Key Amino Acids in Understanding Evolutionary Charac- terization of Mn/Fe-Superoxide Dismutase: A Phylogenetic and Structural Analysis of Proteins from Corynebacterium and Hosts

Superoxide dismutases (SODs) are enzymes widely observed in nature and commonly studied to understand the protection of reactive oxygen species (ROS). This work aims to understand the conservation of and correlation among the enzymes from pathogens and hosts, using coevolution analysis of amino acids in Mn/ Fe-Superoxide Dismutase. Five amino acid sets were found. Some information about the functions of these amino acids was collected from the literature, which may help to better understand what the correlation of these amino acids may imply for the protein. Two pockets on the protein structure near the active site were identified, which contain some residues observed in the sets of correlated residues. The phylogenetic analysis contributed to the understanding of evolutionary differences and similarities between both organisms. It was possible to observe patterns of specific amino acids for each kind of organism and, by contrast, some amino acids that were conserved for all organisms, which are hypothesized to impact crucial functions such as folding and other specific functions.