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acrylamide + H2O
acrylic acid + NH3
-
-
-
-
?
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-asparagine + H2O
D-aspartate + NH3
D-aspartic acid beta-hydroxamate + H2O
D-Asp + hydroxylamine
-
59% of the activity with L-Asn
-
-
?
D-glutamine + H2O
D-glutamate + NH3
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
?
DL-aspartyl hydroxamate + H2O
DL-Asp + hydroxylamine
Gly-D-Asn + H2O
Gly-D-Asp + NH3
-
-
-
?
Gly-L-Asn + H2O
Gly-L-Asp + NH3
-
-
-
?
L-asparagine + H2O
?
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
L-asparagine + H2O
L-aspartic acid + NH3
L-aspartic acid beta-hydrazide + H2O
L-Asp + hydroxylamine
-
2% of the activity with L-Asn
-
-
?
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
-
-
-
?
L-Glu-L-Asn + H2O
L-Glu-L-Asp + NH3
-
-
-
?
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-glutamine + H2O
L-glutamate + NH3
L-glutamine + H2O
L-glutamic acid + NH3
L-glutamyl hydroxamate + H2O
L-glutamate + hydroxylamine
-
16% relative activity compared to L-asparagine as substrate
-
-
?
L-leucine amide + H2O
?
-
5.3% of the activity with L-Asn
-
-
?
L-phenylalanine amide + H2O
?
-
8.2% of the activity with L-Asn
-
-
?
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-Asn + H2O
Nalpha-acetyl-L-Asp + NH3
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
-
-
?
poly-L-asparagine + H2O
?
succinamic acid + H2O
?
-
at 20% of the activity with L-Asn
-
-
?
succinamic acid + H2O
pentanedioic acid + NH3
-
-
-
-
?
succinamic acid + H2O
succinate + NH3
threo-3-hydroxy-L-asparagine + H2O
?
-
36% of the activity with L-Asn
-
-
?
urea + H2O
? + NH3
-
-
-
-
?
additional information
?
-
beta-cyano-L-Ala + H2O

?
-
-
-
-
?
beta-cyano-L-Ala + H2O
?
-
beta-cyano-L-Ala
-
-
?
beta-cyano-L-Ala + H2O
?
-
-
-
-
?
beta-cyano-L-Ala + H2O
?
-
beta-cyano-L-Ala
-
-
?
beta-cyano-L-Ala + H2O
?
-
at 2.4% of the activity with L-Asn
-
-
?
beta-cyano-L-Ala + H2O
?
-
beta-cyano-L-Ala
-
-
?
beta-cyano-L-Ala + H2O
?
-
at 2.4% of the activity with L-Asn
-
-
?
beta-cyano-L-Ala + H2O
?
-
-
-
-
?
beta-cyano-L-Ala + H2O
?
-
beta-cyano-L-Ala
-
-
?
beta-cyano-L-Ala + H2O
?
-
at 5.7% of the activity with L-Asn
-
-
?
beta-cyano-L-Ala + H2O
?
-
9.5% of the activity with L-Asn
-
-
?
beta-cyano-L-Ala + H2O
?
-
9.5% of the activity with L-Asn
-
-
?
beta-L-Asp-L-Phe + H2O

?
-
-
-
-
?
beta-L-Asp-L-Phe + H2O
?
-
-
-
?
D-Asn + H2O

D-Asp + NH3
-
30% of the activity with L-Asn
-
-
?
D-Asn + H2O
D-Asp + NH3
-
at 5% of the activity with L-Asn
-
-
?
D-Asn + H2O
D-Asp + NH3
-
-
-
-
?
D-Asn + H2O
D-Asp + NH3
-
11.5% of the activity with L-Asn
-
-
?
D-Asn + H2O
D-Asp + NH3
-
-
-
-
?
D-Asn + H2O
D-Asp + NH3
-
3% of the activity with L-Asn
-
-
?
D-Asn + H2O
D-Asp + NH3
-
-
-
-
?
D-Asn + H2O
D-Asp + NH3
-
-
-
-
?
D-Asn + H2O
D-Asp + NH3
-
at 5% of the activity with L-Asn
-
-
?
D-Asn + H2O
D-Asp + NH3
-
2% of the activity with D-Asn
-
-
?
D-Asn + H2O
D-Asp + NH3
-
at 5% of the activity with L-Asn
-
-
?
D-Asn + H2O
D-Asp + NH3
-
no activity
-
-
?
D-Asn + H2O
D-Asp + NH3
-
no activity
-
-
?
D-Asn + H2O
D-Asp + NH3
-
-
-
-
?
D-Asn + H2O
D-Asp + NH3
-
at 5% of the activity with L-Asn
-
-
?
D-Asn + H2O
D-Asp + NH3
-
-
-
-
?
D-Asn + H2O
D-Asp + NH3
-
10% of the activity with L-Asn
-
-
?
D-Asn + H2O
D-Asp + NH3
-
6.5% 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
-
-
?
D-asparagine + H2O
D-aspartate + NH3
negligible activity
-
-
?
D-asparagine + H2O
D-aspartate + NH3
-
-
-
?
D-asparagine + H2O
D-aspartate + NH3
-
-
-
?
D-glutamine + H2O

