EC 3.5.1.38 - Glutamin-(asparagin-)ase

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IntEnz Enzyme Nomenclature
EC 3.5.1.38

Names

Accepted name:
glutamin-(asparagin-)ase
Other names:
L-asparagine/L-glutamine amidohydrolase
L-ASNase/L-GLNase
glutaminase-asparaginase
ansB (gene name)
Systematic name:
L-glutamine(L-asparagine) amidohydrolase

Reactions

Comments:

L-Asparagine is hydrolysed at 0.8 of the rate of L-glutamine; the D-isomers are also hydrolysed, but more slowly. cf. EC 3.5.1.2, glutaminase and EC 3.5.1.1, asparaginase.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00132
Structural data: CSA , EC2PDB
Gene Ontology: GO:0050417
CAS Registry Number: 39335-03-0
UniProtKB/Swiss-Prot:

References

  1. Roberts, J., Holcenberg, J.S. and Dolowy, W.C.
    Isolation, crystallization, and properties of Achromobacteraceae glutaminase-asparaginase with antitumor activity.
    J. Biol. Chem. 247: 84-90 (1972). [PMID: 5017769]
  2. Tanaka, S., Robinson, E. A., Appella, E., Miller, M., Ammon, H. L., Roberts, J., Weber, I. T., Wlodawer, A.
    Structures of amidohydrolases. Amino acid sequence of a glutaminase-asparaginase from Acinetobacter glutaminasificans and preliminary crystallographic data for an asparaginase from Erwinia chrysanthemi.
    J. Biol. Chem. 263: 8583-8591 (1988). [PMID: 3379033]
  3. Lubkowski, J., Wlodawer, A., Ammon, H. L., Copeland, T. D., Swain, A. L.
    Structural characterization of Pseudomonas 7A glutaminase-asparaginase.
    Biochemistry 33: 10257-10265 (1994). [PMID: 8068664]
  4. Ortlund, E., Lacount, M. W., Lewinski, K., Lebioda, L.
    Reactions of Pseudomonas 7A glutaminase-asparaginase with diazo analogues of glutamine and asparagine result in unexpected covalent inhibitions and suggests an unusual catalytic triad Thr-Tyr-Glu.
    Biochemistry 39: 1199-1204 (2000). [PMID: 10684596]

[EC 3.5.1.38 created 1976]