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Information on EC 3.5.1.38 - glutamin-(asparagin-)ase
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3.5.1.38 glutamin-(asparagin-)aseIUBMB Comments
The enzyme from the bacterium Achromobacter hydrolyses L-asparagine 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.
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Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
glutaminase-asparaginase, asparaginase a, periplasmic glutaminase/asparaginase, glutaminase/asparaginase, glutamin-(asparagin-)ase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glutaminase-asparaginase
-
-
-
-
glutaminase/asparaginase
periplasmic glutaminase/asparaginase
PGA
PGA
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-glutamine + H2O = L-glutamate + NH3
L-asparagine is hydrolysed at 0.8 of the rate of L-glutamine, the D-isomers are also hydrolysed, but more slowly
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylic acid amide hydrolysis
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-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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Alanine, aspartate and glutamate metabolism, glutamate and glutamine metabolism, glutamate and glutamine metabolism, glutamate and glutamine metabolism, glutamate and glutamine metabolism, glutamate and glutamine metabolism, glutamate and glutamine metabolism, glutamate and glutamine metabolism, glutamate and glutamine metabolism
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SYSTEMATIC NAME
IUBMB Comments
L-glutamine(L-asparagine) amidohydrolase
The enzyme from the bacterium Achromobacter hydrolyses L-asparagine 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.
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CAS REGISTRY NUMBER
COMMENTARY
39335-03-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-carbamoyl-L-asparagine + H2O
N-carbamoyl-L-aspartate + NH3
-
-
-
?
N-glycyl-L-asparagine + H2O
N-glycyl-L-aspartate + NH3
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60% higher activity than on L-asparagine
-
?
beta-D-aspartyl hydroxylammonium sulfate + H2O
L-Asp + hydroxylammonium sulfate
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only asparaginase A, low activity
-
?
beta-D-aspartyl hydroxylammonium sulfate + H2O
L-Asp + hydroxylammonium sulfate
-
-
-
?
beta-L-aspartyl hydroxylammonium sulfate + H2O
L-Asp + hydroxylammonium sulfate
-
higher activity for asparaginase B
-
?
beta-L-aspartyl hydroxylammonium sulfate + H2O
L-Asp + hydroxylammonium sulfate
-
-
-
?
beta-L-aspartyl hydroxylammonium sulfate + H2O
L-Asp + hydroxylammonium sulfate
-
-
-
?
beta-L-aspartyl hydroxylammonium sulfate + H2O
L-Asp + hydroxylammonium sulfate
-
-
-
?
D-asparagine + H2O
D-aspartate + NH3
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one third of the L-isomer
-
?
gamma-L-glutamyl hydroxylammonium sulfate + H2O
L-glutamate + hydroxylammonium sulfate
-
-
-
?
gamma-L-glutamyl hydroxylammonium sulfate + H2O
L-glutamate + hydroxylammonium sulfate
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very low activities for both asparaginases A and B
-
?
gamma-L-glutamyl hydroxylammonium sulfate + H2O
L-glutamate + hydroxylammonium sulfate
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-
-
?
gamma-L-glutamyl hydroxylammonium sulfate + H2O
L-glutamate + hydroxylammonium sulfate
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same rate as for L-glutamine
-
?
gamma-L-glutamyl hydroxylammonium sulfate + H2O
L-glutamate + hydroxylammonium sulfate
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
involved in the maintenance of the correct L-asparagine/L-aspartate ratio
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
ratio of glutaminase to aspariginase activity is 0.7 to 1
-
-
?
L-asparagine + H2O
L-aspartate + NH3
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involved in the maintenance of the correct L-asparagine/L-aspartate ratio
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
hydrolysed at a rate of 0.83 compared to L-glutamine
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?
L-asparagine + H2O
L-aspartate + NH3
-
involved in the maintenance of the correct L-asparagine/L-aspartate ratio
-
-
?
L-asparagine + H2O
L-aspartate + NH3
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ratio of glutaminase to aspariginase activity is 1.4 to 1
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
involved in the maintenance of the correct L-asparagine/L-aspartate ratio
-
-
?
L-asparagine + H2O
L-aspartate + NH3
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ratio of glutaminase to aspariginase activity is 0.8 to 1
-
-
?
L-asparagine + H2O
L-aspartate + NH3
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hydrolysed at a rate of 0.73 compared to L-glutamine
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?
L-asparagine + H2O
L-aspartate + NH3
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hydrolysis at a rate of 0.73 compared to L-glutamine
-
?
L-asparagine + H2O
L-aspartate + NH3
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hydrolysed at a rate of 0.73 compared to L-glutamine
-
?
L-asparagine + H2O
L-aspartate + NH3
-
hydrolysis at a rate of 0.73 compared to L-glutamine
-
?
L-asparagine + H2O
L-aspartate + NH3
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not active on D-asparagine
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?
L-glutamine + H2O
L-glutamate + NH3
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higher activity for glutaminase than for asparaginase
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?
L-glutamine + H2O
L-glutamate + NH3
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involved in the maintenance of the correct L-glutamine/L-glutamate ratio
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-
?
L-glutamine + H2O
L-glutamate + NH3
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ratio of glutaminase to aspariginase activity is 0.7 to 1
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-
?
L-glutamine + H2O
L-glutamate + NH3
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involved in the maintenance of the correct L-glutamine/L-glutamate ratio
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-
?
L-glutamine + H2O
L-glutamate + NH3
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ratio of glutaminase to aspariginase activity is 0.7 to 1
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-
?