D-glutamate + NH3
-
-
-
?
D-glutamine + H2O
D-glutamate + NH3
-
-
-
?
DL-aspartyl hydroxamate + H2O

DL-Asp + hydroxylamine
-
66% of the activity with L-Asn
-
-
?
DL-aspartyl hydroxamate + H2O
DL-Asp + hydroxylamine
-
-
-
-
?
DL-aspartyl hydroxamate + H2O
DL-Asp + hydroxylamine
-
-
-
-
?
L-Asn + H2O

L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
Azotobacter agilis
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
Chlamydomonas sp.
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
Erwinia aroidea
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
Erwinia aroidea NRRL B-138
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
constitutive enzyme
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
constitutive enzyme
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
Salmonella typhosa
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-asparagine + H2O

L-aspartate + NH3
KC573069
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
KC573069
-
-
-
?
L-asparagine + H2O
L-aspartate + 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
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
100% activity
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
highly specific substrate
-
-
?
L-asparagine + H2O
L-aspartate + NH3
100% activity
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
?
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
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
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
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
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
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
strongly preferred substrate
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
strongly preferred substrate
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
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
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
specific for
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
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
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
100% activity
-
-
?
L-asparagine + H2O
L-aspartate + NH3
100% activity
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
best substrate
-
-
?
L-asparagine + H2O
L-aspartate + NH3
best substrate
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
?
L-asparagine + H2O

L-aspartic acid + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartic acid + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartic acid + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartic acid + NH3
-
-
-
?
L-asparagine + H2O
L-aspartic acid + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartic acid + NH3
-
-
-
?
L-asparagine + H2O
L-aspartic acid + NH3
-
-
-
?
L-asparagine + H2O
L-aspartic acid + NH3
-
-
-
?
L-asparagine + H2O
L-aspartic acid + 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-asparagine + H2O
L-aspartic acid + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartic acid + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartic acid + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartic acid + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartic acid + 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-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
-
-
-
?
L-aspartyl hydroxamate + H2O
L-aspartate + hydroxylamine
-
60% relative activity compared to L-asparagine as substrate
-
-
?
L-aspartyl-beta-hydroxamate + H2O

L-Asp + hydroxylamine
-
-
-
-
?
L-aspartyl-beta-hydroxamate + H2O
L-Asp + hydroxylamine
-
-
-
-
?
L-Gln + H2O

L-Glu + NH3
-
-
-
-
?
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
-
-
-
?
L-Gln + H2O
L-Glu + NH3
-
-
-
?
L-Gln + H2O
L-Glu + NH3
-
-
-
-
?
L-Gln + H2O
L-Glu + NH3
-
at 4% of the activity with L-asparagine
-
-
?
L-Gln + H2O
L-Glu + NH3
-
at 4% of the activity with L-asparagine
-
-
?
L-Gln + H2O
L-Glu + NH3
-
no activity
-
-
?
L-Gln + H2O
L-Glu + NH3
-
no activity
-
-
?
L-Gln + H2O
L-Glu + NH3
-
no activity
-
-
?
L-Gln + H2O
L-Glu + NH3
-
-
-
-
?
L-Gln + H2O
L-Glu + NH3
-
at 9% of the activity with L-Asn
-
-
?
L-Gln + H2O
L-Glu + NH3
-
-
-
-
?
L-Gln + H2O
L-Glu + NH3
-
2% of the activity with L-Asn
-
-
?
L-Gln + H2O
L-Glu + NH3
-
-
-
-
?
L-Gln + H2O
L-Glu + NH3
-
-
-
-
?
L-Gln + H2O
L-Glu + NH3
-
-
-
-
?
L-Gln + H2O
L-Glu + NH3
-
-
-
-
?
L-Gln + H2O
L-Glu + NH3
-
not hydrolyzed at significant rate
-
-
?
L-glutamine + H2O

