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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 + 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
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
-
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
-
-
-
-
?
D-Asn + H2O
D-Asp + NH3
-
11.5% 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
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-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
-
36% relative activity compared to L-asparagine as substrate
-
-
?
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
-
-
-
?
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
?
-
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
-
-
?
additional information
?
-
-
enzyme has no antitumor activity
-
-
?
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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+
-
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
K+
-
rapid and reversible activation
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+
-
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
Na+
-
rapid and reversible activation
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+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.12 - 0.41
beta-L-Asp-L-Phe
77.6
D-glutamine
at pH 8.5 and 85°C
0.0095
diazo-4-oxo-L-norvaline
-
-
0.0009 - 110
L-asparagine
0.011 - 1.9
L-aspartyl-beta-hydroxamate
0.597 - 5.613
N-acetyl-L-asparagine
0.8
Nalpha-acetyl-Asn
pH 8, 37°C
0.5
Nalpha-acetyl-L-asparagine
-
pH 8.0, 25°C
0.3 - 18.8
succinamic acid
additional information
L-asparagine
0.0048
Asn
-
-
0.015
Asn
-
pH 7.0, 25°C, wild-type enzyme
0.095
Asn
-
pH 7.0, 25°C, mutant enzyme N248A
2.38
beta-Asp-His
-
pH 8.0, temperature not specified in the publication, wild-type ASPGB1
2.9
beta-Asp-His
-
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
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant N184Q
3.56
beta-Asp-His
-
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
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant S189T
6.79
beta-Asp-His
-
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
0.12
beta-L-Asp-L-Phe
wild type enzyme, at pH 7.5 and 37°C
0.41
beta-L-Asp-L-Phe
-
at pH 7.5 and 37°C
0.43
D-Asn
-
-
1.2
D-asparagine
-
pH 9.2, 70°C, recombinant enzyme
1.8
D-asparagine
-
pH 9.2, 37°C, recombinant enzyme
24.1
D-asparagine
at pH 8.5 and 85°C
0.0058
Gln
-
-
0.00016
L-Asn
-
37°C
3
L-Asn
Erwinia aroidea
-
-
4.1
L-Asn
-
asparaginase I and II
6.2
L-Asn
-
L-asparaginase 2
7.4
L-Asn
-
L-asparaginase 1
0.0009
L-asparagine
KC573069
pH not specified in the publication, temperature not specified in the publication
0.005
L-asparagine
-
pH 9.2, 70°C, recombinant enzyme
0.01
L-asparagine
-
pH 8.6, 37°C
0.014
L-asparagine
-
in 50 mM Tris-HCl buffer (pH 8.6), at 37°C
0.015
L-asparagine
Chlamydomonas sp.
-
enzyme AG
0.017
L-asparagine
pH 8.0, 37°C
0.018
L-asparagine
K0.5 value, Hill coefficient 1.5, pH 8.0, 37°C
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
0.024
L-asparagine
-
pH 8.6, 37°C
0.025
L-asparagine
K0.5 value, Hill coefficient 1.4, presence of 0.9 mM Gln, pH 8.0, 37°C
0.0291
L-asparagine
-
pH 8.6, 37°C, mutant enzyme N41D
0.0291
L-asparagine
-
pH 8.6, 37°C, wild-type enzyme
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
0.038
L-asparagine
mutant D133T
0.0562
L-asparagine
-
pH 8.6, 37°C, mutant enzyme N41D/N281D
0.0577
L-asparagine
at pH 7.5 and 37°C
0.058
L-asparagine
pH 8, 37°C
0.0597
L-asparagine
-
pH 8.6, 37°C, mutant enzyme N281D
0.068
L-asparagine
K0.5 value, Hill coefficient 1.0, presence of 8 mM Gln, pH 8.0, 37°C
0.07
L-asparagine
-
pH 8.0, 25°C
0.075
L-asparagine
-
K0.5 value, pH 8.8, 37°C
0.08
L-asparagine
-
pH 9.2, 37°C, recombinant enzyme
0.097
L-asparagine
mutant D133I
0.098
L-asparagine
-
pH 8.5, 37°C
0.1
L-asparagine
mutant Q63E, pH 7.5, 37°C
0.122
L-asparagine
-
presence of L-glutamine, K0.5 value, pH 8.8, 37°C
0.127
L-asparagine
at pH 8.0 and 37°C
0.133
L-asparagine
pH 7.0, 45°C
0.134
L-asparagine
Chlamydomonas sp.
-
-
0.147
L-asparagine
-
pH 9.0, 37°C
0.153
L-asparagine
mutant D133V
0.16
L-asparagine
mutant D133L
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
0.2
L-asparagine
-
37°C, pH 8.5
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
0.29
L-asparagine
wild-type, pH 7.5, 37°C
0.3
L-asparagine
-
pH 8.0, 37°C
0.3
L-asparagine
pH 8.0, 45°C
0.35
L-asparagine
-
enzyme I
0.36
L-asparagine
-
37°C, mutant enzyme R206H covalently coupled to methoxypoly(ethyene glycol) succinate N-hydroxysuccinimide ester
0.43
L-asparagine
-
at pH 7.5 and 40°C
0.442
L-asparagine
-
Vmax: 0.0699 mM/min, 37°C, pH not specified in the publication
0.55
L-asparagine
-
37°C, mutant enzyme R206H
0.671
L-asparagine
at 37°C and pH 8.0
0.74
L-asparagine
-
enzyme I
0.89
L-asparagine
-
pH 7.0, 37°C, recombinant enzyme
1
L-asparagine
Chlamydomonas sp.
