User:Melissa Siolin Martins/Sandbox 1
From Proteopedia
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==Ohr== | ==Ohr== | ||
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | ||
| - | + | The Ohr protein (organic hydroperoxide resistance) is a thiol-dependent Cys-based peroxidase exclusive to bacteria, that participates in the antioxidant defense system of these organisms against damage induced by organic peroxides (OHPs), such as fatty acid peroxides and peroxynitrite <ref>PMID:20463026</ref>;<ref>PMID:35452809</ref>. This class of peroxides is toxic due to its ability to generate free radicals, highly reactive molecules containing an unpaired electron in an atomic orbital that can cause damage to important molecules such as DNA and proteins. Because of that, these substances are frequently used by the host defense against bacteria pathogens (Mongkolsuk, 1998; Lobo et al. 2010). | |
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== Function == | == Function == | ||
Revision as of 11:33, 28 May 2024
Ohr
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References
- ↑ Cussiol JR, Alegria TG, Szweda LI, Netto LE. Ohr (organic hydroperoxide resistance protein) possesses a previously undescribed activity, lipoyl-dependent peroxidase. J Biol Chem. 2010 Jul 16;285(29):21943-50. doi: 10.1074/jbc.M110.117283. Epub, 2010 May 12. PMID:20463026 doi:http://dx.doi.org/10.1074/jbc.M110.117283
- ↑ Meireles DA, da Silva Neto JF, Domingos RM, Alegria TGP, Santos LCM, Netto LES. Ohr catalysis, phylogeny, regulation, and physiological roles. Free Radic Biol Med. 2022 May 20;185:6-24. PMID:35452809 doi:10.1016/j.freeradbiomed.2022.04.001