?
58.2% activity compared to 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
-
-
-
-
?
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
-
-
-
-
?
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
negligible activity
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
reaction of EC 3.5.1.2
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
?
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
-
-
?
L-glutamine + H2O

L-glutamic acid + NH3
-
-
-
?
L-glutamine + H2O
L-glutamic acid + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamic acid + NH3
-
-
-
?
L-glutamine + H2O
L-glutamic acid + NH3
-
-
-
?
L-glutamine + H2O
L-glutamic acid + NH3
-
-
-
?
L-glutamine + H2O
L-glutamic acid + NH3
-
-
-
?
L-glutamine + H2O
L-glutamic acid + NH3
-
-
-
?
L-glutamine + H2O
L-glutamic acid + NH3
-
-
-
-
?
Nalpha-acetyl-L-Asn + H2O

Nalpha-acetyl-L-Asp + NH3
-
-
-
?
Nalpha-acetyl-L-Asn + H2O
Nalpha-acetyl-L-Asp + NH3
-
-
-
?
poly-L-asparagine + H2O

?
-
at 21.7% of the activity with L-Asn
-
-
?
poly-L-asparagine + H2O
?
-
at 21.7% of the activity with L-Asn
-
-
?
succinamic acid + H2O

succinate + NH3
-
-
-
?
succinamic acid + H2O
succinate + NH3
-
-
-
?
additional information

?
-
-
the enzyme shows anti-leukemic activity
-
-
?
additional information
?
-
-
the enzyme shows anti-leukemic activity
-
-
?
additional information
?
-
not active with N-acetylglucosaminyl-L-Asn
-
-
?
additional information
?
-
-
L-glutamine is a poor substrate
-
-
?
additional information
?
-
-
L-glutamine is a poor substrate
-
-
?
additional information
?
-
-
no substrate: L-glutamine
-
-
?
additional information
?
-
-
no substrate: L-glutamine
-
-
?
additional information
?
-
-
enzyme has no antitumor 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 recombinant enzyme shows low affinity to L-glutamine
-
-
?
additional information
?
-
-
the recombinant enzyme shows low affinity to L-glutamine
-
-
?
additional information
?
-
-
enzyme has antitumor activity
-
-
?
additional information
?
-
-
the enzyme requires autocleavage to become active
-
-
?
additional information
?
-
the enzyme lacks L-glutaminase activity
-
-
?
additional information
?
-
Erwinia aroidea
-
enzyme has antitumor activity
-
-
?
additional information
?
-
-
does not hydrolyse L-glutamine
-
-
?
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
?
-
-
enzyme has antitumor activity
-
-
?
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
?
-
-
enzyme has no antitumor activity
-
-
?
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
?
-
-
enzyme has antitumor activity
-
-
?
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
?
-
-
enzyme has antitumor activity
-
-
?
additional information
?
-
-
enzyme has antitumor activity
-
-
?
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
?
-
-
very poor substrate: L-glutamine
-
-
?
additional information
?
-
-
enzyme has antitumor activity
-
-
?
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
?
-
-
protein kinase activity
-
-
?
additional information
?
-
-
no L-glutaminase activity
-
-
?
additional information
?
-
-
no activity with D-asparagine as substrate
-
-
?
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diphosphate
-
stimulation
EDTA
-
inhibits enzyme, 1, 3, and 10 mM tested
Fe2+
about 203.7% activity at 10 mM
KCl
the catalytic activity of YpA does not vary significantly as a function of ionic strength at 100-3000 mM KCl
Li+
-
rapid and reversible activation
Ni2+
-
5 mM, 37°C, 136% relative activity compared to the activity in absence of metal cations
Pb2+
-
stimulates activity
PO43-
-
enhances activity
Rb+
monovalent cation preference in order of decreasing efficiency is: K+, Na+, Rb+
Triton X-100
-
2 mM, 114% of initial activity
Ca2+

-
slight stimulation
Ca2+
-
10 mM, 110% of initial activity
Ca2+
144% activity at 2 mM
Ca2+
-
5 mM, 40-45% activation of L-asparaginase I and II
Co2+

about 263.9% activity at 10 mM
Co2+
-
5 mM, 37°C, 134% relative activity compared to the activity in absence of metal cations
Cu2+

-
2 mM, 114% of initial activity
Cu2+
about 109.3% activity at 10 mM
Cu2+
-
inhibits enzyme, 1, 3, and 10 mM tested
Fe3+

