Superoxide dismutase (SOD) (SOD)

Superoxide dismutase (SOD) is a critical family of metalloenzymes that serve as the primary antioxidant defense against superoxide radicals in nearly all living cells exposed to oxygen. These enzymes catalyze the dismutation of the superoxide anion (O2−) into molecular oxygen (O2) and hydrogen peroxide (H2O2), which is subsequently neutralized by other enzymes like catalase (StatPearls, PMID: 32491810). In humans, three distinct isoforms exist: SOD1 (cytoplasmic), SOD2 (mitochondrial), and SOD3 (extracellular), each maintaining redox homeostasis in specific cellular compartments (UniProt P00441, P04179, P08294). Mutations in the SOD1 gene are a well-established cause of familial Amyotrophic Lateral Sclerosis (ALS), where the protein gains toxic properties that lead to motor neuron death (PubMed, PMID: 24991777). Therapeutic strategies targeting SOD include the use of SOD mimetics like avasopasem manganese to protect healthy tissue during radiation therapy and antisense oligonucleotides like tofersen, which reduces the production of mutant SOD1 in ALS patients (FDA, 2023). Beyond neurodegeneration, SOD is a target of interest in cardiovascular diseases and inflammatory conditions where oxidative stress plays a central role in pathogenesis.

Other names

Superoxide:superoxide oxidoreductaseCu/Zn-SODMn-SODEC-SODSOD1SOD2SOD3Indelible oxidaseSoluble superoxide dismutase

Catalyzes the dismutation of the superoxide radical (O2−) into molecular oxygen (O2) and hydrogen peroxide (H2O2) through alternate reduction and oxidation of the metal ion at the active site.