title: Horseradish peroxidase: modulation of properties by chemical modification of protein and heme.
abstract: Horseradish peroxidase (HRP) is one of the most studied enzymes of the plant peroxidase superfamily. HRP is also widely used in different bioanalytical applications and diagnostic kits. The methods of genetic engineering and protein design are now widely used to study the catalytic mechanism and to improve properties of the enzyme. Here we review the results of another approach to HRP modification-through the chemical modification of amino acids or prosthetic group of the enzyme. Computer models of HRPs with modified hemes are in good agreement with the experimental data.
authors.affiliation: Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russia.
authors.forename: G S
authors.initials: GS
authors.lastname: Zakharova
authors.forename: I V
authors.initials: IV
authors.lastname: Uporov
authors.forename: V I
authors.initials: VI
authors.lastname: Tishkov
mesh_terms: D019943:Amino Acid Substitution; D003067:Coenzymes / Q000138:chemical synthesis / Q000737:chemistry*; D003198:Computer Simulation; D006418:Heme / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000737:chemistry*; D006735:Horseradish Peroxidase / Q000737:chemistry / Q000235:genetics; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D010940:Plant Proteins / Q000737:chemistry* / Q000235:genetics; D055550:Protein Stability
chemical_list: D003067:Coenzymes; D010940:Plant Proteins; D006418:Heme; D006735:Horseradish Peroxidase