Information on EC 3.5.1.38 - glutamin-(asparagin-)ase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
3.5.1.38
-
RECOMMENDED NAME
GeneOntology No.
glutamin-(asparagin-)ase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-glutamine + H2O = L-glutamate + NH3
show the reaction diagram
L-asparagine is hydrolysed at 0.8 of the rate of L-glutamine, the D-isomers are also hydrolysed, but more slowly
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
carboxylic acid amide hydrolysis
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Alanine, aspartate and glutamate metabolism
-
Arginine and proline metabolism
-
asparagine degradation I
-
Biosynthesis of secondary metabolites
-
citrulline biosynthesis
-
D-Glutamine and D-glutamate metabolism
-
glutamine degradation I
-
Metabolic pathways
-
superpathway of aspartate and asparagine biosynthesis; interconversion of aspartate and asparagine
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
asparaginase A
-
-
asparaginase B
-
-
glutaminase-asparaginase
-
-
-
-
glutaminase/asparaginase
-
-
periplasmic glutaminase/asparaginase
-
-
PGA
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
39335-03-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
NRRL3; strain NRRL3, highest activity in 4 days old nitrate-grown mats
-
-
Manually annotated by BRENDA team
NRRL3; strain NRRL3, highest activity in 4 days old nitrate-grown mats
-
-
Manually annotated by BRENDA team
3 forms: asparaginase-glutaminase, asparaginase A, asparaginase B
-
-
Manually annotated by BRENDA team
; nitrate-grown mat
-
-
Manually annotated by BRENDA team
; nitrate-grown mat
-
-
Manually annotated by BRENDA team
Pseudomonas chlororaphis subsp. aurantiaca 548
strain 548
-
-
Manually annotated by BRENDA team
strain KT2440; strain KT2440, gene gltB
-
-
Manually annotated by BRENDA team
strain 7A
Uniprot
Manually annotated by BRENDA team
Tilachlidium humicola
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-diazo-4-oxo-L-norvaline + H2O
?
show the reaction diagram
-
-
-
-
?
5-diazo-4-oxo-L-norvaline + H2O
?
show the reaction diagram
-
-
-
-
?
5-diazo-4-oxo-L-norvaline + H2O
?
show the reaction diagram
-
-
-
-
?
aspartic acid + H2O
?
show the reaction diagram
-
very low activity only for asparaginase B
-
-
?
beta-cyanoalanine + H2O
alanine + NH3
show the reaction diagram
-
slow hydrolysis rate
-
?
beta-cyanoalanine + H2O
alanine + NH3
show the reaction diagram
-
slow hydrolysis rate
-
?
beta-D-aspartyl hydroxylammonium sulfate + H2O
L-Asp + hydroxylammonium sulfate
show the reaction diagram
-
-
-
?
beta-D-aspartyl hydroxylammonium sulfate + H2O
L-Asp + hydroxylammonium sulfate
show the reaction diagram
-
only asparaginase A, low activity
-
?
beta-L-aspartyl hydroxylammonium sulfate + H2O
L-Asp + hydroxylammonium sulfate
show the reaction diagram
-
-
-
?
beta-L-aspartyl hydroxylammonium sulfate + H2O
L-Asp + hydroxylammonium sulfate
show the reaction diagram
-
-
-
?
beta-L-aspartyl hydroxylammonium sulfate + H2O
L-Asp + hydroxylammonium sulfate
show the reaction diagram
-
-
-
?
beta-L-aspartyl hydroxylammonium sulfate + H2O
L-Asp + hydroxylammonium sulfate
show the reaction diagram
-
higher activity for asparaginase B
-
?
D-asparagine + H2O
D-aspartate + NH3
show the reaction diagram
-
-
-
-
?
D-asparagine + H2O
D-aspartate + NH3
show the reaction diagram
-
-
-
?
D-asparagine + H2O
D-aspartate + NH3
show the reaction diagram
P10182
-
-
?
