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Pathway Description
Degradation of Superoxides
Rattus norvegicus
Category:
Metabolite Pathway
Sub-Category:
Metabolic
Created: 2018-08-10
Last Updated: 2019-08-30
Reactive oxygen species (ROS) are formed by the normal metabolic process of oxygen. Examples are superoxide, oxygen ions and peroxides and can be of either organic or inorganic origin. ROS are highly reactive due to unpaired valence shell electrons, and can cause serious damage to cells and cell organelles. The environment also may cause ROS to form, from sources such as drought, air pollutants, UV light, cold temperatures, and external chemicals. An organic example of ROS being formed is during the beta oxidation of fatty acids, or photorespiration in photosynthetic organisms. Aerobic organisms who produce energy through the electron transport chain in mitochondria produce ROS as a byproduct. ROS damage commmonly includes DNA damage, lipid peroxidation, oxidation of amino acids in proteins, and oxidatively inactivating enzymes by oxidation of cofactors. Most aerobic organisms have adapted to this dangerous condition of life, and have a system of enzymes and scavenging free radicals. Enzymes such as are essential for defense against ROS, and include superoxide dismutases (SODs) and hydroperoxidase (CAT). Superoxide dismutases are the primary method of disposal of ROS, and convert superoxide radicals to hydrogen peroxide and water. Catalase attacks the hydrogen peroxide produced by SODs, and converts it into oxygen and water. In skin cells, 5,6 dihydroxyindole-2-carboxylic acid oxidase in the melanosome membranes breaks down hydrogen peroxide into water and oxygen.
References
Degradation of Superoxides References
Perry AC, Jones R, Hall L: Isolation and characterization of a rat cDNA clone encoding a secreted superoxide dismutase reveals the epididymis to be a major site of its expression. Biochem J. 1993 Jul 1;293 ( Pt 1):21-5. doi: 10.1042/bj2930021.
Pubmed: 8328962
Willems J, Zwijsen A, Slegers H, Nicolai S, Bettadapura J, Raymackers J, Scarcez T: Purification and sequence of rat extracellular superoxide dismutase B secreted by C6 glioma. J Biol Chem. 1993 Nov 25;268(33):24614-21.
Pubmed: 8227019
Carlsson LM, Marklund SL, Edlund T: The rat extracellular superoxide dismutase dimer is converted to a tetramer by the exchange of a single amino acid. Proc Natl Acad Sci U S A. 1996 May 28;93(11):5219-22. doi: 10.1073/pnas.93.11.5219.
Pubmed: 8643556
Ho YS, Crapo JD: cDNA and deduced amino acid sequence of rat copper-zinc-containing superoxide dismutase. Nucleic Acids Res. 1987 Aug 25;15(16):6746. doi: 10.1093/nar/15.16.6746.
Pubmed: 3628012
Hass MA, Iqbal J, Clerch LB, Frank L, Massaro D: Rat lung Cu,Zn superoxide dismutase. Isolation and sequence of a full-length cDNA and studies of enzyme induction. J Clin Invest. 1989 Apr;83(4):1241-6. doi: 10.1172/JCI114007.
Pubmed: 2703531
Hsu JL, Visner GA, Burr IA, Nick HS: Rat copper/zinc superoxide dismutase gene: isolation, characterization, and species comparison. Biochem Biophys Res Commun. 1992 Jul 31;186(2):936-43. doi: 10.1016/0006-291x(92)90836-a.
Pubmed: 1379810
Ho YS, Crapo JD: Nucleotide sequences of cDNAs coding for rat manganese-containing superoxide dismutase. Nucleic Acids Res. 1987 Dec 10;15(23):10070. doi: 10.1093/nar/15.23.10070.
Pubmed: 3697077
Ho YS, Howard AJ, Crapo JD: Molecular structure of a functional rat gene for manganese-containing superoxide dismutase. Am J Respir Cell Mol Biol. 1991 Mar;4(3):278-86. doi: 10.1165/ajrcmb/4.3.278.
Pubmed: 2001291
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Pubmed: 15489334
Furuta S, Hayashi H, Hijikata M, Miyazawa S, Osumi T, Hashimoto T: Complete nucleotide sequence of cDNA and deduced amino acid sequence of rat liver catalase. Proc Natl Acad Sci U S A. 1986 Jan;83(2):313-7. doi: 10.1073/pnas.83.2.313.
Pubmed: 3455767
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Pubmed: 2792765
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Pubmed: 15057822
This pathway was propagated using PathWhiz -
Pon, A. et al. Pathways with PathWhiz (2015) Nucleic Acids Res. 43(Web Server issue): W552–W559.
Propagated from SMP0000468
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