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Background & Aim: The present study was carried out to evaluate the omics of asnA gene fromEnterobactor aerogenes strain KCTC2190. Methods: This was achieved by using various onlinecomputational tools for both genomic and proteomic analysis. Results: Genomic studies states that thepyramidine rich gene codes for 388 aminoacid peptide with approximately 37KD (ss DNA) containingboth left & right primers, a hybridization probe and several restriction sites for restriction enzymes. Thecorresponding peptide primary structure reveals that it is an acidic, stable protein. Secondary structuredefines that it mainly contains the random coils & alpha helix. The protein has a total of tenphosphorylation sites along with net N & O-Glycosylation sites. Conclusion: The present study statesthat the pyramidine rich gene has both left & right primers, Hybridization probe with sufficient GCcontent. The encoded acidic, stable peptide ahs the multiple sites for phosphorylation, glycosylation.Above results shows that the asnA from Enterobactor aerogenes strain KCTC2190 is much suitable forthe experiments to enhance the L-Asparginase enzyme.

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