D-asparagine + H2O
D-aspartate + NH3
show the reaction diagram
-
-
-
?
D-asparagine + H2O
D-aspartate + NH3
show the reaction diagram
-
-
-
?
D-asparagine + H2O
D-aspartate + NH3
show the reaction diagram
Tilachlidium humicola
-
-
-
?
D-asparagine + H2O
D-aspartate + NH3
show the reaction diagram
-
low activity
-
?
D-asparagine + H2O
D-aspartate + NH3
show the reaction diagram
-
low activity
-
?
D-asparagine + H2O
D-aspartate + NH3
show the reaction diagram
-
one third of the L-isomer
-
?
D-asparagine + H2O
D-aspartate + NH3
show the reaction diagram
-
-
-
?
D-glutamine + H2O
D-glutamate + NH3
show the reaction diagram
P10182
-
-
?
D-glutamine + H2O
D-glutamate + NH3
show the reaction diagram
-
-
-
?
D-glutamine + H2O
D-glutamate + NH3
show the reaction diagram
-
-
-
?
D-glutamine + H2O
D-glutamate + NH3
show the reaction diagram
-
low activity
-
?
D-glutamine + H2O
D-glutamate + NH3
show the reaction diagram
-
low activity
-
?
D-glutamine + H2O
D-glutamate + NH3
show the reaction diagram
Tilachlidium humicola
-
low activity
-
?
D-glutamine + H2O
D-glutamate + NH3
show the reaction diagram
-
one third of the L-isomer
-
?
D-glutamine + H2O
D-glutamate + NH3
show the reaction diagram
-
-
-
?
gamma-L-glutamyl hydroxylammonium sulfate + H2O
L-glutamate + hydroxylammonium sulfate
show the reaction diagram
-
-
-
?
gamma-L-glutamyl hydroxylammonium sulfate + H2O
L-glutamate + hydroxylammonium sulfate
show the reaction diagram
-
-
-
?
gamma-L-glutamyl hydroxylammonium sulfate + H2O
L-glutamate + hydroxylammonium sulfate
show the reaction diagram
-
-
-
?
gamma-L-glutamyl hydroxylammonium sulfate + H2O
L-glutamate + hydroxylammonium sulfate
show the reaction diagram
-
same rate as for L-glutamine
-
?
gamma-L-glutamyl hydroxylammonium sulfate + H2O
L-glutamate + hydroxylammonium sulfate
show the reaction diagram
-
very low activities for both asparaginases A and B
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
P10182
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
Tilachlidium humicola
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
not active on D-asparagine
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
hydrolysed at a rate of 0.83 compared to L-glutamine
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
hydrolysed at a rate of 0.73 compared to L-glutamine, hydrolysis at a rate of 0.73 compared to L-glutamine
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
involved in the maintenance of the correct L-asparagine/L-aspartate ratio
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
ratio of glutaminase to aspariginase activity is 0.7 to 1
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
ratio of glutaminase to aspariginase activity is 0.8 to 1
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
ratio of glutaminase to aspariginase activity is 1.4 to 1
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
involved in the maintenance of the correct L-asparagine/L-aspartate ratio
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
Pseudomonas chlororaphis subsp. aurantiaca 548
-
hydrolysed at a rate of 0.73 compared to L-glutamine, hydrolysis at a rate of 0.73 compared to L-glutamine
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
-
-
?
L-asparagine + H2O
L-aspartate + 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
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
P10182
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
low activity
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
Tilachlidium humicola
-
lower activity than for L-asparagine
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
higher activity for glutaminase than for asparaginase
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
higher activity for glutaminase than for asparaginase
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
higher activity for glutaminase than for asparaginase
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
one fifth of the activity on L-asparagine
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
involved in the maintenance of the correct L-glutamine/L-glutamate ratio
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
ratio of glutaminase to aspariginase activity is 0.7 to 1
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
ratio of glutaminase to aspariginase activity is 0.8 to 1
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
ratio of glutaminase to aspariginase activity is 1.4 to 1
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-, involved in the maintenance of the correct L-glutamine/L-glutamate ratio, ratio of glutaminase to aspariginase activity is 0.7 to 1
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
Pseudomonas chlororaphis subsp. aurantiaca 548
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
higher activity for glutaminase than for asparaginase
-
?
