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Catalase is a common enzyme found in nearly all living organisms exposed to oxygen which catalyzes the decomposition of hydrogen peroxide to water and oxygen. It is a very important enzyme in protecting the cell from oxidative damage by reactive oxygen species (ROS). Catalase has one of the highest turnover numbers of all enzymes; one catalase molecule can convert millions of hydrogen peroxide molecules to water and oxygen each second.
Glutathione peroxidase (GPx) is the general name of an enzyme family with peroxidase activity whose main biological role is to protect the organism from oxidative damage. The biochemical function of glutathione peroxidase is to reduce lipid hydroperoxides to their corresponding alcohols and to reduce free hydrogen peroxide to water.
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:
Ascorbate peroxidase (or L-ascorbate peroxidase, APX) (EC 1.11.1.11) is an enzyme that catalyzes the chemical reaction
(S)-Tetrahydroberberine oxidase is an enzyme that catalyzes the final transformation in the biosynthesis of berberine, a quaternary benzylisoquinoline alkaloid of the protoberberine structural subgroup. This reaction pathway catalyzes the four-electron oxidation of (S)-tetrahydroberberine in the presence of oxygen to produce berberine and hydrogen peroxide as products.
In enzymology, a 5beta-cholestane-3alpha,7alpha-diol 12alpha-hydroxylase (EC 1.14.13.96) is an enzyme that catalyzes the chemical reaction
In enzymology, a peptidylglycine monooxygenase (EC 1.14.17.3) is an enzyme that catalyzes the chemical reaction
In enzymology, a choline oxidase (EC 1.1.3.17) is an enzyme that catalyzes the chemical reaction
In enzymology, a lignin peroxidase (EC 1.11.1.14) is an enzyme that catalyzes the chemical reaction
In enzymology, a manganese peroxidase (EC 1.11.1.13) is an enzyme that catalyzes the chemical reaction
In enzymology, a NADH peroxidase (EC 1.11.1.1) is an enzyme that catalyzes the chemical reaction
Amine oxidase (copper-containing) (AOC) (EC 1.4.3.21 and EC 1.4.3.22; formerly EC 1.4.3.6) is a family of amine oxidase enzymes which includes both primary-amine oxidase and diamine oxidase; these enzymes catalyze the oxidation of a wide range of biogenic amines including many neurotransmitters, histamine and xenobiotic amines. They act as a disulphide-linked homodimer. They catalyse the oxidation of primary amines to aldehydes, with the subsequent release of ammonia and hydrogen peroxide, which requires one copper ion per subunit and topaquinone as cofactor:
In enzymology, a D-glutamate oxidase (EC 1.4.3.7) is an enzyme that catalyzes the chemical reaction
In enzymology, an L-amino acid oxidase (LAAO) (EC 1.4.3.2) is an enzyme that catalyzes the chemical reaction
In enzymology, a (R)-6-hydroxynicotine oxidase (EC 1.5.3.6) is an enzyme that catalyzes the chemical reaction
In enzymology, a (S)-6-hydroxynicotine oxidase (EC 1.5.3.5) is an enzyme that catalyzes the chemical reaction
Haem peroxidases (or heme peroxidases) are haem-containing enzymes that use hydrogen peroxide as the electron acceptor to catalyse a number of oxidative reactions. Most haem peroxidases follow the reaction scheme:
Versatile peroxidase (EC 1.11.1.16, VP, hybrid peroxidase, polyvalent peroxidase) is an enzyme with systematic name reactive-black-5:hydrogen-peroxide oxidoreductase. This enzyme catalyses the following chemical reaction
Eosinophil peroxidase is an enzyme found within the eosinophil granulocytes, innate immune cells of humans and mammals. This oxidoreductase protein is encoded by the gene EPX, expressed within these myeloid cells. EPO shares many similarities with its orthologous peroxidases, myeloperoxidase (MPO), lactoperoxidase (LPO), and thyroid peroxidase (TPO). The protein is concentrated in secretory granules within eosinophils. Eosinophil peroxidase is a heme peroxidase, its activities including the oxidation of halide ions to bacteriocidal reactive oxygen species, the cationic disruption of bacterial cell walls, and the post-translational modification of protein amino acid residues.
KatG is an enzyme that functions as both catalase and peroxidase. Its mutation is the cause for Mycobacterium resistance with the drug isoniazid, which targets the mycolic acids within the tuberculosis bacteria. Due to both its catalase and peroxidase activity, this enzyme protects M. Tuberculosis against reactive oxygen species. M. tuberculosis' survival within macrophages depends on the KatG enzyme.
References
- ↑ Loewen PC, Triggs BL, George CS, Hrabarchuk BE (May 1985). "Genetic mapping of katG, a locus that affects synthesis of the bifunctional catalase-peroxidase hydroperoxidase I in Escherichia coli". Journal of Bacteriology. 162 (2): 661–7. doi:10.1128/JB.162.2.661-667.1985. PMC 218901 . PMID 3886630.
- ↑ Hochman A, Goldberg I (April 1991). "Purification and characterization of a catalase-peroxidase and a typical catalase from the bacterium Klebsiella pneumoniae". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1077 (3): 299–307. doi:10.1016/0167-4838(91)90544-a. PMID 2029529.
- ↑ Fraaije MW, Roubroeks HP, Hagen WR, Van Berkel WJ (January 1996). "Purification and characterization of an intracellular catalase-peroxidase from Penicillium simplicissimum". European Journal of Biochemistry. 235 (1–2): 192–8. CiteSeerX 10.1.1.317.1785 . doi:10.1111/j.1432-1033.1996.00192.x. PMID 8631329.
- ↑ Bertrand T, Eady NA, Jones JN, Nagy JM, Jamart-Grégoire B, Raven EL, Brown KA (September 2004). "Crystal structure of Mycobacterium tuberculosis catalase-peroxidase". The Journal of Biological Chemistry. 279 (37): 38991–9. doi: 10.1074/jbc.M402382200 . PMID 15231843.
- ↑ Vlasits J, Jakopitsch C, Bernroitner M, Zamocky M, Furtmüller PG, Obinger C (August 2010). "Mechanisms of catalase activity of heme peroxidases". Archives of Biochemistry and Biophysics. 500 (1): 74–81. doi:10.1016/j.abb.2010.04.018. PMID 20434429.
