An in-silico characterization of the structure, function and hosting of the antioxidative enzymes of the bacterial microorganisms

Reactive oxygen species, which lead to oxidative stress and related diseases via both intra- and extracellular pathways, could be identified and cleaning through some of the bacterial enzymes. Bearing in mind, the assessment of the structure, function and hosting of the antioxidative enzymes while lead to disclose species of bacteria with probiotics capability, provides approaches to designing genetics constructs. In this regard, the nucleotide and protein sequences of the katA, katE, katE*, sodA, sodA*, gshR, gshR1, gshR4, trxB1 and trxR genes were retrieved from databases. Then the structural, functional,topological and physicochemical properties of the protein sequences of related enzymes were investigated. Moreover, their hosting in bacterial microorganisms were explored. The results of this study whilst disclosed the physicochemical properties of these enzymes reveal that KATE, KATA, KATE* and SODA are secretory capacity. Structural monitoring of these enzymes introduced collaborative and pragmatic domains with the ability to remove reactive oxygen species, hydrogen peroxide decomposition and regulation of redox reactions as well as immunomodulatory effects and ammonia removal in some of them.In this regard, examination the binding affinity of these enzymes to oxidant agents revealed high binding affinity of them, in particular KATA, to O2-. Additionally, checking the host of these enzymes revealed the presence of homologous sequences especially sequences like to TRXB1 and TRXR in different species of Weissella, Pediococcus, Leuconostoc, Tetragenococcus, Peptoniphilus and Listeria. Meanwhile, similarity search lead to detection seven encoding sequences with antioxidative capacity in the genomic context of the Pediococcus acidilactici, Lactobacillus pentosus and Lactobacillus plantarum.