N-acetyl-L-asparagine + H2O
N-acetyl-L-aspartate + NH3
show the reaction diagram
-
-
-
?
N-acetyl-L-asparagine + H2O
N-acetyl-L-aspartate + NH3
show the reaction diagram
-
5% of the activity compared to L-asparagine
-
?
N-carbamoyl-L-asparagine + H2O
N-carbamoyl-L-aspartate + NH3
show the reaction diagram
-
-
-
?
N-glycyl-L-asparagine + H2O
N-glycyl-L-aspartate + NH3
show the reaction diagram
-
60% higher activity than on L-asparagine
-
?
succinamic acid + H2O
succinate + NH3
show the reaction diagram
-
slow hydrolysis rate
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-, higher activity for glutaminase than for asparaginase
-
?
additional information
?
-
-
glutaminase/asparaginase is downregulated during growth of the aauR mutant on Glu
-
-
-
additional information
?
-
-
acetamide, nicotinamide, and NAD are not hydrolyzed
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
P10182
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
Tilachlidium humicola
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
hydrolysed at a rate of 0.83 compared to L-glutamine
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
hydrolysis at a rate of 0.73 compared to L-glutamine
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
involved in the maintenance of the correct L-asparagine/L-aspartate ratio
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
Pseudomonas chlororaphis subsp. aurantiaca 548
-
hydrolysis at a rate of 0.73 compared to L-glutamine
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
-
-
?
L-asparagine + H2O
L-aspartate + 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
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
P10182
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
low activity
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
Tilachlidium humicola
-
lower activity than for L-asparagine
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
higher activity for glutaminase than for asparaginase
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
higher activity for glutaminase than for asparaginase
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
one fifth of the activity on L-asparagine
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
involved in the maintenance of the correct L-glutamine/L-glutamate ratio
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
Pseudomonas chlororaphis subsp. aurantiaca 548
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
higher activity for glutaminase than for asparaginase
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
?
additional information
?
-
-
glutaminase/asparaginase is downregulated during growth of the aauR mutant on Glu
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Fe3+
Tilachlidium humicola
-
30% activation at 1 mM
Ni2+
-
slightly enhanced activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(NH4)2SO4
-
inhibition above 10 mM
2-Hydroxy-5-nitrobenzyl bromide
-
40% inhibition at 10 mM, concentration-dependent, protection against inhibition in presence of substrate
5-diazo-4-oxo-D-norvaline
-
40% inhibition at 2 mM
5-Diazo-4-oxo-L-norvaline
-
inactivation by covalent binding to Thr20 and Tyr34
5-Diazo-4-oxo-L-norvaline
-
marked inhibition at 0.1 mM
5-Diazo-4-oxo-L-norvaline
-
50% inhibition at 0.6 mM
6-diazo-5-oxo-L-norleucine
-
inactivation by covalent binding to Thr20 and Tyr34
6-diazo-5-oxo-L-norleucine
-
competitive not reversible inhibition of both activities after extensive dialysis
6-diazo-5-oxo-L-norleucine
-
irreversible inhibition at very low concentrations
acivicin
-
competitive inhibition
aspartic acid
-
competitive inhibition, Ki: glutaminase activity 0.16 mM, asparaginase activity 0.53 mM
azaserine
-
competitive not reversible inhibition of both activities
Bromocresol green
-
