Article
Role of arginine 38 in horseradish peroxidase. A critical residue for substrate binding and catalysis.
The Journal of biological chemistry - 23 Feb 1996
Rodriguez-Lopez J N, Smith A T, Thorneley R N
Abstract excerpt
The observed pseudo-first order rate constant for the reaction between a horseradish peroxidase (HRP) variant (R38L)HRPC* and hydrogen peroxide saturates at high peroxide concentrations (Km = 11. 8 mm). The data are consistent with a two-step mechanism involving the formation of an HRP-H2O2 intermediate (k = 1.1 x 10(4) m-1 s-1) whose conversion to compound I is rate-limiting (k = 142 s-1) suggesting that Arg-38...
Topics
- Amino Acid Sequence
- Arginine
- Base Sequence
- Binding Sites
- Catalysis
- Cresols
- DNA Primers
- Genes, Synthetic
- Genetic Variation
- Guaiacol
- Horseradish Peroxidase
- Hydrogen Peroxide
- Kinetics
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Point Mutation
- Polymerase Chain Reaction
- Recombinant Proteins