3.5.1.1: asparaginase
This is an abbreviated version!
For detailed information about asparaginase, go to the full flat file.
Word Map on EC 3.5.1.1
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3.5.1.1
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leukemia
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lymphoblastic
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children
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remission
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erwinia
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hypersensitivity
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methotrexate
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lymphoma
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vincristine
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pegylated
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relapse
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pancreatitis
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thrombosis
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prednisone
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high-dose
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venous
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oncology
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event-free
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schedule
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cytarabine
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consolidation
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intensification
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antileukemic
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intrathecal
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antithrombin
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l-aspartic
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chrysanthemi
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anthracyclines
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medicine
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reinduction
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cyclophosphamide
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pegaspargase
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thromboembolism
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allergy
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acrylamide
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arabinoside
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mercaptopurine
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daunorubicin
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osteonecrosis
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analysis
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philadelphia
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extranodal
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fried
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b-precursor
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succinogenes
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standard-risk
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synthesis
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coli-derived
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food industry
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diagnostics
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biotechnology
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dana-farber
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pharmacology
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teniposide
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carotovora
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multiagent
- 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
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multiagent
Reaction
Synonyms
14270 ASNase, alpha-asparaginase, AnsA, ansA3, AnsB, ansZ, Asn, ASNase, ASNase1, ASNase3, ASP1, ASP3, asparaginase, asparaginase II, asparagine amidohydrolase, asparginase II, ASPG, ASPG II, ASPGA1, ASPGB1, ASRGL1, At3g16150, colaspase, crasnitin, DiAsp, EcAII, EcAIII, EcaL-ASNase, ECAR-LANS, elspar, ErA, Erwinase, glutaminase-free L-asparaginase, glutamine-(asparagin-)ase, HPA, L-ASNase, L-asparaginase, L-asparaginase 2, L-asparaginase I, L-asparaginase II, L-asparaginase III, L-asparaginase type II, L-asparaginase type III, L-asparaginase-I, L-asparaginase-II, L-asparagine amidohydrolase, L-asparagine amino hydrolase, L-asparagine aminohydrolase, leunase, PfA, PhA, potassium-dependent asparaginase, potassium-independent asparaginase, potassium-independent L-asparaginase, SAMN05216263_10744, SGR ASNase, type I L-asparaginase, type II L-asparaginase, Ypa
ECTree
3.5.1.1 asparaginaseAdvanced search results
results (
results (KM Value
KM Value on EC 3.5.1.1 - asparaginase
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
2.38
beta-Asp-His
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pH 8.0, temperature not specified in the publication, wild-type ASPGB1
2.9
beta-Asp-His
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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
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pH 8.0, temperature not specified in the publication, ASPGB1 mutant N184Q
3.56
beta-Asp-His
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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
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pH 8.0, temperature not specified in the publication, ASPGB1 mutant S189T
6.79
beta-Asp-His
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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
0.0009
L-asparagine
KC573069
pH not specified in the publication, temperature not specified in the publication
0.021
L-asparagine
K0.5 value, Hill coefficient 1.4, presence of 0.3 mM Gln, pH 8.0, 37°C
0.0217
L-asparagine
wild-type, 37°C, pH not specified in the publication
0.0236
L-asparagine
mutant S121P, 37°C, pH not specified in the publication
0.025
L-asparagine
K0.5 value, Hill coefficient 1.4, presence of 0.9 mM Gln, pH 8.0, 37°C
0.03
L-asparagine
wild-type, pH not specified in the publication, temperature not specified in the publication
0.03
L-asparagine
mutant N24S, pH not specified in the publication, temperature not specified in the publication
0.068
L-asparagine
K0.5 value, Hill coefficient 1.0, presence of 8 mM Gln, pH 8.0, 37°C
0.122
L-asparagine
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presence of L-glutamine, K0.5 value, pH 8.8, 37°C
0.16
L-asparagine
-
pH 8.0, 37°C, recombinant AspSP, L-asparaginase II with signal peptide
0.18
L-asparagine
-
pH not specified in the publication, temperature not specified in the publication
0.23
L-asparagine
mutant M121C/T169M, cooperative kinetic toward L-Asn, Hill coefficient 1.7, pH 7.5, 37°C
0.25
L-asparagine
mutant M121C, cooperative kinetic toward L-Asn, Hill coefficient 1.5, pH 7.5, 37°C
0.25
L-asparagine
mutant T169M, cooperative kinetic toward L-Asn, Hill coefficient 1.8, pH 7.5, 37°C
0.36
L-asparagine
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37°C, mutant enzyme R206H covalently coupled to methoxypoly(ethyene glycol) succinate N-hydroxysuccinimide ester
0.442
L-asparagine
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Vmax: 0.0699 mM/min, 37°C, pH not specified in the publication
1.1
L-asparagine
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pH 8.0, 37°C, recombinant AspMP, L-asparaginase II without signal peptide
2.1
L-asparagine
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mutant S180N/D289T/E260F/E292S, pH not specified in the publication, 37°C
3.25
L-asparagine
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant F162L
3.25
L-asparagine
-
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
7.02
L-asparagine
-
pH not specified in the publication, temperature not specified in the publication
10.5
L-asparagine
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pH 8.0, temperature not specified in the publication, ASPGB1 mutant N184Q
10.7
L-asparagine
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pH 8.0, temperature not specified in the publication, ASPGB1 mutant R165T
12.7
L-asparagine
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pH 8.0, temperature not specified in the publication, ASPGA1 mutant L163F
14.3
L-asparagine
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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
0.32
L-glutamine
mutant S121P, 37°C, pH not specified in the publication
0.38
L-glutamine
wild-type, 37°C, pH not specified in the publication
2.6
L-glutamine
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pH 8.0, 37°C, recombinant AspSP, L-asparaginase II with signal peptide
3.95
L-glutamine
wild-type, pH not specified in the publication, temperature not specified in the publication
4.14
L-glutamine
mutant N24S, pH not specified in the publication, temperature not specified in the publication
4.4
L-glutamine
-
pH 8.0, 37°C, recombinant AspMP, L-asparaginase II without signal peptide
46.4
L-glutamine
wild-type, cooperative kinetic toward L-Gln, Hill coefficient 2.0, pH 7.5, 37°C
76.5
L-glutamine
mutant Q63E, cooperative kinetic toward L-Gln, Hill coefficient 2.3, pH 7.5, 37°C
additional information
L-asparagine
kcat/Km: 66.41 1/mM*s, pH7.5, 37°C
additional information
L-glutamine
kcat/Km: 0.48 1/mM*s, pH7.5, 37°C
additional information
additional information
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the Km of the immobilized enzyme is 8fold lower compared to the free enzyme
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additional information
additional information
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thermodynamic analysis, kinetic study and molecular modelling
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additional information
additional information
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thermodynamics, overview
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additional information
additional information
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Michaelis-Menten steady-state kinetics, overview
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additional information
additional information
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kinetic parameters of wild-type and chimeric ASPGA1 and -B1, overview
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additional information
additional information
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Lineweaver-Burk and Michaelis-Menten kinetic analysis of activity, overview. Thiol compounds reduce the Km and increase the Vmax vlaues
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additional information
additional information
steady-state enzyme kinetics at different conditions of wild-type and mutant enzymes, overview
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additional information
additional information
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steady-state enzyme kinetics at different conditions of wild-type and mutant enzymes, overview
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