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Information on EC 3.5.1.1 - asparaginase
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3.5.1.1 asparaginaseSpecify your search results
Word Map
- 3.5.1.1
- leukemia
- lymphoblastic
- children
-
remission
-
pediatric
- erwinia
- vincristine
- hypersensitivity
-
relapse
- methotrexate
- lymphoma
- thrombosis
- prednisone
-
pegylated
-
pharmacokinetics
-
schedule
-
high-dose
- cyclophosphamide
-
oncology
-
intensification
-
consolidation
- venous
- cytarabine
-
intrathecal
-
event-free
- l-glutamine
- mercaptopurine
- anthracyclines
- allergy
-
l-aspartic
- chrysanthemi
- carotovora
-
cranial
- medicine
- thromboembolism
- antithrombin
- daunorubicin
-
arabinoside
-
prophylaxis
-
reinduction
- food industry
- pharmacology
-
b-precursor
- diagnostics
-
coli-derived
-
standard-risk
- synthesis
- osteonecrosis
-
b-lineage
-
extranodal
-
dana-farber
-
antileukaemic
-
multiagent
- analysis
- biotechnology
- teniposide
- succinogenes
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
14270 ASNase, alpha-asparaginase, AnsA, ansA3, ansZ, Asn, ASNase, ASNase1, ASNase3, asparaginase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
14270 ASNase
alpha-asparaginase
-
-
-
-
AnsA
ansA3
ansZ
Asn
ASNase
ASNase3
asparaginase
asparaginase II
asparagine amidohydrolase
ASPG II
-
three forms, ASPG I, ASPG II, and ASPG III. ASPG II shows the highest specific activity
colaspase
-
-
-
-
crasnitin
-
-
-
-
DiAsp
-
-
-
-
elspar
-
-
-
-
ErA
glutamine-(asparagin-)ase
HPA
L-ASNase
L-asparaginase
L-asparaginase II
L-asparaginase III
L-asparagine amidohydrolase
leunase
-
-
-
-
SGR ASNase
type II L-asparaginase
Ypa
asparaginase II
-
-
-
-
L-ASNase
-
-
-
-
L-asparaginase
-
-
-
-
L-asparaginase
-
-
L-asparagine amidohydrolase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-asparagine + H2O = L-aspartate + NH3
-
-
-
-
L-asparagine + H2O = L-aspartate + NH3
active site structure with a flexible loop that is stabilized by a beta-hairpin formation and intracellular interaction with the alpha-helical region, modelling
-
L-asparagine + H2O = L-aspartate + NH3
kinetic model, substrate specificity, and catalytic mechanism, active site residues are Asp115 and Glu82, the structural transition of the enzyme is rate-limiting in the reaction, entropy changes are the main determinants for the substrate specificity
-
L-asparagine + H2O = L-aspartate + NH3
active site structure involving Thr193, autocatalytic activation mechanism involving Thr193
-
L-asparagine + H2O = L-aspartate + NH3
kinetic model, substrate specificity, and catalytic mechanism, active site residues are Asp115 and Glu82, the structural transition of the enzyme is rate-limiting in the reaction, entropy changes are the main determinants for the substrate specificity
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylic acid amide hydrolysis
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
L-asparagine amidohydrolase
-
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CAS REGISTRY NUMBER
COMMENTARY
9015-68-3
-
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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
benzyloxycarbonyl-Gly-L-Asn + H2O
benzyloxycarbonyl-Gly-L-Asp
-
-
-
?
beta-Asp-His + H2O
?
-
substrate of ASPGA1 and ASPGB1, ASPGA1 has a 4fold substrate preference for beta-Asp-His over Asn
-
-
?
beta-aspartoethylamide + H2O
?
-
at 0.4% of the activity with L-Asn
-
-
?
beta-aspartomethylamide + H2O
L-Asp + ethylamine
-
at 0.5% of the activity with L-Asn
-
-
?
beta-aspartopropylamide + H2O
?
-
at 0.7% of the activity with L-Asn
-
-
?
