Article
Cloning, overexpression, and characterization of glutaredoxin 2, an atypical glutaredoxin from Escherichia coli.
The Journal of biological chemistry - 25 Apr 1997
Vlamis-Gardikas A, Aslund F, Spyrou G, Bergman T, Holmgren A
Abstract excerpt
Glutaredoxin 2 (Grx2) from Escherichia coli catalyzes GSH-disulfide oxidoreductions via two redox-active cysteine residues, but in contrast to glutaredoxin 1 (Grx1) and glutaredoxin 3 (Grx3), is not a hydrogen donor for ribonucleotide reductase. To characterize Grx2, a chromosomal fragment contai...
Topics
- Amino Acid Sequence
- Bacterial Proteins
- Base Sequence
- Cloning, Molecular
- Escherichia coli
- Genes, Bacterial
- Glutaredoxins
- Glutathione
- Insulin
- Membrane Proteins
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Oxidation-Reduction
- Oxidoreductases
- Protein Biosynthesis
- Protein Structure, Secondary
- Proteins