Hamid R Kalhor - Department of Chemistry, Sharif University of Technology, Tehran, Iran
Daniel Yousefi - Department of Chemistry, Sharif University of Technology, Tehran, Iran

Asparaginase is an enzyme that hydrolyzes the amide bond in L-asparagine and similar amides and possesses expandable anti-cancer properties. In this study, the E. coli L-asparaginase II gene was cloned and the recombinant protein was expressed and its enzymatic activity was measured. To find a mutant with altered substrate specificity, two active site residues were chosen as the starting point for mutagenesis and the effect of the mutation on the enzyme s structure was studied by computational methods

L-asparaginase II, molecular cloning, substrate specificity, protein engineering, molecular modeling