52-66% inhibition at 1 mM
Cu2+
Tilachlidium humicola
-
slight inhibition at 1 mM
D-asparagine
Tilachlidium humicola
-
mixed type of competitive and non-competitive inhibition, Ki: 7.2-8.4 mM
EDTA
Tilachlidium humicola
-
slight inhibition at 8 mM
glutamic acid
-
competitive inhibition, Ki: glutaminase acitvity 5 mM, asparaginase activity 3 mM
Hg2+
-
slight inhibition
Hg2+
Tilachlidium humicola
-
slight inhibition at 1 mM
iodoacetamide
-
slight inhibition
KCN
Tilachlidium humicola
-
slight inhibition at 8 mM
L-asparagine
-
competitive inhibition of glutaminase activity, Ki: 0.02 mM
L-methionine sulfoximine
-
competitive inhibition
N-bromosuccinimide
-
concentration-dependent inhibition, 40% at 10 mM, protection against inhibition in presence of substrate
NaAsO2
Tilachlidium humicola
-
90% inhibition at 8 mM
NaF
Tilachlidium humicola
-
slight inhibition at 8 mM
NH4Cl
-
weak non-competitive inhibition of glutaminase activity
Ni2+
Tilachlidium humicola
-
33% inhibition at 1 mM
p-chloromercuribenzoate
-
slight inhibition
p-chloromercuribenzoate
-
26% inhibition at 0.1 mM
p-chloromercuribenzoate
-
complete inhibition at 0.1 mM, asparaginases A and B
p-chloromercuribenzoate
Tilachlidium humicola
-
slight inhibition
Urea
-
95% loss of activity in 2.25 M
additional information
-
no product inhibition
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
slight activation
cysteine
-
slight activation
dithiothreitol
-
slight activation
additional information
-
use of phosphate buffer yields higher activities than Tris, phthalate, or citrate buffer, optimum concentration is 0.08 - 0.16 M phosphate
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0026
-
L-asparagine
-
pH6, 40C
0.004
-
L-asparagine
-
-
0.005
-
L-asparagine
-
-
0.015
-
L-asparagine
-
-
0.029
-
L-asparagine
-
asparaginase A
0.3
-
L-asparagine
Tilachlidium humicola
-
-
1.43
-
L-asparagine
-
-
1.7
-
L-asparagine
-
asparaginase B
2.57
-
L-asparagine
-
-
0.002
-
L-glutamine
-
-
0.005
-
L-glutamine
-
-
0.0051
-
L-glutamine
-
pH6, 40C
0.022
-
L-glutamine
-
-
0.083
-
L-glutamine
-
for succinylated enzyme
0.6
-
L-glutamine
Tilachlidium humicola
-
-
5.05
-
L-glutamine
-
-
6.45
-
L-glutamine
-
-
10
-
N-acetyl-L-asparagine
-
-
8
-
N-carbamoyl-L-asparagine
-
-
2.4
-
N-glycyl-L-asparagine
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.6
-
5-Diazo-4-oxo-L-norvaline
-
-
7.2
8.4
D-asparagine
Tilachlidium humicola
-
mixed type of competitive and non-competitive inhibition
0.02
-
L-asparagine
-
competitive inhibition of glutaminase activity
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1.6
-
-
asparaginase B
17.2
-
Tilachlidium humicola
-
-
86
-
-
asparaginase activity
100
-
-
for L-asparagine
104
-
-
glutaminase activity
133
-
-
asparaginase A
2156
-
-
glutaminase activity
10510
-
-
asparaginase activity
additional information
-
-
intracellular amino acid levels of wild-type and mutant strains
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
activity is higher in phosphate buffer than in citrate buffer
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
7
-
optimal range for asparaginase activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
55
Tilachlidium humicola
-
-
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
induction of enzyme synthesis by addition of glutamic acid to the medium, glucose inhibits enzyme synthesis
Manually annotated by BRENDA team
Tilachlidium humicola
-
enzyme formation affected by culture conditions
Manually annotated by BRENDA team
-
highest enzyme formation in L-glutamic acid containing medium
Manually annotated by BRENDA team
Pseudomonas chlororaphis subsp. aurantiaca 548
-
-
-
Manually annotated by BRENDA team
-
induction of enzyme synthesis by addition of glutamic acid to the medium, glucose inhibits enzyme synthesis
