Superoxide Dismutase (SOD), also known as orgotein, is a bio-derived active substance that eliminates harmful substances produced during metabolic processes in organisms. With free-radical-scavenging activity, SOD exerts anti-aging, immunomodulatory, lipid-regulating, blood-glucose-regulating, anti-radiation and skin-beautifying effects.
Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Catalyzes the oxidation of hydrogen sulfide (H2S) to sulfate, playing an important role in detoxifying H2S and limiting the accumulation of reactive sulfur species (RSS) such as persulfides and polysulfides. Miscellaneous: The protein (both wild-type and ALS1 variants) has a tendency to form fibrillar aggregates in the absence of the intramolecular disulfide bond or of bound zinc ions. These aggregates may have cytotoxic effects. Zinc binding promotes dimerization and stabilizes the native form. Catalytic activity: superoxide + 2 H+ = H2O2 + O2.
Post-translational: Unlike wild-type protein, the pathogenic variants ALS1 Arg-38, Arg-47, Arg-86 and Ala-94 are polyubiquitinated by RNF19A leading to their proteasomal degradation. The pathogenic variants ALS1 Arg-86 and Ala-94 are ubiquitinated by MARCH5 leading to their proteasomal degradation. The ditryptophan cross-link at Trp-33 is responsible for the non-disulfide-linked homodimerization. Such modification might only occur in extreme conditions and additional experimental evidence is required. Palmitoylation helps nuclear targeting and decreases catalytic activity. Succinylation, adjacent to copper catalytic site, probably inhibits activity. Desuccinylation by SIRT5 enhances activity.
ZJ26F0838225
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