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Synonyms
asparaginase, l-asnase, asrgl1, asparaginase ii, l-asparaginase ii, erwinase, ecaii, l-asparaginase i, ecaiii, diasp,
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alpha-asparaginase
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asparagine amidohydrolase
ASPG II
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three forms, ASPG I, ASPG II, and ASPG III. ASPG II shows the highest specific activity
glutaminase-free L-asparaginase
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glutamine-(asparagin-)ase
L-asparaginase type III
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L-asparagine amidohydrolase
L-asparagine amino hydrolase
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L-asparagine aminohydrolase
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potassium-dependent asparaginase
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potassium-independent asparaginase
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potassium-independent L-asparaginase
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type I L-asparaginase
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14270 ASNase
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AnsA
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ansA3
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AnsB
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ansZ
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Asn
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ASNase
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ASNase1
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ASNase3
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ASP1
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asparaginase
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asparaginase II
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asparagine amidohydrolase
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asparagine amidohydrolase
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ErA
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glutamine-(asparagin-)ase
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glutamine-(asparagin-)ase
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HPA
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HPA
Helicobacter pylori L-asparaginase
L-ASNase
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L-asparaginase
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L-asparaginase II
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L-asparaginase III
isoform
L-asparaginase III
isoform
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L-asparagine amidohydrolase
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L-asparagine amidohydrolase
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L-asparagine amidohydrolase
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L-asparagine amidohydrolase
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L-asparagine amidohydrolase
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L-asparagine amidohydrolase
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L-asparagine amidohydrolase
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L-asparagine amidohydrolase
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L-asparagine amidohydrolase
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L-asparagine amidohydrolase
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SGR ASNase
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type II L-asparaginase
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type II L-asparaginase
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Ypa
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L-asparagine + H2O = L-aspartate + NH3
L-asparagine + H2O = L-aspartate + NH3
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L-asparagine + H2O = L-aspartate + NH3
active site structure involving Thr193, autocatalytic activation mechanism involving Thr193
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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
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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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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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acrylamide + H2O
acrylic acid + NH3
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?
benzyloxycarbonyl-Gly-L-Asn + H2O
benzyloxycarbonyl-Gly-L-Asp
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?
beta-Asp-His + H2O
?
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substrate of ASPGA1 and ASPGB1, ASPGA1 has a 4fold substrate preference for beta-Asp-His over Asn
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?
beta-aspartoethylamide + H2O
?
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at 0.4% of the activity with L-Asn
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?
beta-aspartomethylamide + H2O
L-Asp + ethylamine
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at 0.5% of the activity with L-Asn
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?
beta-aspartopropylamide + H2O
?
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at 0.7% of the activity with L-Asn
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?
D-asparagine + H2O
D-aspartate + NH3
D-aspartic acid beta-hydroxamate + H2O
D-Asp + hydroxylamine
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59% of the activity with L-Asn
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?
D-glutamine + H2O
D-glutamate + NH3
diazo-4-oxo-L-norvaline + H2O
5-hydroxy-4-oxo-L-norvaline + NH3
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?
DL-Ala-DL-Asn + H2O
DL-Ala-DL-Asn + DL-Ala-DL-Asp
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75% Ala-Asp + 25% Ala-Asn
?
DL-aspartyl hydroxamate + H2O
DL-Asp + hydroxylamine
Gly-D-Asn + H2O
Gly-D-Asp + NH3
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?
Gly-L-Asn + H2O
Gly-L-Asp + NH3
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?
L-asparagine + H2O
?
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?
L-asparagine + H2O
L-aspartate + NH3
L-asparagine + H2O
L-aspartic acid + NH3
L-aspartic acid beta-hydrazide + H2O
L-Asp + hydroxylamine
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2% of the activity with L-Asn
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?
L-aspartic acid beta-hydroxamate + H2O
L-Asp + hydroxylamine
L-aspartyl hydroxamate + H2O
L-aspartate + hydroxylamine
L-aspartyl-beta-hydroxamate + H2O
L-Asp + hydroxylamine
L-Gln-L-Asn + H2O
L-Gln-L-Asp + NH3
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?
L-Glu-L-Asn + H2O
L-Glu-L-Asp + NH3
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?
L-glutamic acid gamma-hydroxamate + H2O
L-Glu + hydroxylamine
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1% of the activity with L-Asn
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?