D-aspartic acid beta-hydroxamate + H2O
D-Asp + hydroxylamine
-
59% of the activity with L-Asn
-
-
?
diazo-4-oxo-L-norvaline + H2O
5-hydroxy-4-oxo-L-norvaline + NH3
-
-
-
?
DL-Ala-DL-Asn + H2O
DL-Ala-DL-Asn + DL-Ala-DL-Asp
-
-
75% Ala-Asp + 25% Ala-Asn
?
L-aspartic acid beta-hydrazide + H2O
L-Asp + hydroxylamine
-
2% of the activity with L-Asn
-
-
?
L-glutamic acid gamma-hydroxamate + H2O
L-Glu + hydroxylamine
-
1% of the activity with L-Asn
-
-
?
L-glutamine + H2O
L-glutamate + H2O
-
36% relative activity compared to L-asparagine as substrate
-
-
?
L-glutamyl hydroxamate + H2O
L-glutamate + hydroxylamine
-
16% relative activity compared to L-asparagine as substrate
-
-
?
N4-ethyl-L-asparagine
L-Asp + propylamine
-
12% of the activity with L-Asn
-
-
?
N4-methoxy-L-asparagine + H2O
L-Asp + O-methylhydroxylamine
-
154% of the activity with L-Asn
-
-
?
N4-methyl-L-asparagine
L-Asp + methylamine
-
12% of the activity with L-Asn
-
-
?
Nalpha-methyl-L-Asn + H2O
Nalpha-methyl-L-Asp + NH3
-
26% of the activity with L-Asn
-
-
?
threo-3-hydroxy-L-asparagine + H2O
?
-
36% of the activity with L-Asn
-
-
?
beta-cyano-L-Ala + H2O
?
-
at 5.7% of the activity with L-Asn
-
-
?
D-Asn + H2O
D-Asp + NH3
-
at 5% of the activity with L-Asn
-
-
?
D-asparagine + H2O
D-aspartate + NH3
-
catalytic activity of the recombinant enzyme for L-asparagine is 5fold higher than for D-asparagine
-
-
?
D-asparagine + H2O
D-aspartate + NH3
-
less than 10% activity compared to L-asparagine
-
-
?
D-asparagine + H2O
D-aspartate + NH3
negligible activity
-
-
?
DL-aspartyl hydroxamate + H2O
DL-Asp + hydroxylamine
-
66% of the activity with L-Asn
-
-
?
L-asparagine + H2O
L-aspartate + NH3
strictly specific for L-Asn, has no activity towards beta-aspartyl dipeptides
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
substrate of ASPGA1 and ASPGB1, but ASPGB1 has a 45fold higher specific activity with Asn as substrate than ASPGA1, ASPGA1 has a 4fold substrate preference for beta-Asp-His over Asn
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
catalytic activity of the recombinant enzyme for L-asparagine is 5fold higher than for D-asparagine
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
highly specific substrate
-
-
?
L-asparagine + H2O
L-aspartate + NH3
100% activity
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
substrate hydrolysis efficiency of L-asparagine is 8fold higher than that of L-glutamine
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
the enzyme does not reduce alpha-antiplasmin and plasminogen levels in human patients with acute lymphoblastic leukemia
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
the enzyme reduces alpha-antiplasmin and plasminogen levels in human patients with acute lymphoblastic leukemia
-
-
?
L-asparagine + H2O
L-aspartate + NH3
I0ZIE0
strongly preferred substrate
-
-
?
L-asparagine + H2O
L-aspartate + NH3
I0ZIE0
strongly preferred substrate
-
-
?
L-asparagine + H2O
L-aspartate + NH3
highly specific substrate
-
-
?
L-asparagine + H2O
L-aspartate + NH3
highly specific substrate
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
highest specificity for L-asparagine
-
-
?
L-asparagine + H2O
L-aspartate + NH3
highest specificity for L-asparagine
-
-
?
L-asparagine + H2O
L-aspartate + NH3
best substrate
-
-
?
L-asparagine + H2O
L-aspartic acid + NH3
-
specificity: free from L-glutaminase activity
-
-
?
