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Enzyme Activity Measurement for Peroxidase

Creative Enzymes is the leading company in the field of enzyme activity assays, which is well known to provide the best customer satisfaction. We have a group of brilliant scientists who have been working on enzyme activity assays for many years. Here we are proud to offer the catalytic activity assay for peroxidase. The unique advantage of our spectrophotometric analysis allows us to surpass our competitors and ensures the reliability of the test results.

Peroxidases (EC 1.11.1.7) are a large family of ubiquitous oxidative heme-containing enzymes which can be isolated from plants, bacteria, and fungi, as well as mammalian sources. The peroxidases belong to a family of glycoproteins containing iron atoms as a prosthetic group and different quantities of carbohydrate residues. Peroxidases are involved in multiple biological processes which include cell wall synthesis and degradation, stress response, signaling during oxidative stress, and removal of xenobiotics.

Reactions catalyzed by peroxidase. Figure 1: Reactions catalyzed by peroxidase.
Reference: Berglund G I et al. Nature, 2002, 417(6887): 463-468.

Heme-containing redox enzymes join in a strikingly diverse range of chemistry, yet all biological oxidation reactions catalyzed by these enzymes involve very similar high-oxidation-state intermediates whose reactivity is modulated by the protein environment. The main overall reaction catalyzed by peroxidases can be summarized as H2O2 + 2RH → 2H2O + 2R (where RH stands for a reducing substrate and R is a free radical product). This reaction involves several steps with two highly oxidized heme intermediates, compound I and compound II (Figure 1). Additionally, peroxidases can also convert hydrogen peroxide to water and dioxygen (2H2O2 → 2H2O + O2). This is the catalase-like activity of the enzyme, but in contrast to true catalases, the rate of this reaction in peroxidases is slow. Peroxidases activity can be influenced by small molecule ligands, including carbon monoxide, cyanide, azide, and fluoride, formate and acetate. Both acetate and formate bind to ferric horseradish peroxidase, and formate binds more strongly than acetate.

Additionally, peroxidases also play an important role in the environment, agriculture and manufacturing industries. For example, peroxidases can be used for the treatment of industrial waste waters; peroxidases can be used in many manufacturing processes (e.g., as adhesives for linings of drums, cans and car parts). Moreover, peroxidases could be used to polymerize anilines and phenols in organic solvent matrices. Therefore, more detailed information about peroxidases should be obtained due to its significant value. However, the enzymatic activity assay of this enzyme has not been well established probably because of its complicated chemistry behind the enzymatic reaction and its activity regulation by small molecule ligands. Fortunately, Creative Enzymes, equipped with the leading technique, the up-to-date experiment instruments, and the experienced technical experts, promises our customers to supply the most precise test results for the activity quantification of peroxidases. Creative Enzymes is always looking forward to collaborating with you!

The crystal structure of ferric horseradish peroxidase C1A from Armoracia rusticana. Figure 2: The crystal structure of ferric horseradish peroxidase C1A from Armoracia rusticana.
PDB: 1W4W



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