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Enzyme Nomenclature
Information on EC 3.5.1.1 - asparaginase
for references in articles please use BRENDA:EC3.5.1.1
Word Map on EC 3.5.1.1
- 3.5.1.1
- leukemia
- lymphoblastic
- children
-
childhood
-
remission
- vincristine
-
pediatric
-
regimen
- erwinia
- lymphoma
- methotrexate
-
relapse
- thrombosis
- prednisone
-
pharmacokinetics
- hypersensitivity
-
intrathecal
-
high-dose
-
schedule
- cytarabine
- cyclophosphamide
-
consolidation
-
event-free
-
intensification
-
pegylated
-
oncology
-
arabinoside
- mercaptopurine
- daunorubicin
-
cranial
-
antithrombin
- l-glutamine
- chrysanthemi
- medicine
- allergy
- carotovora
-
l-aspartic
- anthracyclines
- thromboembolism
-
reinduction
- osteonecrosis
-
dana-farber
-
b-precursor
-
extranodal
-
coli-derived
- pharmacology
- succinogenes
- analysis
-
b-lineage
-
antileukaemic
-
standard-risk
- synthesis
- diagnostics
- teniposide
- biotechnology
-
multiagent
- food industry
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Specify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
3.5.1.1
-
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RECOMMENDED NAME
GeneOntology No.
asparaginase
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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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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylic acid amide hydrolysis
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
comprehensive comparison shows that the Asparagus officinalis A7 variety has the highest asparaginase activity, while A1 has the lowest, regardless of the tissue type
-
-
L-asparaginase cultivated in the presence of the oxygen vectors liquid paraffin, silicone oil, and n-dodecane
-
-
Erwinia aroidea
highest yield in aerobically grown cells in corn steep medium, addition of L-glutamic acid, L-methionine, and lactic acid enhances enzyme production, addition of glucose or sodium depresses enzyme production
-
-
marine actinomycetes, soil isolate S1, S2, S3, S4, S5, S6, S8. K2, K4, K5, and K8, whereof S3, S4 and S6 are designated as Streptomyces spp.
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out of the 40 strains isolated, six strains (LA-2, LA-8, LA-15, LA-20, LA29 and LA-35) show significant activity
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Enterobacteriaceae, bacterium isolated from cow dung, gene ansB
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-
potassium-independent asparaginase ASPGA1, and potassium-dependent asparaginase ASPGB1
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-
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208939, 208944, 208953, 208963, 208966, 654031, 654088, 657311, 667907, 668053, 668077, 669496, 669734, 670217, 684147, 686454, 686619, 688355, 688561, 695591, 696592, 699167, 699417, 701277, 711845, 714599
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highest yield in aerobically grown cells in corn steep medium, addition of L-glutamic acid, L-methionine, and lactic acid enhances enzyme production, addition of glucose or sodium depresses enzyme production
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208939, 208949, 208953, 655078, 667091, 669556, 684146, 684973, 686239, 686244, 687060, 695841, 697899, 711172, 720205, 720400, 733045
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recombinant protein, using the Pichia pastoris expression system
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various cultivars: Kareem 7, Dokki 331, Kafer El-Sheikh 1, Kaha 1, and Fodder
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme is a member of an increasing rhizobial-type family of L-asparaginases
metabolism
-
L-asparaginase is degraded by leukemic lysosomal cysteine proteases
physiological function
additional information
physiological function
-
the cytotoxic activity of L-asparaginase from Yersinia pseudotuberculosis and Erwinia carotovora are investigated and compared in vitro using human T-lymphoblastic leukemia (Jurkat and Molt-4 cells) and also solid tumor cell lines MCF-7 (human breast adenocarcinoma), LnCap (human prostate carcinoma), NGUK1 (ratGasser node neurinoma). The data obtained indicate that the Yersinia pseudotuberculosis L-asparaginase significantly inhibits growth of leukemic and solid tumor cells. Comparing effectiveness of L-asparaginases from various sources one can see that L-asparaginase from Yersinia pseudotuberculosis exhibits higher activity in suppression of tumor cell growth than the enzyme from Erwinia carotovora
physiological function
-
the cytotoxic activity of L-asparaginase from Yersinia pseudotuberculosis and Erwinia carotovora are investigated and compared in vitro using human T-lymphoblastic leukemia (Jurkat and Molt-4 cells) and also solid tumor cell lines MCF-7 (human breast adenocarcinoma), LnCap (human prostate carcinoma), NGUK1 (ratGasser node neurinoma). The data obtained indicate that the Yersinia pseudotuberculosis L-asparaginase significantly inhibits growth of leukemic and solid tumor cells. Comparing effectiveness of L-asparaginases from various sources one can see that L-asparaginase from Yersinia pseudotuberculosis exhibits higher activity in suppression of tumor cell growth than the enzyme from Erwinia carotovora
physiological function
-
amino acid starvation by asparaginase enhances phosphorylation of eukaryotic initiation factor 2, eIF2 by general control nonderepressible 2 kinase GCN2, leading to reduced global mRNA translation rates. GCN2+/+ and GCN2-/-2 mice are injected once daily with asparaginase or saline for up to 7 d. In both thymus and spleen, activation of amino acid stress response genes to asparaginase, such as asparagine synthetase and CAAT enhancer binding protein homologous protein, requires GCN2. Asparaginase reduces food intake and body weight in both genotypes, but spleen and thymus wet weights and total cell numbers in thymus, spleen, bone marrow, and mesenteric lymph nodes are less in GCN2-/- mice treated with asparaginase. In the thymus, GCN2-/- mice treated with asparaginase demonstrate enhanced apoptosis and fewer cells in all subpopulations examined compared with GCN2+/+ mice treated with asparaginase. In the spleen, GCN2 deletion magnifies asparaginase-induced reductions in CD4+ T cells, CD8+ T cells, CD19+ B cells, and CD11b+ leukocytes
