Biology:Glutamin-(asparagin-)ase

From HandWiki
glutamin-(asparagin-)ase
Identifiers
EC number3.5.1.38
CAS number39335-03-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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

L-glutamine + H2O [math]\displaystyle{ \rightleftharpoons }[/math] 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

  • "Isolation, crystallization, and properties of Achromobacteraceae glutaminase-asparaginase with antitumor activity". J. Biol. Chem. 247 (1): 84–90. 1972. PMID 5017769.