Superoxide dismutase 2 (mitochondrial) (SOD2) (SOD2)

Superoxide dismutase 2 (SOD2), commonly referred to as manganese superoxide dismutase (MnSOD), is a vital antioxidant enzyme located in the mitochondrial matrix of eukaryotic cells (UniProt P04179). Its primary biological function is to catalyze the conversion of superoxide radicals—highly reactive byproducts of oxidative phosphorylation—into less harmful hydrogen peroxide and molecular oxygen (PubMed: 21671300). By maintaining low levels of mitochondrial superoxide, SOD2 prevents the formation of toxic peroxynitrite and protects mitochondrial DNA and proteins from oxidative damage (NCBI Gene: 6648). In clinical settings, SOD2 is a significant therapeutic target for conditions involving oxidative stress, such as radiation-induced oral mucositis and ischemia-reperfusion injury (ClinicalTrials.gov: NCT03689712). Pharmacological interventions often utilize SOD mimetics, like avasopasem manganese, which replicate the enzyme's catalytic cycle to reduce tissue damage (PubMed: 31557470). Furthermore, alterations in SOD2 expression or genetic polymorphisms, such as the Val16Ala variant, are associated with increased risks of cancer, neurodegenerative diseases, and cardiovascular disorders (PubMed: 21111018). These drugs aim to mimic the natural catalytic function of SOD2 to mitigate tissue injury and inflammation while avoiding excessive accumulation of hydrogen peroxide (PubMed: 19439452).

Other names

MnSODManganese superoxide dismutaseManganese-dependent superoxide dismutaseIPO-BMNSODSuperoxide dismutase [Mn], mitochondrial

Superoxide dismutase mimetic activity; catalysis of superoxide dismutation into hydrogen peroxide and molecular oxygen.