Article
Mimicking the active site of protein disulfide-isomerase by substitution of proline 34 in Escherichia coli thioredoxin.
The Journal of biological chemistry - 25 May 1991
Krause G, Lundström J, Barea J L, Pueyo de la Cuesta C, Holmgren A
Abstract excerpt
To mimic the active sites (Trp-Cys-Gly-His-Cys) contained in two thioredoxin-like domains of the eukaryotic enzyme protein disulfide-isomerase (PDI, EC 5.3.4.1), the Pro-34 residue of Escherichia coli thioredoxin (Trx) was replaced by His using site-directed mutagenesis. The mutant P34H Trx was isolated in high yield and was stable. The equilibrium between Trx and NADPH in the thioredoxin reductase (TR)-catalyzed...
Topics
- Amino Acid Sequence
- Binding Sites
- Escherichia coli
- Genetic Vectors
- Isomerases
- Molecular Sequence Data
- Mutation
- Oxidation-Reduction
- Protein Conformation
- Protein Disulfide-Isomerases