Glutamin-(asparagin-)ase

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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 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

  • IUBMB entry for 3.5.1.38
  • BRENDA references for 3.5.1.38 (Recommended.)
  • PubMed references for 3.5.1.38
  • PubMed Central references for 3.5.1.38
  • Google Scholar references for 3.5.1.38
  • Roberts J, Holcenberg JS, Dolowy WC (1972). "Isolation, crystallization, and properties of Achromobacteraceae glutaminase-asparaginase with antitumor activity". J. Biol. Chem. 247: 84&ndash, 90. PMID 5017769.

External links

The CAS registry number for this enzyme class is 39335-03-0.

Gene Ontology (GO) codes


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