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Information on EC 3.5.1.38 - glutamin-(asparagin-)ase and Organism(s) Pseudomonas sp. and UniProt Accession P10182

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IUBMB 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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This record set is specific for:
Pseudomonas sp.
UNIPROT: P10182
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Word Map
The taxonomic range for the selected organisms is: Pseudomonas sp.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
glutaminase-asparaginase, asparaginase a, periplasmic glutaminase/asparaginase, glutamin-(asparagin-)ase, glutaminase/asparaginase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glutaminase-asparaginase
-
-
-
-
PGA
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylic acid amide hydrolysis
-
-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
39335-03-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-asparagine + H2O
D-aspartate + NH3
show the reaction diagram
D-glutamine + H2O
D-glutamate + NH3
show the reaction diagram
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
5-diazo-4-oxo-L-norvaline + H2O
?
show the reaction diagram
-
-
-
-
?
beta-cyanoalanine + H2O
alanine + NH3
show the reaction diagram
-
slow hydrolysis rate
-
?
D-asparagine + H2O
D-aspartate + NH3
show the reaction diagram
-
-
-
?
D-glutamine + H2O
D-glutamate + NH3
show the reaction diagram
-
-
-
?
gamma-L-glutamyl hydroxylammonium sulfate + H2O
L-glutamate + hydroxylammonium sulfate
show the reaction diagram
-
same rate as for L-glutamine
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
succinamic acid + H2O
succinate + NH3
show the reaction diagram
-
slow hydrolysis rate
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-Diazo-4-oxo-L-norvaline
inactivation by covalent binding to Thr20 and Tyr34
6-diazo-5-oxo-L-norleucine
inactivation by covalent binding to Thr20 and Tyr34
(NH4)2SO4
-
inhibition above 10 mM
5-Diazo-4-oxo-L-norvaline
-
marked inhibition at 0.1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004
L-asparagine
-
-
0.005
L-glutamine
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
-
for L-asparagine
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
140000
-
sedimentation equilibrium analysis
36000
-
4 * 36000, sedimentation equilibrium analysis in the presence of guanidine HCl, amino acid analysis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
native crystallization
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, in presence of inhibitors
molecular replacement method, 1.7 A resolution
molecular replacement method, 2.0 A resolution, 20-residue loop as part of the active site
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to crystalline form, 3step chromatography
-
to homogeneity
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Pseudomonas sp. (P10182), Pseudomonas sp. 7A (P10182), Pseudomonas sp. 7A
Manually annotated by BRENDA team
Jakob, C.G.; Lewinski, K.; LaCount, M.W.; Roberts, J.; Lebioda, L.
Ion binding induces closed conformation in Pseudomonas 7A glutaminase-asparaginase (PGA): Crystal structure of the PGA-SO42-NH4+ complex at 1.7 A resolution
Biochemistry
36
923-931
1997
Pseudomonas sp. (P10182), Pseudomonas sp. 7A (P10182), Pseudomonas sp. 7A
Manually annotated by BRENDA team
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
Pseudomonas sp., Pseudomonas sp. 7A
Manually annotated by BRENDA team
Holcenberg, J.S.; Teller, D.C.
Physical properties of antitumor glutaminase-asparaginase from Pseudomonas 7A
J. Biol. Chem.
251
5375-5380
1976
Pseudomonas sp., Pseudomonas sp. 7A
Manually annotated by BRENDA team
Roberts, J.
Purification and properties of a highly potent antitumor glutaminase-asparaginase from Pseudomonas 7A
J. Biol. Chem.
251
2119-2123
1976
Pseudomonas sp., Pseudomonas sp. 7A
Manually annotated by BRENDA team