-
Manually annotated by BRENDA team
additional information
-
the organism is able to grow on asparagine and glutamine as sole carbon and nitrogen source
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Tilachlidium humicola
-
-
-
Manually annotated by BRENDA team
-
; a functional gltB gene (encoding a subunit of EC 1.4.1.13) is essential for utilization of acidic amino acids and expression of periplasmic glutaminase/asparaginase
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Pseudomonas sp. (strain ATCC 29598 / 7A)
Pseudomonas sp. (strain ATCC 29598 / 7A)
Pseudomonas sp. (strain ATCC 29598 / 7A)
Pseudomonas sp. (strain ATCC 29598 / 7A)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
132000
138000
-
sedimentation equilibrium analysis
140000
-
-
asparaginase A, gel filtration
140000
-
-
sedimentation equilibrium analysis
156000
-
-
gel filtration
180000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
2 * 87000, SDS-PAGE
tetramer
P10182
native crystallization
tetramer
-
-
tetramer
-
native crystallization
tetramer
-
4 * 39000, SDS-PAGE
tetramer
-
4 * 33000, SDS-PAGE
tetramer
-
4 * 36000, sedimentation equilibrium analysis in the presence of guanidine HCl, amino acid analysis
tetramer
-
4 * 33000, denaturating sedimentation equilibrium analysis
tetramer
-
; 4 * 36000, sedimentation equilibrium analysis in the presence of guanidine HCl, amino acid analysis
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging drop vapor diffusion method, single subunit, 2 A resolution
-
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
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
-
-
complete inactivation
7.2
-
Tilachlidium humicola
-
less stable than at pH 5.6 or pH 10
7.4
-
-
70% activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
Tilachlidium humicola
-
stable within 16 h between pH 4-10
40
-
-
30 min, about 10% loss of activity
50
-
-
half-life: 10 min, protection against thermal inactivation by addition of substrate
50
-
-
30 min, about 40% loss of activity
51
-
-
asparaginase B, half-life: 10 min
60
-
-
30 min, about 70% loss of activity; incubation at 60C in the absence of substrate for 20 min causes a 70% increase in activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
stabilizing effect during purification by sodium glutamate
-
stabilizing effect by addition of glycine and maintaining the pH to 9.0
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
activity is retained in the freezer for some months
-
4C, 12 months, asparaginase A, asparaginase B: DTT required, 6 months
-
4C, 50 mM borate buffer, pH 7.0, 100 mM NaCl, 1 mM EDTA, 3 to 4 months
-
-10C, lyophilized to dryness in the presence of 50 mM Tris, 250 mM glycine, pH 9.0, 90% activity in 3 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
to homogeneous crystals
-
to homogeneity, asparaginase A
-
to homogeneity, 3step chromatography
-
to homogeneity, improved purification by treatment with protamine sulfate, heating in the presence of stabilizer sodium glutamate
-
near homogeneity, recombinant enzyme
-
to crystalline form, 3step chromatography
-
to homogeneity
-
to homogeneity, chromatography, preparative gel electrophoresis
-
partial
Tilachlidium humicola
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
transposon mutagenesis with self-cloning promoter probe vector Tn5-OT182 for inactivation by disruption of gene gltB, gltB mutants lose the ability to utilize amino acids as carbon source, inactivation of gene gltB and other glutamate-induced genes by random mutagenesis, phenotype, overview
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
drug development
-
enzyme could possibly be used as an anti-tumor therapeutic agent
drug development
-
enzyme could possibly be used as an anti-tumor therapeutic agent
-