxin system is crucial for pathogens like Corynebacterium pseudotuberculosis, helping them manage oxidative stress and maintain proper protein function through disulfide bond formation.
- Despite the unknown specific role of TrxA1 in this bacterium, the conservation of its active site across different thioredoxins suggests its importance.
- Testing revealed that compounds such as suramin and hesperetin effectively inhibited TrxA1's activity by about 80%, indicating their potential as lead molecules for developing targeted inhibitors against this pathogen.
Article Synopsis
- Glutaredoxin A1, a mycoredoxin protein from Corynebacterium pseudotuberculosis, was overexpressed and purified to study its behavior in different redox environments.
- The study measured the enzyme's ability to reduce insulin using a quantitative assay, finding that Glutaredoxin A1 accelerated insulin reduction under specific conditions, particularly at pH 7.4.
- Research also investigated potential inhibitors for Glutaredoxin A1, highlighting the effects of ligands such as heparin, suramin, hesperetin, and hesperidin on its activity and structure.
The conformational stability of the Cold shock protein A (CspA) from C. pseudotuberculosis (Cp), a nucleic acid binding protein in function of pH and salt concentration was examined by using differential scanning calorimetry and CD spectroscopy in combination with computational analysis to identify the specify amino acids undergoing change. Our approach identified a sodiumbinding site in CpCspA and at pH 8.
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