physiological function
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Helicobacter pylori L-asparaginase is able to inhibit the cell-cycle of fibroblasts and gastric cell lines. Interference with cell-cycle in vitro depends on cell genotype and is related to the expression levels of the concurrent enzyme asparagine synthetase
physiological function
-
antiproliferative effect of YpA in vitro and in vivo, overview
physiological function
-
antiproliferative effect of YpA in vitro and in vivo, overview
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additional information
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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. Structure-function analysis of active site residues T53 and K274
additional information
-
a divergent sequence between the two enzymes forms a variable loop at the C-terminal of the alpha subunit, the asparaginase variable loop plays a role in the determination of substrate preference in plants. The variable loop itself spans positions 169-182 of ASPGA1 and 168-194 of ASPGB1, dynamic simulations and comparative protein structure modeling based on the crystal structure of Lupinus luteus LlA, PDB accession number 2GEZ, overview
additional information
-
ASNase3 is not the enzyme responsible for the antitumor effects of guinea pig serum
additional information
H0VQC8
ASNase3 is not the enzyme responsible for the antitumor effects of guinea pig serum
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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
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-
?
L-asparagine + H2O
L-aspartate + NH3
-
the enzyme does not reduce alpha-antiplasmin and plasminogen levels in human patients with acute lymphoblastic leukemia
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-
?
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
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-
?
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-aspartic acid + NH3
-
specificity: free from L-glutaminase activity
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-
?
L-asparagine + H2O
L-aspartic acid + NH3
-
specificity: free from L-glutaminase activity
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-
?
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
?
-
-
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
?
-
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 SUBSTRATES
NATURAL PRODUCTS
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
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-
-
additional information
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-
no activity with D-asparagine monohydrate and L-glutamic acid
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-
-
additional information
?
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R4L284
no activity with D-asparagine monohydrate and L-glutamic acid
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-
-
additional information
?
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-
no activity with D-glutamine, L-aspartic acid, D-aspartic acid, L-glutamic acid, and ornathine
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-
-
additional information
?
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R4L284
no activity with D-asparagine monohydrate and L-glutamic acid
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-
-
additional information
?
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-
the enzyme requires autocleavage to become active
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-
-
additional information
?
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H0VQC8
the enzyme requires autocleavage to become active
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-
-
additional information
?
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residues 195RKH197 are critical for enzyme antigenicity
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-
-
additional information
?
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L-asparaginase from Escherichia coli is more immuno-depressive and immunotoxic than that from Erwinia carotovora
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-
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additional information
?
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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
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-
-
additional information
?
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Q7L266
to become enzymatically active, ASNase3 must undergo autocleavage between residues Gly167 and Thr168
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-
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additional information
?
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L-asparaginase from Escherichia coli is more immuno-depressive and immunotoxic than that from Erwinia carotovora
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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
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potassium-independent L-asparaginase (AtA), Arabidopsis thaliana potassium-dependent L-asparaginase (AtAK)
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Glutaraldehyde
-
inhibits the enzyme during immobilization at concentrations above 0.2%
N-ethoxycarbonyl-2-ethoxy-1,2-dihydroquinone
-
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
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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
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urea and EDTA do not reveal any inhibitory effects on enzyme activity
-
additional information
urea and EDTA do not reveal any inhibitory effects on enzyme activity
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