-
stimulates activity
Fe3+
145.97% activity at 1 mM
Fe3+
1 mM, 117% of initial activity
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+
-
rapid and reversible activation
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
K+
123.41% activity at 1 mM
K+
-
activates 133% at 1 mM
K+
-
10 mM, 150% of initial activity
K+
150 mM, about 130% of initial activity
Mg2+

-
stimulates
Mg2+
slightly increased activity at 5 mM
Mg2+
-
2 mM, 116% of initial activity
Mg2+
5 mM, 2fold activation
Mg2+
-
5 mM, 122% of initial activity
Mg2+
-
1 mM, 149% of initial activity
Mg2+
marginal increase in enzyme activity in the presence of 1 mM Mg2+ (less than 15%)
Mg2+
138% activity at 1 mM
Mn2+

-
activation
Mn2+
slightly increased activity at 5 mM
Mn2+
-
2 mM, 112% of initial activity
Mn2+
183% activity at 2 mM
Mn2+
-
activates enzyme, 1, 3, and 10 mM tested
Na+

monovalent cation preference in order of decreasing efficiency is: K+, Na+, Rb+
Na+
-
rapid and reversible activation
Na+
-
activates at 100 mM
Na+
slightly increased activity at 5 mM
Na+
-
probably, metal binding loop structure involving Leu59, Glu60, Ile62, Phe65, Ala67, and Ile69, overview
Na+
-
maximal activity at 2% NaCl
Na+
128.21% activity at 1 mM
Na+
-
activates 117% at 1 mM
Na+
-
10 mM, 110% of initial activity
Na+
-
2 mM, 113% of initial activity
Na+
50 mM, about 115% of initial activity
Zn2+

contains zinc
Zn2+
1 mM, 109% of initial activity, 5 mM, 86% of initial activity
Zn2+
-
inhibits enzyme, 1, 3, and 10 mM tested
additional information

-
potassium-independent L-asparaginase (AtA), Arabidopsis thaliana potassium-dependent L-asparaginase (AtAK)
additional information
-
enzyme is not a metalloprotein
additional information
not influenced by K+
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2-amino-5-chloro-4-oxo pentanoic acid
-
-
4-chloromercuribenzoate
-
complete inhibition at 0.5 mM
4-methylene-L-glutamine
-
-
4-phenylbutanoic acid
-
more than 80% residual activity at 10 mM
5-Bromo-4-oxo-L-norvaline
-
-
5-Diazo-4-oxo-L-norvaline
6-diazo-5-oxo-L-norleucine
-
-
beta-aspartyl hydroxamate
48% inhibition at 5 mM
cyclo-(Pro-Phe)
21% inhibition at 0.02 mM
cyclo-(Pro-Tyr)
21% inhibition at 0.002 mM
D-asparagine
39% inhibition at 5 mM
DL-aspartate 3-hydroxamate
-
-
DL-aspartyl hydroxamate
-
-
Glutaraldehyde
-
inhibits the enzyme during immobilization at concentrations above 0.2%
H2O2
-
76% inhibition at 1.0 mM
L-Asn
-
inhibits hydrolysis of diazo-4-oxo-L-norvaline
L-asparagine
-
substrate inhibition above 20 mM L-asparagine
L-aspartate
-
competitive
L-glutamate
-
competitive
Lactate
-
about 70% inhibition at 10 mM
Li+
KC573069
10 mM, 17% residual activity
N-bromosuccinimide
-
1 mM, 5% inhibition
N-ethoxycarbonyl-2-ethoxy-1,2-dihydroquinline
-
no effect up to 1 mM: Mg2+, Mn2+ and Ca2+
N4-hydroxyethyl-L-asparagine
-
-
O-(diazoacetyl)-L-serine
-
-
oxylate
-
about 70% inhibition at 10 mM
p-chloromercuribenzoic acid
-
-
Phenylglyoxal
-
protection by substrate
phenylmethylsulfonyl fluoride
-
more than 80% residual activity at 10 mM
potassium ferricyanide
-
-
Sodium azide
-
1 mM, 15% inhibition
Thiourea
1 mM, about 85% residual activtiy
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
-
2-mercaptoethanol

-
strongest inhibition
2-mercaptoethanol
complete inhibition at 2 mM
2-mercaptoethanol
1 mM, 31.3% residual activity
2-mercaptoethanol
-
1 mM, 10% inhibition
2-mercaptoethanol
55% residual activity at 2 mM
2-mercaptoethanol
55% residual activity
3-Cyano-L-Ala

