Article
Characterisation of a haem active-site mutant of horseradish peroxidase, Phe41----Val, with altered reactivity towards hydrogen peroxide and reducing substrates.
European journal of biochemistry - 15 Jul 1992
Smith A T, Sanders S A, Thorneley R N, Burke J F, Bray R R
Abstract excerpt
A horseradish peroxidase variant ([F41V] HRP-C*), in which Val replaces the conserved Phe at position 41 adjacent to the distal His, has been constructed. Its composition and spectroscopic, catalytic and substrate-binding properties were compared with those of the wild-type recombinant (HRP-C*) a...
Topics
- Amino Acid Sequence
- Base Sequence
- Binding Sites
- Heme
- Horseradish Peroxidase
- Hydrogen Peroxide
- Kinetics
- Models, Molecular
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- Oligodeoxyribonucleotides
- Oxidation-Reduction
- Phenylalanine
- Recombinant Proteins
- Spectrum Analysis
- Structure-Activity Relationship
- Valine