L-Asparaginase from Escherichia coli

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Abstract
Crystalline L-asparaginase from Escherichia coli A-1-3 hydrolyzed D-asparagine, L- and D-glutamine but at much slower rates than the rate at which it hydrolyzed L-asparagine. Inhibitions by these substrates and related compounds were revealed to be competitive. D-Asparagine showed the same affinity for the enzyme both in its hydrolysis and in-hibition of L-asparagine hydrolysis. L-Aspartate, D-aspartate and α-N-ethylasparagine in-hibited various hydrolysis reactions with the respective inhibitor constants. The enzyme was found to hydrolyze β-methylaspartate as well as β-aspartohydroxamate. These data strongly suggest that the hydrolysis occurred at the same active site of the enzyme molecule with relatively low specificity for the configuration of the substrate molecule and the kind of bonding which it hydrolyzes

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