Related Research Articles
A hemeprotein, or heme protein, is a protein that contains a heme prosthetic group. They are a very large class of metalloproteins. The heme group confers functionality, which can include oxygen carrying, oxygen reduction, electron transfer, and other processes. Heme is bound to the protein either covalently or noncovalently or both.
Peroxidases or peroxide reductases are a large group of enzymes which play a role in various biological processes. They are named after the fact that they commonly break up peroxides.
Heme, or haem, is a precursor to hemoglobin, which is necessary to bind oxygen in the bloodstream. Heme is biosynthesized in both the bone marrow and the liver.
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:
Cytochromes P450 are a superfamily of enzymes containing heme as a cofactor that mostly, but not exclusively, function as monooxygenases. In mammals, these proteins oxidize steroids, fatty acids, and xenobiotics, and are important for the clearance of various compounds, as well as for hormone synthesis and breakdown. In 1963, Estabrook, Cooper, and Rosenthal described the role of CYP as a catalyst in steroid hormone synthesis and drug metabolism. In plants, these proteins are important for the biosynthesis of defensive compounds, fatty acids, and hormones.
Cytochrome P450 2E1 is a member of the cytochrome P450 mixed-function oxidase system, which is involved in the metabolism of xenobiotics in the body. This class of enzymes is divided up into a number of subcategories, including CYP1, CYP2, and CYP3, which as a group are largely responsible for the breakdown of foreign compounds in mammals.
Ascorbate peroxidase (or L-ascorbate peroxidase, APX) (EC 1.11.1.11) is an enzyme that catalyzes the chemical reaction
The enzyme horseradish peroxidase (HRP), found in the roots of horseradish, is used extensively in biochemistry applications. It is a metalloenzyme with many isoforms, of which the most studied type is C. It catalyzes the oxidation of various organic substrates by hydrogen peroxide.
In enzymology, a camphor 5-monooxygenase (EC 1.14.15.1) is an enzyme that catalyzes the chemical reaction
In enzymology, a trans-cinnamate 4-monooxygenase (EC 1.14.14.91) 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
Animal heme-dependent peroxidases is a family of peroxidases. Peroxidases are found in bacteria, fungi, plants and animals. On the basis of sequence similarity, a number of animal heme peroxidases can be categorized as members of a superfamily: myeloperoxidase (MPO); eosinophil peroxidase (EPO); lactoperoxidase (LPO); thyroid peroxidase (TPO); prostaglandin H synthase (PGHS); and peroxidasin.
Haloperoxidases are peroxidases that are able to mediate the oxidation of halides by hydrogen peroxide. Both halides and hydrogen peroxide are widely available in the environment.
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:
Bromide peroxidase (EC 1.11.1.18, bromoperoxidase, haloperoxidase (ambiguous), eosinophil peroxidase) is a family of enzymes with systematic name bromide:hydrogen-peroxide oxidoreductase. These enzymes catalyse the following chemical reaction:
Unspecific peroxygenase (EC 1.11.2.1, aromatic peroxygenase, mushroom peroxygenase, haloperoxidase-peroxygenase, Agrocybe aegerita peroxidase) is an enzyme with systematic name substrate:hydrogen peroxide oxidoreductase (RH-hydroxylating or -epoxidising). This enzyme catalyses the following chemical reaction
Fatty-acid peroxygenase is an enzyme with systematic name fatty acid:hydroperoxide oxidoreductase (RH-hydroxylating). 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.
References
- ↑ Hofrichter, M.; Ullrich, R.; Pecyna, Marek J.; Liers, Christiane; Lundell, Taina (2010). "New and classic families of secreted fungal heme peroxidases". Appl Microbiol Biotechnol. 87 (3): 871–897. doi:10.1007/s00253-010-2633-0. PMID 20495915. S2CID 24417282.
- ↑ Butler, Alison; Carter-Franklin, Jayme N. (2004). "The role of vanadium bromoperoxidase in the biosynthesis of halogenated marine natural products". Natural Product Reports. 21 (1): 180–8. doi:10.1039/b302337k. PMID 15039842. (this paper also discussed chloroperoxidases.
- ↑ Poulos TL, Sundaramoorthy M, Terner J (1995). "The crystal structure of chloroperoxidase: a heme peroxidase--cytochrome P450 functional hybrid". Structure. 3 (12): 1367–1377. doi: 10.1016/S0969-2126(01)00274-X . PMID 8747463.
