Peroxidase

Peroxidase is an enzyme found primarily in plants; it can also be found in white blood cells and milk. This enzyme catalyzes the dehydrogenation (oxidation) of various substances in the presence of hydrogen peroxide, which acts as a hydrogen scavenger and is converted to water in this chemical reaction.

Peroxidase is an enzyme found primarily in plants; it can also be found in white blood cells and milk. This enzyme catalyzes the dehydrogenation (oxidation) of various substances in the presence of hydrogen peroxide, which acts as a hydrogen scavenger and is converted to water in this chemical reaction.

Peroxidase plays an important role in protecting plants from pathogens, and is also involved in the processes of lignification and suberinization of cell walls. In addition, this enzyme is involved in the oxidation reactions of various substrates, such as phenols, aromatic amines, indoles, etc. In plants, several isoforms of peroxidase are isolated, localized in different cellular compartments and performing specific functions.

Peroxidases are a widespread class of enzymes that participate in various biochemical processes to protect plants from oxidative stress that occurs during fluctuations in pH and temperature. These small proteins, about 20 kDa in size, catalyze the oxidation of a wide range of organic substrates to peroxide or H2O2, such as carbohydrate dehydrogenases, nitric oxide, L-cystine, lipofuscin and phenolic compounds. All of these compounds can be toxic to the body and if not removed by the peroxide oxidase enzyme, they lead to various diseases. In this study, we attempt to describe the structure, function, biochemical properties of this important class of enzymes, as well as their role in crop production

Plants and animals possess peroxidases. They are single-chain glycoproteins containing 60-70 amino acid residues twisted into an α-helix (see Fig. 1). Several cysteine ​​residues (in the form of disulfide bridges) facing the inner edge of the structure are conformationally fixed and are not hydroxylated. This configuration stabilizes the fiber and makes peroxidase more resistant to thermolysis and proteolytic degradation. In addition, the large size of the enzyme binds a protective chaperone protein, preventing