EC 3 - Hydrolases
EC 3.5 - Acting on carbon-nitrogen bonds, other than peptide bonds
EC 3.5.1 - In linear amides
EC 3.5.1.38 - Glutamin-(asparagin-)ase
IntEnz view
ENZYME view
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)
L-ASNase/L-GLNase
glutaminase-asparaginase
ansB (gene name)
Systematic name:
L-glutamine(L-asparagine) amidohydrolase
Reactions
- (1) L-glutamine + H2O = L-glutamate + NH3
- (2) L-asparagine + H2O = L-aspartate + NH3
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
Protein domains and families:
PROSITE:PDOC00132
Gene Ontology:
GO:0050417
CAS Registry Number:
39335-03-0
UniProtKB/Swiss-Prot:
ASPQ_ACIGL
ASPQ_DELAC
ASPQ_PSEAE
ASPQ_PSEFA
ASPQ_PSEPK
ASPQ_PSES7
References
-
Isolation, crystallization, and properties of Achromobacteraceae glutaminase-asparaginase with antitumor activity.J. Biol. Chem. 247 : 84-90 (1972). [PMID: 5017769]
-
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]
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Structural characterization of Pseudomonas 7A glutaminase-asparaginase.Biochemistry 33 : 10257-10265 (1994). [PMID: 8068664]
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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]