descriptionPublicationkeyboard_double_arrow_right Article 01 Jul 1979 English Publisher:Elsevier BVJournal:Biochemical and Biophysical Research Communications, volume 89, pages 764-768 (issn: 0006-291X,

Authors: Tsunehisa Araiso; H. Brian Dunford;

doi: 10.1016/0006-291x(79)90695-8

pmid: 486194

Horseradish peroxidase. XXXVI. On the difference between peroxidase and metmyoglobin

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Abstract

Abstract A mechanism for the reaction of hydrogen peroxide with horseradish peroxidase is proposed which involves the catalytic activity of the carboxylate side chain of aspartate residue 43. The corresponding residue in the active site of metmyoglobin is glycine E8, which explains the inability of metmyoglobin to form compound I. Certain aspects of the proposed peroxidase mechanism may be relevant to the catalytic triad for the serine proteases.

Related Organizations

University of Alberta
Canada

Keywords

Structure-Activity Relationship, Binding Sites, Peroxidases, Myoglobin, Amino Acid Sequence, Horseradish Peroxidase, Peptide Fragments

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