L-asparagine + H2O
L-aspartic acid + NH3
-
specificity: free from L-glutaminase activity
-
-
?
L-aspartic acid + NH3
?
less than 3% activity compared to L-asparagine
-
-
?
L-aspartic acid + NH3
?
less than 3% activity compared to L-asparagine
-
-
?
L-aspartic acid beta-hydroxamate + H2O
L-Asp + hydroxylamine
-
59% of the activity with L-Asn
-
-
?
L-aspartic acid beta-hydroxamate + H2O
L-Asp + hydroxylamine
-
11% of the activity with L-Asn
-
-
?
L-aspartic acid beta-hydroxamate + H2O
L-Asp + hydroxylamine
-
11% of the activity with L-Asn
-
-
?
L-aspartic acid beta-hydroxamate + H2O
L-Asp + hydroxylamine
-
-
-
-
?
L-aspartyl hydroxamate + H2O
L-aspartate + hydroxylamine
-
60% relative activity compared to L-asparagine as substrate
-
-
?
L-Gln + H2O
L-Glu + NH3
-
to about the same extent as L-Asn
-
-
?
L-Gln + H2O
L-Glu + NH3
-
at 10% of the activity with L-Asn
-
-
?
L-Gln + H2O
L-Glu + NH3
-
at 4% of the activity with L-asparagine
-
-
?
L-glutamine + H2O
?
58.2% activity compared to L-asparagine
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
recombinant enzyme has 4fold higher activity for L-asparagine than for L-glutamine
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
less than 1% activity compared to L-asparagine
-
-
?
L-glutamine + H2O
L-glutamate + NH3
less than 1% activity compared to L-asparagine
-
-
?
L-glutamine + H2O
L-glutamate + NH3
less than 1% activity compared to L-asparagine
-
-
?
L-glutamine + H2O
L-glutamate + NH3
negligible activity
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
YpA L-glutaminase activity is relatively low and more than 15 times less than specific activity towards L-Asn
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
YpA L-glutaminase activity is relatively low and more than 15 times less than specific activity towards L-Asn
-
-
?
poly-L-asparagine + H2O
?
-
at 21.7% of the activity with L-Asn
-
-
?
additional information
?
-
-
the enzyme shows anti-leukemic activity
-
-
-
additional information
?
-
not active with N-acetylglucosaminyl-L-Asn
-
-
-
additional information
?
-
-
no activity with D-asparagine monohydrate and L-glutamic acid
-
-
-
additional information
?
-
no activity with D-asparagine monohydrate and L-glutamic acid
-
-
-
additional information
?
-
-
no activity with D-glutamine, L-aspartic acid, D-aspartic acid, L-glutamic acid, and ornathine
-
-
-
additional information
?
-
-
no activity with D-asparagine monohydrate and L-glutamic acid
-
-
-
additional information
?
-
no activity with D-asparagine monohydrate and L-glutamic acid
-
-
-
additional information
?
-
-
the recombinant enzyme shows low affinity to L-glutamine
-
-
-
additional information
?
-
-
the recombinant enzyme shows low affinity to L-glutamine
-
-
-
additional information
?
-
-
the enzyme requires autocleavage to become active
-
-
-
additional information
?
-
H0VQC8
the enzyme requires autocleavage to become active
-
-
-
additional information
?
-
the enzyme lacks L-glutaminase activity
-
-
-
additional information
?
-
-
the enzyme selectively inhibits rapamycin-targeted signaling pathway in leukemic cell lines, the enzyme suppresses synthesis of ribosomal proteins at the level of mRNA translation
-
-
-
additional information
?
-
-
residues 195RKH197 are critical for enzyme antigenicity
-
-
-
additional information
?
-
-
L-asparaginase from Escherichia coli is more immuno-depressive and immunotoxic than that from Erwinia carotovora
-
-
-
additional information
?
-
-
L-asparaginase is cytotoxic, resistance to L-asparaginase in TEL-AML1-negative but not TEL-AML1-positive pediatric acute lymphoblastic cells is due to increased cellular expression of asparagine synthase, overview
-
-
-
additional information
?
