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Catalase-peroxidase (EC 1.11.1.21, katG ... This enzyme is a strong catalase with H 2 O 2 as donor which releases O 2. References External links ...
Catalase is a tetramer of four polypeptide chains, each over 500 amino acids long. [7] It contains four iron-containing heme groups that allow the enzyme to react with hydrogen peroxide. The optimum pH for human catalase is approximately 7, [8] and has a fairly broad maximum: the rate of reaction does not change appreciably between pH 6.8 and 7 ...
It is thought that catalase-peroxidase provides protection to cells under oxidative stress. [5] Class II consists of secretory fungal peroxidases: ligninases, or lignin peroxidases (LiPs), and manganese-dependent peroxidases (MnPs). These are monomeric glycoproteins involved in the degradation of lignin. In MnP, Mn 2+ serves as the reducing ...
Peroxidase can be used for treatment of industrial waste waters. For example, phenols, which are important pollutants, can be removed by enzyme-catalyzed polymerization using horseradish peroxidase. Thus phenols are oxidized to phenoxy radicals, which participate in reactions where polymers and oligomers are produced that are less toxic than ...
Additionally, enzymes including superoxide dismutase, catalase, and peroxidase contribute to the oxidation response by reducing the presence of hydrogen peroxide, which is a prevalent precursor of the hydroxyl radical (OH•).
The cytosols of virtually all eukaryotic cells contain a SOD enzyme with copper and zinc (Cu-Zn-SOD). For example, Cu-Zn-SOD available commercially is normally purified from bovine red blood cells. The bovine Cu-Zn enzyme is a homodimer of molecular weight 32,500. It was the first SOD whose atomic-detail crystal structure was solved, in 1975. [10]
Cytochrome c peroxidase, or CCP, is a water-soluble heme-containing enzyme of the peroxidase family that takes reducing equivalents from cytochrome c and reduces hydrogen peroxide to water: CCP + H 2 O 2 + 2 ferrocytochrome c + 2H + → CCP + 2H 2 O + 2 ferricytochrome c
Prxs were historically divided into three (mechanistic) classes: Typical 2-Cys Prxs; Atypical 2-Cys Prxs and; 1-Cys Prxs. The designation of "1-Cys" and "2-Cys" Prxs was introduced in 1994 [2] as it was noticed that, among the 22 Prx sequences known at the time, only one Cys residue was absolutely conserved; this is the residue now recognized as the (required) peroxidatic cysteine, C P.