Effect of linking allyl and aromatic chains to histidine 170 in horseradish peroxidase
Autor: | Michel Baboulene, Armand Lattes, Jean-Louis Seris, Martine Urrutigoïty, Jerome Souppe |
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Rok vydání: | 1991 |
Předmět: |
Hemeprotein
Stereochemistry Biophysics Heme Biochemistry Horseradish peroxidase Structural Biology Diethyl Pyrocarbonate Histidine Trypsin Molecular Biology Horseradish Peroxidase Binding Sites biology Chemistry Chemical modification Active site Substrate (chemistry) Acetophenones Ligand (biochemistry) Allyl Compounds Kinetics biology.protein Peptides Peroxidase |
Zdroj: | Biochimica et biophysica acta. 1079(2) |
ISSN: | 0006-3002 |
Popis: | Histidine residues in horseradish peroxidase (HRP) were modified chemically with diethyl pyrocarbonate, 4,omega-dibromoacetophenone or diallylpyrocarbonate. Histidines were chosen as His-170, the fifth ligand of the heme iron atom, forms part of the active site of this enzyme. Good yields of hemoprotein were obtained in all cases. Analysis by HPLC of peptides obtained after tryptic digestion showed that His-170 of HRP was in fact modified. The specific activity remained satisfactory after chemical modification of the histidine residues, and so the active site of HRP can thus be altered without a dramatic loss of hemoprotein or peroxidase activity. This may open routes to the preparation of novel biocatalysts. |
Databáze: | OpenAIRE |
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