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In enzymology, a glutamin-(asparagin-)ase (EC 3.5.1.38) is an enzyme that catalyzes the chemical reaction

L-glutamine + H₂O ${\displaystyle \rightleftharpoons }$ L-glutamate + NH₃

Thus, the two substrates of this enzyme are L-glutamine and H₂O, whereas its two products are L-glutamate and NH₃.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is L-glutamine(L-asparagine) amidohydrolase. This enzyme participates in 4 metabolic pathways: glutamate metabolism, alanine and aspartate metabolism, d-glutamine and d-glutamate metabolism, and nitrogen metabolism.

Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1DJO, 1DJP, and 4PGA.

References

• Roberts J, Holcenberg JS, Dolowy WC (1972). "Isolation, crystallization, and properties of Achromobacteraceae glutaminase-asparaginase with antitumor activity". J. Biol. Chem. 247 (1): 84–90. doi:10.1016/S0021-9258(19)45762-1. PMID 5017769.

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