Three residues His29, His84 and His171 were found to be the ligands of metal ions of one hyperthermostable Mn-SOD produced by Thermus thermophilus HB27 after multiple sequence alignment.
Moreover, the SODs produce potentially toxic O2 as a product, while the SORs do not.
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One unit of SOD activity was defined as the amount of SOD that produces 50% inhibition of cytochrome c reduction.
On the other hand, when SOD levels were found higher in periodontitis patients, it can be explained as that more SOD were produced to afford biological protection against increased superoxide generation during periodontal inflammation.
In this case, most SOD is produced as the native Mn-containing form, which is an essential virulence factor, accompanied by a small amount of the apoprotein.
The most abundant ROS generated in living systems is the superoxide radical, which is acted upon by SOD to produce hydrogen peroxide, which in turn is broken down by catalase and/or GSH-Px into water and oxygen.
The three major antioxidant enzymes are the superoxide dismutase (SOD) which produces H2O2 by converting O2−, then, the enzyme catalase (CAT) that splits H2O2 to oxygen and water, and the third antioxidant enzyme, that is, glutathione peroxides (GPx), that converts H2O2 and organic peroxides.
These problems may be overcome either by the design of SOD-mimetic drugs or by genetically re-engineering the human SOD genes to produce SODs with more desirable and controllable properties for human clinical usage.
A human Cu, Zn-SOD cDNA fragment was isolated using the PCR technique from the λZap human placenta cDNA library [ 14] and a monoclonal antibody against human Cu, Zn-SOD was produced in our laboratory.
