Glutamin-(asparagin-)ase

glutamin-(asparagin-)ase
Identifiers
EC number	3.5.1.38
CAS number	39335-03-0
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search PMC articles PubMed articles NCBI proteins

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

L-glutamine + H₂O $\rightleftharpoons$ 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. PMID 5017769.