SODA E.Coli (Superoxide Dismutase [Mn]) is a 25.2 kDa enzyme composed of 226 amino acids, including a 20-amino-acid His-tag at the N-terminus for purification . It is expressed in E. coli and functions as an antioxidant by catalyzing the conversion of superoxide radicals () into hydrogen peroxide () and oxygen (), which are further metabolized by other enzymes .
Specific Activity: >350 units/mg, measured by inhibition of cytochrome c reduction in a xanthine/xanthine oxidase system .
SODA E.Coli is essential for mitigating oxidative stress caused by aerobic metabolism and host immune responses. Its roles include:
Antioxidant Defense: Neutralizes superoxide radicals generated during respiration .
Stress Adaptation: Induced under oxidative stress conditions, such as exposure to paraquat or hydrogen peroxide .
Studies on avian pathogenic E. coli (APEC) highlight SodA’s contribution to virulence:
Key Findings:
Feature | SodA (MnSOD) | SodB (FeSOD) |
---|---|---|
Metal Cofactor | Manganese | Iron |
Expression | Inducible under stress | Constitutive |
Primary Role | Stress response | Baseline detoxification |
Rescue Function | Compensates for SodB | Not applicable |
In E. coli, SodA acts as a backup system under oxidative stress, whereas SodB maintains baseline superoxide detoxification .
There are three main types of superoxide dismutase based on their metal co-factors:
Recombinant superoxide dismutase is produced using genetic engineering techniques where the SOD gene is inserted into a host organism, such as Escherichia coli (E. coli), to produce the enzyme in large quantities. This method ensures a consistent and high-purity product suitable for research and therapeutic applications.
E. coli is a preferred host for recombinant protein production due to its rapid growth, well-understood genetics, and ability to express high levels of protein. The process involves:
Recombinant SOD has several applications, including: