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The mechanism of catalysis by the  l -glutaminase-asparaginase from  Pseudomonas 7A  (PGA) was investigated using structural, mass spectrometry, and kinetic data. We had previously proposed mechanism of hydrolysis of  l -Asn by the type II  l -asparaginase from  E. coli  (EcAII), but that work was limited to just one enzyme. Based on results presented in this report, we postulate that all homotetrameric  l -asparaginases from mesophilic bacteria utilize a common ping-pong mechanism of catalysis consisting of two subsequent nucleophilic substitutions. Several new structures of non-covalent complexes of PGA with different substrates, as well as structures of covalent acyl-enzyme intermediates of PGA with canonical substrates ( l -Asp and  l -Glu) and an opportunistic ligand, a citrate anion, were determined. The results of kinetic experiments monitored by high-resolution LC/MS, when combined with new structural data, clearly show that the reaction catalyzed by  l -glutaminase-asparaginases proceeds through formation of a covalent intermediate, as observed previously for EcAII. Additionally, by showing that the same mechanism applies to  l -Asn and  l -Gln, we postulate that it is common for all these structurally related enzymes.

Generalized enzymatic mechanism of catalysis by tetrameric l-asparaginases from mesophilic bacteria