-
to become enzymatically active, ASNase3 must undergo autocleavage between residues Gly167 and Thr168
-
-
-
additional information
?
-
-
the enzyme performs autocatalytic activation, overview
-
-
-
additional information
?
-
no activity with L-glutamine, L-aspartic acid, L-glutamic acid, thiourea, L-histidine, glutathione, L-arginine, and glycine
-
-
-
additional information
?
-
-
no activity with L-glutamine, L-aspartic acid, L-glutamic acid, thiourea, L-histidine, glutathione, L-arginine, and glycine
-
-
-
additional information
?
-
no activity with L-glutamine, L-aspartic acid, L-glutamic acid, thiourea, L-histidine, glutathione, L-arginine, and glycine
-
-
-
additional information
?
-
-
L-asparaginase from Escherichia coli is more immuno-depressive and immunotoxic than that from Erwinia carotovora
-
-
-
additional information
?
-
-
no glutaminase activity is observed
-
-
-
additional information
?
-
-
the hydrolysis efficiency of asparagine is at least 11925fold higher than that of L-glutamine
-
-
-
additional information
?
-
Q8TZE8
increased substrate accessibility through the active site loop plays a major role in determining activity, dynamic flipping of a critical Tyr residue is responsible for the activity of thermophilic L-asparaginases, molecular dynamic simulation and reaction mechanism, overview
-
-
-
additional information
?
-
-
the N-terminal domain of L-asparaginase functions as a non-specific, stable, molecular chaperone
-
-
-
additional information
?
-
-
enzyme shows negligible activity with both D-asparagine (22 U/mg) and L-glutamine (36 U/mg) as the substrates
-
-
-
additional information
?
-
-
antiproliferating activity on the breast cancer cell lines T47D, BT20, and MCF-7
-
-
-
additional information
?
-
-
no activity with D-asparagine as substrate
-
-
-
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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
D-asparagine + H2O
D-aspartate + NH3
-
less than 10% activity compared to L-asparagine
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
highly specific substrate
-
-
?
L-asparagine + H2O
L-aspartate + NH3
R4L284
100% activity
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
substrate hydrolysis efficiency of L-asparagine is 8fold higher than that of L-glutamine
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
the enzyme does not reduce alpha-antiplasmin and plasminogen levels in human patients with acute lymphoblastic leukemia
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
the enzyme reduces alpha-antiplasmin and plasminogen levels in human patients with acute lymphoblastic leukemia
-
-
?
L-asparagine + H2O
L-aspartate + NH3
I0ZIE0
strongly preferred substrate
-
-
?
L-asparagine + H2O
L-aspartate + NH3
I0ZIE0
strongly preferred substrate
-
-
?
L-asparagine + H2O
L-aspartate + NH3
W0KM71
highly specific substrate
-
-
?
L-asparagine + H2O
L-aspartate + NH3
W0KM71
highly specific substrate
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
W0G253
highest specificity for L-asparagine
-
-
?
L-asparagine + H2O
L-aspartate + NH3
W0G253
highest specificity for L-asparagine
-
-
?
L-asparagine + H2O
L-aspartate + NH3
C5A6Q4
best substrate
-
-
?
L-aspartic acid + NH3
?
R4L284
less than 3% activity compared to L-asparagine
-
-
?
L-aspartic acid + NH3
?
R4L284
less than 3% activity compared to L-asparagine
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
less than 1% activity compared to L-asparagine
-
-
?
L-glutamine + H2O
L-glutamate + NH3
R4L284
less than 1% activity compared to L-asparagine
-
-
?
L-glutamine + H2O
L-glutamate + NH3
R4L284
less than 1% activity compared to L-asparagine
-
-
?
additional information
?
-
-
the enzyme shows anti-leukemic activity
-
-
-
additional information
?
-
-
no activity with D-asparagine monohydrate and L-glutamic acid
-
-
-
additional information
?
