Article
A novel monothiol glutaredoxin (Grx4) from Escherichia coli can serve as a substrate for thioredoxin reductase.
The Journal of biological chemistry - 1 Jul 2005
Fernandes Aristi Potamitou, Fladvad Malin, Berndt Carsten, Andrésen Cecilia, Lillig Christopher Horst, Neubauer Peter, Sunnerhagen Maria, Holmgren Arne, Vlamis-Gardikas Alexios
Abstract excerpt
Glutaredoxins are ubiquitous proteins that catalyze the reduction of disulfides via reduced glutathione (GSH). Escherichia coli has three glutaredoxins (Grx1, Grx2, and Grx3), all containing the classic dithiol active site CPYC. We report the cloning, expression, and characterization of a novel monothiol E. coli glutaredoxin, which we name glutaredoxin 4 (Grx4). The protein consists of 115 amino acids (12.7 kDa),...
Topics
- Amino Acid Sequence
- Amino Acids
- Binding Sites
- Cell-Free System
- Circular Dichroism
- Cloning, Molecular
- Disulfides
- Electrons
- Enzyme-Linked Immunosorbent Assay
- Escherichia coli