-
-
5-Diazo-4-oxo-L-norvaline

-
-
5-Diazo-4-oxo-L-norvaline
-
inhibits L-asparaginase activity and affects broth culture filtrate inhibition of the cell cycle
5-Diazo-4-oxo-L-norvaline
-
-
5-Diazo-4-oxo-L-norvaline
-
-
Ag+

42% residual activity at 2 mM
Ag+
2 mM, 42% residual activity
aspartic acid

-
-
aspartic acid
competitive
Ba2+

KC573069
10 mM, 12% residual activity
Ba2+
30% residual activity at 2 mM
Ba2+
2 mM, 30% residual activity
Ba2+
-
5 mM, 37°C, 25% relative activity compared to the activity in absence of metal cations
Ca2+

KC573069
10 mM, 28% residual activity
Ca2+
about 70% residual activity at 5 mM
Ca2+
-
25 mM, 26% loss of activity
Ca2+
23.69% residual activity at 1 mM
Ca2+
-
22% inhibition at 1.0 mM
Ca2+
-
10 mM, 16.5% of initial activity
Ca2+
-
2 mM, 64% of initial activity
Ca2+
150 mM, about 75% of initial activity
Ca2+
31% inhibition at 1 mM
Ca2+
-
10 mM, 90% residual activity
Ca2+
80% residual activity at 1 mM
Cd2+

-
-
Cd2+
complete inhibition at 1 mM
Cd2+
-
complete inhibition at 1.0 mM
Cd2+
10 mM, loss of activity
Co2+

-
-
Co2+
91.24% residual activity at 1 mM
Co2+
-
10 mM, 35.6% of initial activity
Co2+
-
2 mM, 67% of initial activity
Co2+
-
1 mM, 53 inhibition
Co2+
69% residual activity at 2 mM
Co2+
2 mM, 69% residual activity
Co2+
complete inhibition at 1 mM
Cr2+

37% residual activity at 2 mM
Cr2+
2 mM, 37% residual activity
Cu2+

-
-
Cu2+
KC573069
10 mM, 23% residual activity
Cu2+
-
20 mM, 44% inhibition
Cu2+
complete inhibition at 1 mM
Cu2+
1 mM, no residual activity
Cu2+
-
complete inhibition at 1.0 mM
Cu2+
-
10 mM, 22.3% of initial activity
Cu2+
-
1 mM, 47inhibition
Cu2+
13% residual activity at 2 mM
Cu2+
2 mM, 13% residual activity
Cu2+
-
10 mM, 92% residual activity
Cu2+
15% residual activity at 1 mM
cysteine

complete inhibition at 1 mM
cysteine
-
1 mM, 13% inhibition
D-Asn

-
-
D-Asn
-
competitive, reverses antiproliferating effect on breast cancer cells
dithiothreitol

-
-
dithiothreitol
-
14% inhibition at 0.5 mM
EDTA

less than 60% residual activity at 5 mM
EDTA
-
30% residual activity at 10 mM
EDTA
1 mM, 13.9% residual activity
EDTA
-
3 mM, 45.8% residual activity
EDTA
-
10 mM, 62% residual activity
EDTA
-
1 mM, 19% inhibition
EDTA
5 mM, about 85% residual activity
EDTA
24% residual activity
EDTA
90% residual activity at 1 mM
Fe2+

KC573069
10 mM, 44% residual activity
Fe2+
-
10 mM, 13.3% of initial activity
Fe2+
-
5 mM, 82% of initial activity
Fe3+

less than 60% residual activity at 5 mM
Fe3+
-
53% inhibition at 1.0 mM
Fe3+
-
3 mM, 50.3% residual activity
Fe3+
100 mM, about 55% of initial activity
Fe3+
41% residual activity at 2 mM
Fe3+
2 mM, 41% residual activity
Hg2+

-
-
Hg2+
KC573069
10 mM, 33% residual activity
Hg2+
complete inhibition at 5 mM
Hg2+
-
1 mM, 80% loss of activity. 3 mM, complete inhibition
Hg2+
complete inhibition at 1 mM
Hg2+
1 mM, no residual activity
Hg2+
-
complete inhibition at 1.0 mM
Hg2+
-
3 mM, no residual activity
Hg2+
-
10 mM, 33% residual activity
Hg2+
-
10 mM, 23% of initial activity
Hg2+
-
2 mM, 2% of initial activity
Hg2+
100 mM, loss of activity
Hg2+
24% residual activity at 2 mM
Hg2+
2 mM, 24% residual activity
Hg2+
-
5 mM, 37°C, 20% relative activity compared to the activity in absence of metal cations
iodoacetamide