-
R4L284
no activity with D-asparagine monohydrate and L-glutamic acid
-
-
-
additional information
?
-
-
no activity with D-glutamine, L-aspartic acid, D-aspartic acid, L-glutamic acid, and ornathine
-
-
-
additional information
?
-
-
no activity with D-asparagine monohydrate and L-glutamic acid
-
-
-
additional information
?
-
R4L284
no activity with D-asparagine monohydrate and L-glutamic acid
-
-
-
additional information
?
-
-
the enzyme requires autocleavage to become active
-
-
-
additional information
?
-
H0VQC8
the enzyme requires autocleavage to become active
-
-
-
additional information
?
-
-
residues 195RKH197 are critical for enzyme antigenicity
-
-
-
additional information
?
-
-
L-asparaginase from Escherichia coli is more immuno-depressive and immunotoxic than that from Erwinia carotovora
-
-
-
additional information
?
-
-
L-asparaginase is cytotoxic, resistance to L-asparaginase in TEL-AML1-negative but not TEL-AML1-positive pediatric acute lymphoblastic cells is due to increased cellular expression of asparagine synthase, overview
-
-
-
additional information
?
-
Q7L266
to become enzymatically active, ASNase3 must undergo autocleavage between residues Gly167 and Thr168
-
-
-
additional information
?
-
-
L-asparaginase from Escherichia coli is more immuno-depressive and immunotoxic than that from Erwinia carotovora
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Cu2+
Fe3+
K+
KCl
-
the catalytic activity of YpA does not vary significantly as a function of ionic strength at 100-3000 mM KCl
Mg2+
Mn2+
Na+
Ni2+
-
5 mM, 37°C, 136% relative activity compared to the activity in absence of metal cations
Rb+
monovalent cation preference in order of decreasing efficiency is: K+, Na+, Rb+
Zn2+
additional information
Co2+
-
5 mM, 37°C, 134% relative activity compared to the activity in absence of metal cations
K+
catalytic activity of At3g16150 is enhanced approximately tenfold in the presence of K+
K+
-
potassium-independent asparaginase ASPGA1, and potassium-dependent asparaginase ASPGB1
K+
-
potassium independent and dependent enzymes appear to be distinct proteins. The proportion of the two enzymes varies with plant species, organ and developmental age
Mg2+
marginal increase in enzyme activity in the presence of 1 mM Mg2+ (less than 15%)
Na+
monovalent cation preference in order of decreasing efficiency is: K+, Na+, Rb+
Na+
-
probably, metal binding loop structure involving Leu59, Glu60, Ile62, Phe65, Ala67, and Ile69, overview
additional information
-
potassium-independent L-asparaginase (AtA), Arabidopsis thaliana potassium-dependent L-asparaginase (AtAK)
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Glutaraldehyde
-
inhibits the enzyme during immobilization at concentrations above 0.2%
N-ethoxycarbonyl-2-ethoxy-1,2-dihydroquinline
-
no effect up to 1 mM: Mg2+, Mn2+ and Ca2+
phenylmethylsulfonyl fluoride
-
more than 80% residual activity at 10 mM
Trypsin
-
the free enzyme is completely inactivated by trypsin within 10 min, while the immobilized enzyme is stable for 240 min with loss of 30% activity
-
5-Diazo-4-oxo-L-norvaline
-
inhibits L-asparaginase activity and affects broth culture filtrate inhibition of the cell cycle
Ba2+
-
5 mM, 37°C, 25% relative activity compared to the activity in absence of metal cations
D-Asn
-
competitive, reverses antiproliferating effect on breast cancer cells
Hg2+
-
5 mM, 37°C, 20% relative activity compared to the activity in absence of metal cations
iodoacetamide
-
at pH 6.0 protection by substrate, at pH 8.0 no protection by substrate
Mn2+
-
5 mM, 37°C, 42% relative activity compared to the activity in absence of metal cations
Zn2+
-
5 mM, 37°C, 36% relative activity compared to the activity in absence of metal cations
additional information
urea and EDTA do not reveal any inhibitory effects on enzyme activity
-
additional information
-
probable mechanism of deactivation of purified L-asparaginase, thermodynamics, overview
-
additional information
-
glucose, in supplemented culture medium, causes a slight suppression of enzyme expression in wild-type strain NRRL B771
