Horseradish peroxidase
From Proteopedia
FunctionHorseradish peroxidase (HRP) catalyzes the oxidation of luminol to 3-aminophthalate using hydrogen peroxide. The reaction is accompanied by emission of light. In the presence of chemicals, particularly – p-iodophenol, the light emission is enhanced 1000-fold. Upon addition of the proper substrate, the HRP complex emits colored light. HRP contains a heme group[1]. RelevanceHRP isozyme C1a is widely used for detection of a labeled molecule to which it conjugates. Structural highlightsThe active site contains a heme group and the substrate benzhydroxamic acid[2]. Fe coordination site. Water molecules shown as red spheres. |
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3D structures of horseradish peroxidase
Updated on 22-May-2023
References
- ↑ Veitch NC. Horseradish peroxidase: a modern view of a classic enzyme. Phytochemistry. 2004 Feb;65(3):249-59. PMID:14751298
- ↑ Henriksen A, Schuller DJ, Meno K, Welinder KG, Smith AT, Gajhede M. Structural interactions between horseradish peroxidase C and the substrate benzhydroxamic acid determined by X-ray crystallography. Biochemistry. 1998 Jun 2;37(22):8054-60. PMID:9609699 doi:10.1021/bi980234j