-
-
iodoacetamide
complete inhibition at 1 mM
iodoacetamide
-
complete inhibition at 0.5 mM
iodoacetamide
-
1 mM, 20% inhibition
iodoacetamide
-
at pH 6.0 protection by substrate, at pH 8.0 no protection by substrate
K+

less than 60% residual activity at 5 mM
K+
-
2 mM, 69% of initial activity
K+
92% residual activity at 2 mM
L-Asp

-
-
L-Asp
-
product inhibition at pH 8.5
Mg2+

-
-
Mg2+
29.47% residual activity at 1 mM
Mg2+
-
76% inhibition at 1.0 mM
Mg2+
-
10 mM, 3.3% of initial activity
Mg2+
40 mM, about 30% of initial activity
Mg2+
31% inhibition at 1 mM
Mg2+
28% residual activity at 2 mM
Mg2+
2 mM, 28% residual activity
Mg2+
about 25% residual activity at 10 mM
Mn2+

-
-
Mn2+
-
20 mM, 50% inhibition
Mn2+
31.56% residual activity at 1 mM
Mn2+
-
29% inhibition at 1.0 mM
Mn2+
-
3 mM, 60.4% residual activity
Mn2+
-
10 mM, 20.5% of initial activity
Mn2+
100 mM, about 75% of initial activity
Mn2+
52% inhibition at 1 mM
Mn2+
-
5 mM, 37°C, 42% relative activity compared to the activity in absence of metal cations
Na+

-
-
Na+
91% residual activity at 2 mM
NaCl

-
-
NH4+

-
-
NH4+
-
product inhibition at pH 8.5
Ni2+

-
-
Ni2+
about 85% residual activity at 5 mM
Ni2+
-
49% inhibition at 1.0 mM
Ni2+
10 mM, loss of activity
Ni2+
85% residual activity at 2 mM
Ni2+
about 90% residual activity at 10 mM
Ni2+
complete inhibition at 1 mM
p-chloromercuribenzoate

-
-
p-chloromercuribenzoate
-
-
p-hydroxymercuribenzoate

-
-
p-hydroxymercuribenzoate
-
-
Pb2+

-
1 mM, 59inhibition
PCMB

-
reversed by mercaptoethanol
PMSF

-
1 mM, 63% inhibition
PMSF
-
partial inactivation
pyruvate

-
about 70% inhibition at 10 mM
pyruvate
-
10 mM, 26% inhibition
SDS

-
-
SDS
33.21% residual activity at 2% (w/v)
SDS
-
78% inhibition at 3.0 mM, 119% activation at 1.0 mM
SDS
-
2 mM, 3.1% of initial activity
SDS
-
2 mM, 30% of initial activity
SDS
2 mM, about 55% residual activity
SDS
56% residual activity at 2 mM
SDS
56% residual activity
SDS
-
10 mM, 30% residual activity
Sn2+

-
-
Sn2+
87% residual activity at 2 mM
Urea

less than 60% residual activity at 5 mM
Urea
-
30% residual activity at 10 mM
Urea
-
1 mM, 13% inhibition
Zn2+

KC573069
10 mM, 34% residual activity
Zn2+
-
25 mM, 25% inhibition
Zn2+
10.43% residual activity at 1 mM
Zn2+
1 mM, 40.1% residual activity
Zn2+
-
94% inhibition at 1.0 mM
Zn2+
-
2 mM, 19% of initial activity
Zn2+
1 mM, 109% of initial activity, 5 mM, 86% of initial activity
Zn2+
-
5 mM, 72% of initial activity
Zn2+
-
1 mM, 54inhibition
Zn2+
100 mM, about 60% of initial activity
Zn2+
38% inhibition at 1 mM
Zn2+
17% residual activity at 2 mM
Zn2+
2 mM, 17% residual activity
Zn2+
about 90% residual activity at 10 mM
Zn2+
-
40% inhibition by 0.5 mM, 60% inhibition by 1.0 mM
Zn2+
-
5 mM, 37°C, 36% relative activity compared to the activity in absence of metal cations
additional information

KC573069
not inhibitory: EDTA at 1-50 mM
-
additional information
-
not inhibitory: high NaCl conditions
-
additional information
-
not inhibitory: high NaCl conditions
-
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
-
additional information
poor inhibition by L-glutamine at 5 mM
-
additional information
-
poor inhibition by L-glutamine at 5 mM
-
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