L-glutamine + H2O
L-glutamate + NH3
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involved in the maintenance of the correct L-glutamine/L-glutamate ratio
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-
?
L-glutamine + H2O
L-glutamate + NH3
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ratio of glutaminase to aspariginase activity is 1.4 to 1
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-
?
L-glutamine + H2O
L-glutamate + NH3
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involved in the maintenance of the correct L-glutamine/L-glutamate ratio
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-
?
L-glutamine + H2O
L-glutamate + NH3
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ratio of glutaminase to aspariginase activity is 0.8 to 1
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-
?
L-glutamine + H2O
L-glutamate + NH3
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-
-
?
L-glutamine + H2O
L-glutamate + NH3
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-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
higher activity for glutaminase than for asparaginase
-
?
L-glutamine + H2O
L-glutamate + NH3
-
higher activity for glutaminase than for asparaginase
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?
L-glutamine + H2O
L-glutamate + NH3
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higher activity for glutaminase than for asparaginase
-
?
L-glutamine + H2O
L-glutamate + NH3
-
higher activity for glutaminase than for asparaginase
-
?
L-glutamine + H2O
L-glutamate + NH3
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one fifth of the activity on L-asparagine
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?
L-glutamine + H2O
L-glutamate + NH3
Tilachlidium humicola
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lower activity than for L-asparagine
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?
N-acetyl-L-asparagine + H2O
N-acetyl-L-aspartate + NH3
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5% of the activity compared to L-asparagine
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?
additional information
?
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acetamide, nicotinamide, and NAD are not hydrolyzed
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?
additional information
?
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acetamide, nicotinamide, and NAD are not hydrolyzed
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?
additional information
?
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acetamide, nicotinamide, and NAD are not hydrolyzed
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?
additional information
?
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acetamide, nicotinamide, and NAD are not hydrolyzed
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?
additional information
?
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glutaminase/asparaginase is downregulated during growth of the aauR mutant on Glu
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-
?
additional information
?
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glutaminase/asparaginase is downregulated during growth of the aauR mutant on Glu
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-asparagine + H2O
L-aspartate + NH3
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involved in the maintenance of the correct L-asparagine/L-aspartate ratio
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-
?
L-asparagine + H2O
L-aspartate + NH3
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involved in the maintenance of the correct L-asparagine/L-aspartate ratio
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-
?
L-asparagine + H2O
L-aspartate + NH3
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hydrolysed at a rate of 0.83 compared to L-glutamine
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?
L-asparagine + H2O
L-aspartate + NH3
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involved in the maintenance of the correct L-asparagine/L-aspartate ratio
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-
?
L-asparagine + H2O
L-aspartate + NH3
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involved in the maintenance of the correct L-asparagine/L-aspartate ratio
-
-
?
L-asparagine + H2O
L-aspartate + NH3
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hydrolysis at a rate of 0.73 compared to L-glutamine
-
?
L-asparagine + H2O
L-aspartate + NH3
-
hydrolysis at a rate of 0.73 compared to L-glutamine
-
?
L-glutamine + H2O
L-glutamate + NH3
-
higher activity for glutaminase than for asparaginase
-
?
L-glutamine + H2O
L-glutamate + NH3
-
involved in the maintenance of the correct L-glutamine/L-glutamate ratio
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
involved in the maintenance of the correct L-glutamine/L-glutamate ratio
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
involved in the maintenance of the correct L-glutamine/L-glutamate ratio
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
involved in the maintenance of the correct L-glutamine/L-glutamate ratio
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
higher activity for glutaminase than for asparaginase
-
?
L-glutamine + H2O
L-glutamate + NH3
-
higher activity for glutaminase than for asparaginase
-
?
L-glutamine + H2O
L-glutamate + NH3
-
one fifth of the activity on L-asparagine
-
?
L-glutamine + H2O
L-glutamate + NH3
Tilachlidium humicola
-
lower activity than for L-asparagine
-
?
additional information
?
-
-
glutaminase/asparaginase is downregulated during growth of the aauR mutant on Glu
-
-
?
additional information
?
-
-
glutaminase/asparaginase is downregulated during growth of the aauR mutant on Glu
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-Hydroxy-5-nitrobenzyl bromide
-
40% inhibition at 10 mM, concentration-dependent, protection against inhibition in presence of substrate
aspartic acid
-
competitive inhibition, Ki: glutaminase activity 0.16 mM, asparaginase activity 0.53 mM
azaserine
-
competitive not reversible inhibition of both activities
D-asparagine
Tilachlidium humicola
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mixed type of competitive and non-competitive inhibition, Ki: 7.2-8.4 mM
glutamic acid
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competitive inhibition, Ki: glutaminase acitvity 5 mM, asparaginase activity 3 mM
L-asparagine
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competitive inhibition of glutaminase activity, Ki: 0.02 mM
N-bromosuccinimide
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concentration-dependent inhibition, 40% at 10 mM, protection against inhibition in presence of substrate
NH4Cl
-
weak non-competitive inhibition of glutaminase activity
5-Diazo-4-oxo-L-norvaline
inactivation by covalent binding to Thr20 and Tyr34
6-diazo-5-oxo-L-norleucine
-
irreversible inhibition at very low concentrations
6-diazo-5-oxo-L-norleucine
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competitive not reversible inhibition of both activities after extensive dialysis
6-diazo-5-oxo-L-norleucine
inactivation by covalent binding to Thr20 and Tyr34
p-chloromercuribenzoate
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complete inhibition at 0.1 mM, asparaginases A and B
p-chlor