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-amino-6-methyl-4-phenyl-2-thioxy-1,2,3,4-tetrahydropyrimidine-5-carboxylic acid methyl ester
-
enhances activity
L-cystine
-
causes an increase in Vmax value and a decrease in Km value, nonessential mode of activation
L-methionine
-
causes an increase in Vmax value and a decrease in Km value, nonessential mode of activation
liquid paraffin
-
6% (v/v) results in 34% increase in the L-asparaginase activity accompanied by a 48% increase in the production of cell mass at a 10 l scale
-
N-acetyl-L-cysteine
-
causes an increase in Vmax value and a decrease in Km value, nonessential mode of activation
n-dodecane
-
exhibit a stimulatory effect in L-asparaginase activity, ca. 104% compared to control
silicone oil
-
exhibit a stimulatory effect in L-asparaginase activity, ca. 108% compared to control
-
glycine
the enzyme is activated by incubating for 4 days in a 2.0 M glycine (pH 9.0) solution at room temperature
GSH
-
causes an increase in Vmax value and a decrease in Km value, nonessential mode of activation, activates 136% at 1 mM
additional information
-
cell disrupting agents EDTA, lysozyme, and penicillin-G enhance the release of L-asparaginase from the cell culture
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.38
beta-Asp-His
-
pH 8.0, temperature not specified in the publication, wild-type ASPGB1
2.9
beta-Asp-His
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant N184A
3.13
beta-Asp-His
-
pH 8.0, temperature not specified in the publication, ASPGA1 mutant T166R
3.28
beta-Asp-His
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant N184Q
3.56
beta-Asp-His
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant S189C
3.9
beta-Asp-His
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant F162W
4.15
beta-Asp-His
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant N184D
4.91
beta-Asp-His
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant S189A
5.56
beta-Asp-His
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant F162L
5.62
beta-Asp-His
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant R165T
6.65
beta-Asp-His
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant S189T
6.79
beta-Asp-His
-
pH 8.0, temperature not specified in the publication, ASPGA1 mutant L163F
12.6
beta-Asp-His
-
pH 8.0, temperature not specified in the publication, wild-type ASPGA1
0.0291
L-asparagine
-
pH 8.6, 37°C, mutant enzyme N41D; pH 8.6, 37°C, wild-type enzyme
0.16
L-asparagine
-
pH 8.0, 37°C, recombinant AspSP, L-asparaginase II with signal peptide
0.36
L-asparagine
-
37°C, mutant enzyme R206H covalently coupled to methoxypoly(ethyene glycol) succinate N-hydroxysuccinimide ester
0.442
L-asparagine
-
Vmax: 0.0699 mM/min, 37°C, pH not specified in the publication
1.1
L-asparagine
-
pH 8.0, 37°C, recombinant AspMP, L-asparaginase II without signal peptide
3.25
L-asparagine
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant F162L; pH 8.0, temperature not specified in the publication, ASPGB1 mutant S189T
4.11
L-asparagine
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant N184D
4.23
L-asparagine
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant S189A
4.53
L-asparagine
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant N184A
4.72
L-asparagine
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant S189C
5.12
L-asparagine
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant F162W
6.83
L-asparagine
-
pH 8.0, temperature not specified in the publication, wild-type ASPGB1
10.5
L-asparagine
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant N184Q
10.7
L-asparagine
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant R165T
12.7
L-asparagine
-
pH 8.0, temperature not specified in the publication, ASPGA1 mutant L163F
14.3
L-asparagine
-
pH 8.0, temperature not specified in the publication, ASPGA1 mutant T166R
14.7
L-asparagine
-
pH 8.0, temperature not specified in the publication, wild-type ASPGA1
0.05
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme G57V; pH 7.0, 25°C, mutant enzyme G88I
1.8