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InterPro: IPR000866 Alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen
Protein matches
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UniProtKB Matches: 8100 proteins |
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Accession
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IPR000866 Alkyl_hydroperoxide_Rdtase |
Type
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Domain |
Signatures
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InterPro Relationships
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Parent
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IPR017936 Thioredoxin-like
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Found in
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IPR012335 Thioredoxin fold
IPR013478 Methylamine dehydrogenase accessory protein MauD
IPR017559 Peroxiredoxin
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GO Term annotation
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Function
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GO:0016209 antioxidant activity
GO:0016491 oxidoreductase activity
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InterPro annotation
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Entry Details in BioMart
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Abstract
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Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant enzymes that also control cytokine-induced peroxide levels which mediate signal transduction in mammalian cells. Prxs can be regulated by changes to phosphorylation, redox and possibly oligomerisation states. Prxs are divided into three classes: typical 2-Cys Prxs; atypical 2-Cys Prxs; and 1-Cys Prxs. All Prxs share the same basic catalytic mechanism, in which an active-site cysteine (the peroxidatic cysteine) is oxidised to a sulphenic acid by the peroxide substrate. The recycling of the sulphenic acid back to a thiol is what distinguishes the three enzyme classes. Using crystal structures, a detailed catalytic cycle has been derived for typical 2-Cys Prxs, including a model for the redox-regulated oligomeric state proposed to control enzyme activity [1].
Alkyl hydroperoxide reductase (AhpC) is responsible for directly reducing organic hyperoxides in its reduced dithiol form. Thiol specific antioxidant (TSA) is a physiologically important antioxidant which constitutes an enzymatic defence against sulphur-containing radicals. This family contains AhpC and TSA, as well as related proteins.
Some of the proteins in this family are allergens. Allergies are hypersensitivity reactions of the immune system to specific substances called allergens (such as pollen, stings, drugs, or food) that, in most people, result in no symptoms. A nomenclature system has been established for antigens (allergens) that cause IgE-mediated atopic allergies in humans [WHO/IUIS Allergen Nomenclature Subcommittee, King T.P., Hoffmann D., Loewenstein H., Marsh D.G., Platts-Mills T.A.E., Thomas W. Bull. World Health Organ. 72:797-806(1994)]. This nomenclature system is defined by a designation that is composed of the first three letters of the genus; a space; the first letter of the species name; a space and an arabic number. In the event that two species names have identical designations, they are discriminated from one another by adding one or more letters (as necessary) to each species designation.
The allergens in this family include allergens with the following designations: Asp f 3, Mal f 2 and Mal f 3.
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Structural links
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Database links
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Pfam Clan: CL0172.13
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Additional Reading
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Nakamura T, Yamamoto T, Abe M, Matsumura H, Hagihara Y, Goto T, Yamaguchi T, Inoue T.
Oxidation of archaeal peroxiredoxin involves a hypervalent sulfur intermediate.
Proc. Natl. Acad. Sci. U.S.A. 105 2008 6238-42
[PubMed: 18436649]
http://dx.doi.org/10.1073/pnas.0709822105
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Jonsson TJ, Johnson LC, Lowther WT.
Structure of the sulphiredoxin-peroxiredoxin complex reveals an essential repair embrace.
Nature 451 2008 98-101
[PubMed: 18172504]
http://dx.doi.org/10.1038/nature06415
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Vedadi M, Lew J, Artz J, Amani M, Zhao Y, Dong A, Wasney GA, Gao M, Hills T, Brokx S, Qiu W, Sharma S, Diassiti A, Alam Z, Melone M, Mulichak A, Wernimont A, Bray J, Loppnau P, Plotnikova O, Newberry K, Sundararajan E, Houston S, Walker J, Tempel W, Bochkarev A, Kozieradzki I, Edwards A, Arrowsmith C, Roos D, Kain K, Hui R.
Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms.
Mol. Biochem. Parasitol. 151 2007 100-10
[PubMed: 17125854]
http://dx.doi.org/10.1016/j.molbiopara.2006.10.011
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Nakamura T, Yamamoto T, Inoue T, Matsumura H, Kobayashi A, Hagihara Y, Uegaki K, Ataka M, Kai Y, Ishikawa K.
Crystal structure of thioredoxin peroxidase from aerobic hyperthermophilic archaeon Aeropyrum pernix K1.
Proteins 62 2006 822-6
[PubMed: 16342268]
http://dx.doi.org/10.1002/prot.20796
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Chae HZ, Robison K, Poole LB, Church G, Storz G, Rhee SG.
Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes.
Proc. Natl. Acad. Sci. U.S.A. 91 1994 7017-21
[PubMed: 8041738]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=8041738
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Boucher IW, McMillan PJ, Gabrielsen M, Akerman SE, Brannigan JA, Schnick C, Brzozowski AM, Wilkinson AJ, Muller S.
Structural and biochemical characterization of a mitochondrial peroxiredoxin from Plasmodium falciparum.
Mol. Microbiol. 61 2006 948-59
[PubMed: 16879648]
http://dx.doi.org/10.1111/j.1365-2958.2006.05303.x
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InterPro 23.1
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