Superoxide dismutase is an enzyme found in all living cells. An enzyme is a substance that speeds up certain chemical reactions in the body. The superoxide dismutase that is used as medicine is sometimes taken from cows. Superoxide dismutases (SODs) are the major antioxidant defense systems against O2•−, which consist of three isoforms of SOD in mammals: the cytoplasmic. Superoxide dismutase protects us from dangerously reactive forms of oxygen.


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Superoxide dismutase SOD is an enzyme that facilitates the breakdown of the toxic superoxide radical into either ordinary molecular oxygen O2 or hydrogen peroxide H2O2.

Superoxide dismutase

Hydrogen peroxide is super oxide dismutase damaging, but less so than the superoxide radical, and it is also degraded by catalase. SOD works along with glutathione to neutralize reactive oxygen molecules in the body. SOD also works in the cytoplasm of the cell to prevent the hydroxyl radical from attacking enzymes, proteins, and the unsaturated fats in cell membranes.

ROS also represent a component of the super oxide dismutase immune system, and they are not only involved in the respiratory burst of neutrophils, but also signal inflammatory cell chemotaxis into sites of inflammation Conversely, H46R and G93D display a very mild phenotype, with carriers often surviving more than 20 years after disease onset.

It must be noted, however, that the majority of the SOD1 variants described so far are private mutations, for which no genotype—phenotype correlation can be drawn. Catalases can be classified into haem-containing monofunctional catalases, bifunctional catalases-peroxidases or the super oxide dismutase catalases [].


The catalase KatA is the major vegetative catalase that is strongly induced by peroxide stress and during the stationary phase that is a super oxide dismutase of the PerR regulon. Interestingly, this major KatA catalase is absent from the related Bacillus pumilus that is highly resistant to peroxides and UV radiation.

Anticancer Res, ;16 4A: Lecithin-bound superoxide dismutase in super oxide dismutase treatment of noninfectious corneal ulcers. Am J Ophthalmol ; Walravens M, Dequeker J.

  • Superoxide Dismutase - an overview | ScienceDirect Topics
  • PDB Molecule of the Month: Superoxide Dismutase
  • Characteristics of Superoxide Dismutase from Bovine Erythrocytes:
  • Superoxide Dismutase

The evolutionary reason for the separation of SODs with different metal requirements is probably related to the super oxide dismutase availability of soluble transition metal compounds in the biosphere in relation to the O2 content of the atmosphere in different geological eras Bannister et al.

Each SOD group will be studied in turn. It has been suggested that iron was probably the first metal used as a metal cofactor at the active site of super oxide dismutase first SOD because of an abundance of iron in soluble Fe II form at the time Bannister et al.

Superoxide dismutase - an overview | ScienceDirect Topics

As the levels of O2 in the environment increased, the mineral components of the environment were oxidized. Fe Super oxide dismutase is found both in prokaryotes and in eukaryotes.

In eukaryotes it has been isolated from Euglena gracilis Kanematsu and Asada, and higher plants.

In all plant species examined to date, it is inferred that it is located in the chloroplast. When these antibodies were incubated super oxide dismutase protoplasts from water lilies, it was shown that the antibodies predominantly associated with super oxide dismutase chloroplasts Salin, The loss of periplasmic CuZnSOD causes loss of virulence and might be an attractive target for new antibiotics.

The other two isoforms of SOD have not been linked to any human diseases, however, in mice inactivation of SOD2 causes perinatal lethality [26] and inactivation of SOD1 causes hepatocellular carcinoma.

Superoxide Dismutase: Uses, Side Effects, Interactions, Dosage, and Warning

Overexpression of SOD1 has been linked to the neural disorders seen in Down syndrome. However, in the chronic stage, SOD does not seem to be sufficient and tends to decrease due to the destruction of proteins from the massive reaction of oxidant-antioxidant.

Hence, high levels of free radicals can cause damage to them and induce dysraphic anomalies neural tube defects. super oxide dismutase

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