L-glutamine + H2O
L-glutamate + NH3
L-glutamine + H2O
L-glutamic acid + NH3
L-glutamyl hydroxamate + H2O
L-glutamate + hydroxylamine
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16% relative activity compared to L-asparagine as substrate
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?
L-leucine amide + H2O
?
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5.3% of the activity with L-Asn
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?
L-phenylalanine amide + H2O
?
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8.2% of the activity with L-Asn
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?
N-acetyl-L-asparagine + H2O
N-acetyl-L-aspartic acid + NH3
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?
N4-ethyl-L-asparagine
L-Asp + propylamine
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12% of the activity with L-Asn
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?
N4-methoxy-L-asparagine + H2O
L-Asp + O-methylhydroxylamine
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154% of the activity with L-Asn
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?
N4-methyl-L-asparagine
L-Asp + methylamine
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12% of the activity with L-Asn
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?
Nalpha-acetyl-L-Asn + H2O
Nalpha-acetyl-L-Asp + NH3
Nalpha-acetyl-L-asparagine + H2O
Nalpha-acetyl-L-aspartate + NH3
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?
Nalpha-methyl-L-Asn + H2O
Nalpha-methyl-L-Asp + NH3
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26% of the activity with L-Asn
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?
poly-L-asparagine + H2O
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succinamic acid + H2O
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at 20% of the activity with L-Asn
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?
succinamic acid + H2O
succinate + NH3
threo-3-hydroxy-L-asparagine + H2O
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36% of the activity with L-Asn
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?
urea + H2O
? + NH3
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?
additional information
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beta-cyano-L-Ala + H2O
?
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?
beta-cyano-L-Ala + H2O
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beta-cyano-L-Ala
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?
beta-cyano-L-Ala + H2O
?
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?
beta-cyano-L-Ala + H2O
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beta-cyano-L-Ala
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?
beta-cyano-L-Ala + H2O
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at 2.4% of the activity with L-Asn
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?
beta-cyano-L-Ala + H2O
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beta-cyano-L-Ala
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?
beta-cyano-L-Ala + H2O
?
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at 2.4% of the activity with L-Asn
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?
beta-cyano-L-Ala + H2O
?
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?
beta-cyano-L-Ala + H2O
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beta-cyano-L-Ala
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?
beta-cyano-L-Ala + H2O
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at 5.7% of the activity with L-Asn
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?
beta-cyano-L-Ala + H2O
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9.5% of the activity with L-Asn
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?
beta-cyano-L-Ala + H2O
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9.5% of the activity with L-Asn
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?
beta-L-Asp-L-Phe + H2O
?
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?
beta-L-Asp-L-Phe + H2O
?
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?
D-Asn + H2O
D-Asp + NH3
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30% of the activity with L-Asn
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?
D-Asn + H2O
D-Asp + NH3
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at 5% of the activity with L-Asn
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?
D-Asn + H2O
D-Asp + NH3
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?
D-Asn + H2O
D-Asp + NH3
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3% of the activity with L-Asn
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?
D-Asn + H2O
D-Asp + NH3
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?
D-Asn + H2O
D-Asp + NH3
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?
D-Asn + H2O
D-Asp + NH3
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at 5% of the activity with L-Asn
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?
D-Asn + H2O
D-Asp + NH3
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2% of the activity with D-Asn
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?
D-Asn + H2O
D-Asp + NH3
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at 5% of the activity with L-Asn
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?
D-Asn + H2O
D-Asp + NH3
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no activity
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?
D-Asn + H2O
D-Asp + NH3
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no activity
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?
D-Asn + H2O
D-Asp + NH3
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?
D-Asn + H2O
D-Asp + NH3
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at 5% of the activity with L-Asn
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?
D-Asn + H2O
D-Asp + NH3
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?
D-Asn + H2O
D-Asp + NH3
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10% of the activity with L-Asn
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?
D-Asn + H2O
D-Asp + NH3
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?
D-Asn + H2O
D-Asp + NH3
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11.5% of the activity with L-Asn
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?
D-Asn + H2O
D-Asp + NH3
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6.5% of the activity with L-Asn
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?
D-asparagine + H2O
D-aspartate + NH3
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catalytic activity of the recombinant enzyme for L-asparagine is 5fold higher than for D-asparagine
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?
D-asparagine + H2O
D-aspartate + NH3
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less than 10% activity compared to L-asparagine
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?
D-asparagine + H2O
D-aspartate + NH3
negligible activity
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?
D-asparagine + H2O
D-aspartate + NH3
negligible activity
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?
3.5.1.1 asparaginase
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