Abstract
Abstract Aspartic-β-semialdehyde has been found to be a potent, rapid, and reversible inhibitor of Escherichia coli l-asparaginase. A Ki value of 3.6 x 10-6 m has been estimated for the l-enantiomer of the aldehyde in sodium borate-phosphate buffer (0.05 m, pH 8.6) at 37°. dl-Aspartic β-semialdehyde dimethyl acetal and dl-homoserine were found to be ineffective inhibitors, with Ki values exceeding 10-3 m. The aldehyde was shown not to exist as a cyclic acylal to an extent greater than one part in 106. Inhibition appears to be consistent with a double displacement mechanism for the hydrolytic action of this enzyme, and not with mechanisms involving either direct water attack or a cyclic anhydride intermediate.
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