BRENDA home
History
Information on EC 3.5.1.1 - asparaginase
for references in articles please use BRENDA:EC3.5.1.1Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.5.1.1 asparaginaseSpecify your search results
Word Map
- 3.5.1.1
- leukemia
- lymphoblastic
- children
-
remission
- erwinia
- hypersensitivity
- methotrexate
- lymphoma
- vincristine
-
pegylated
-
relapse
- pancreatitis
- thrombosis
- prednisone
-
high-dose
- venous
-
oncology
-
event-free
-
schedule
- cytarabine
-
consolidation
-
intensification
-
antileukemic
-
intrathecal
- antithrombin
-
l-aspartic
- chrysanthemi
- anthracyclines
- medicine
-
reinduction
- cyclophosphamide
-
pegaspargase
- thromboembolism
- allergy
- acrylamide
-
arabinoside
- mercaptopurine
- daunorubicin
- osteonecrosis
- analysis
-
philadelphia
-
extranodal
-
fried
-
b-precursor
- succinogenes
-
standard-risk
- synthesis
-
coli-derived
- food industry
- diagnostics
- biotechnology
-
dana-farber
- pharmacology
- teniposide
- carotovora
-
multiagent
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
14270 ASNase, alpha-asparaginase, AnsA, ansA3, AnsB, ansZ, Asn, ASNase, ASNase1, ASNase3, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
14270 ASNase
alpha-asparaginase
-
-
-
-
AnsA
ansA3
AnsB
ansZ
Asn
ASNase
ASNase1
ASNase3
ASP1
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
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-asparagine + H2O = L-aspartate + NH3
-
-
-
-
L-asparagine + H2O = L-aspartate + NH3
active site structure involving Thr193, autocatalytic activation mechanism involving Thr193
-
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
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
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylic acid amide hydrolysis
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
KEGG
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
L-asparagine amidohydrolase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9015-68-3
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
?
N-acetyl-L-asparagine + H2O
N-acetyl-L-aspartic acid + NH3
-
-
-
?
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-acetyl-L-asparagine + H2O
Nalpha-acetyl-L-aspartate + NH3
-
-
-
-
?
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-Asn + H2O
L-Asp + NH3
-
-
-
-
?
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
strongly preferred substrate
-
-
?
L-asparagine + H2O
L-aspartate + NH3
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-aspartate + NH3
-
-
-
?
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
reaction of EC 3.5.1.2
-
-
?
L-glutamine + H2O
L-glutamate + NH3
reaction of EC 3.5.1.2
-
-
?
L-glutamine + H2O
L-glutamate + NH3
reaction of EC 3.5.1.2
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
reaction of EC 3.5.1.2
-
-
?
L-glutamine + H2O
L-glutamate + NH3
negligible activity
-
-
?
L-glutamine + H2O
L-glutamate + NH3
reaction of EC 3.5.1.2
-
-
?
L-glutamine + H2O
L-glutamate + NH3
reaction of EC 3.5.1.2
-
-
?
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
?
-
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
?
-
-
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
?
-
enzyme exhibits strict substrate specificity towards L-asparagine, with trace activity towards L-glutamine
-
-
?
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
?
-
-
no substrate: D-asparagine, beta-alanine amide
-
-
?
additional information
?
-
-
poor substrates: D-asparagine, L-aspartic acid, and L-glutamic acid. No substrate: L-glutamine
-
-
?
additional information
?
-
poor or no substrates: D-asparagine, L-glutamine, D-glutamine, L-histidine, L-ornithine, Boc-L-asapragine, N-alpha-acetyl-L-asparagine, urea, acrylamide
-
-
?
additional information
?
-
-
poor or no substrates: D-asparagine, L-glutamine, D-glutamine, L-histidine, L-ornithine, Boc-L-asapragine, N-alpha-acetyl-L-asparagine, urea, acrylamide
-
-
?
additional information
?
-
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
?
-
-
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
?
-
the activity against L-glutamine, reaction of EC 3.5.1.2, corresponds to 2.2% of the activity against L-asparagine
-
-
?
additional information
?
-
-
the activity against L-glutamine, reaction of EC 3.5.1.2, corresponds to 2.2% of the activity against L-asparagine
-
-
?
additional information
?
-
-
very poor substrate: L-glutamine
-
-
?
additional information
?
-
-
less than 0.5% of the activity with L-asparagine: L-glutamine, D-asparagine, D-glutamine
-
-
?
additional information
?
-
-
less than 0.5% of the activity with L-asparagine: L-glutamine, D-asparagine, D-glutamine
-
-
?
additional information
?
-
-
antiproliferating activity on the breast cancer cell lines T47D, BT20, and MCF-7
-
-
?
additional information
?
-
-
no activity with D-asparagine as substrate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
strongly preferred substrate
-
-
?
L-asparagine + H2O
L-aspartate + NH3
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-aspartate + NH3
-
-
-
?
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-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
-
-
?
additional information
?
-
-
the enzyme shows anti-leukemic activity
-
-
?
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 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
?
-
to become enzymatically active, ASNase3 must undergo autocleavage between residues Gly167 and Thr168
-
-
?
additional information
?
-
-
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
Zn2+
1 mM, 109% of initial activity, 5 mM, 86% of initial activity
additional information
-
potassium-independent L-asparaginase (AtA), Arabidopsis thaliana potassium-dependent L-asparaginase (AtAK)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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+
1 mM, 109% of initial activity, 5 mM, 86% of initial activity
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
albumin