-
enzyme A
1.1
L-asparagine
-
pH 7.0, 37°C
1.1
L-asparagine
-
pH 8.0, 37°C, recombinant AspMP, L-asparaginase II without signal peptide
1.25
L-asparagine
-
pH 8.0, 37°C
1.41
L-asparagine
-
pH 8.0, 40°C
2.09
L-asparagine
wild type enzyme, at pH 7.5 and 37°C
2.1
L-asparagine
-
pH 8.0, 40°C
2.1
L-asparagine
pH 8.2, 80°C, mutant K274E
2.1
L-asparagine
-
mutant S180N/D289T/E260F/E292S, pH not specified in the publication, 37°C
2.2
L-asparagine
at pH 8.6 and 37°C
2.24
L-asparagine
-
at pH 7.5 and 37°C
2.6
L-asparagine
at pH 8.0 and 90°C
3.2
L-asparagine
-
mutant E292S, pH not specified in the publication, 37°C
3.2 - 3.7
L-asparagine
-
-
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
3.3
L-asparagine
-
pH 7.2, 37°C
3.6
L-asparagine
pH 8.5, 45°C
3.7
L-asparagine
-
mutant E260F, pH not specified in the publication, 37°C
3.9
L-asparagine
-
mutant D289T, pH not specified in the publication, 37°C
3.9
L-asparagine
-
mutant S180N, pH not specified in the publication, 37°C
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
4.3
L-asparagine
pH 7.4, 37°C, mutant K274E
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
L-asparagine
-
wild-type, pH not specified in the publication, 37°C
5.1
L-asparagine
-
37°C, pH 8.0, mutant enzyme D178P
5.12
L-asparagine
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant F162W
5.3
L-asparagine
-
37°C, pH 8.0, wild-type enzyme
5.41
L-asparagine
pH 7.4, 37°C, mutant T53Q/K274E
6.4
L-asparagine
-
pH 8.0, 37°C
6.72
L-asparagine
-
pH 8.0, 37°C
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
7.2
L-asparagine
-
pH 7.5, 37°C
7.52
L-asparagine
pH 7.4, 37°C, mutant T53Q
8.12
L-asparagine
pH 7.4, 37°C, wild-type enzyme
8.2
L-asparagine
pH 8.2, 80°C, mutant T53Q/K274E
8.3
L-asparagine
pH 8.2, 80°C, mutant T53Q
8.9
L-asparagine
pH 7.5, 37°C, recombinant enzyme
10
L-asparagine
at pH 8.5 and 85°C
10.5
L-asparagine
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant N184Q
10.7
L-asparagine
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant R165T
12.1
L-asparagine
pH 8.2, 80°C, wild-type enzyme
12.7
L-asparagine
-
pH 8.0, temperature not specified in the publication, ASPGA1 mutant L163F
14.3
L-asparagine
-
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
21.6
L-asparagine
-
mutant V26A/E30G/D181G/V245G/G276D, pH 8.0, 40°C
23.8
L-asparagine
-
pH 7.2, 37°C
26.1
L-asparagine
-
mutant V26A/E30G/K122N/G276D, pH 8.0, 40°C
28.6
L-asparagine
-
wild-type, pH 8.0, 40°C
63.3
L-asparagine
37°C, pH 7.5
100
L-asparagine
-
at pH 6.3 and 30°C
110
L-asparagine
-
pH 6.3, 28°C
0.011
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme V27L
0.015
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme V27M
0.035
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, wild-type enzyme
0.037
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme Q59E
0.04
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme G88A
0.05
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme G57V
0.05
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme G88I
0.056
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme N248D
0.069
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme G57A
0.07
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme G11V
0.082
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme G57L
0.13
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme G11L
0.14
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme N248W
0.15
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme N248Q
0.19
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme N248A
0.21
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme N248G
0.442
L-aspartyl-beta-hydroxamate
-
37°C
1.8
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme Q59G
1.9
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme Q59A
0.005
L-Gln
-
-
0.035
L-Gln
-
pH 7.0, 25°C, wild-type enzyme
2 - 3
L-Gln
-
pH 7.0, 25°C, mutant enzyme Q59E
2.4
L-Gln
-
pH 7.0, 25°C, mutant enzyme G57V
3.5
L-Gln
-
pH 7.0, 25°C, mutant enzyme N248D
4
L-Gln
-
pH 7.0, 25°C, mutant enzyme V27M
4.4
L-Gln
-
pH 7.0, 25°C, mutant enzyme V27L
5.7
L-Gln
-
pH 7.0, 25°C, mutant enzyme G57A
6
L-Gln
-
pH 7.0, 25°C, mutant enzyme N248G
10
L-Gln
-
pH 7.0, 25°C, mutant enzyme Q59A
16
L-Gln
-
pH 7.0, 25°C, mutant enzyme N248A
21
L-Gln
-
pH 7.0, 25°C, mutant enzyme N248Q
50
L-Gln
-
pH 7.0, 25°C, mutant enzyme Q59G
70
L-Gln
-
pH 7.0, 25°C, mutant enzyme N248E
0.2
L-glutamine
-
pH 9.2, 70°C, recombinant enzyme
0.32
L-glutamine
mutant S121P, 37°C, pH not specified in the publication
0.35
L-glutamine
-
pH 9.2, 37°C, recombinant enzyme
0.38
L-glutamine
wild-type, 37°C, pH not specified in the publication
1.008
L-glutamine
mutant D133T
1.099
L-glutamine
mutant D133I
1.6
L-glutamine
K0.5 value, Hill coefficient 1.1, pH 8.0, 37°C
1.677
L-glutamine
mutant D133L
1.999
L-glutamine
mutant D133V
2.6
L-glutamine
-
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
5.2
L-glutamine
-
pH 8.0, 25°C
39.5
L-glutamine
at pH 8.5 and 85°C
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
0.597
N-acetyl-L-asparagine
mutant D133V
1.788
N-acetyl-L-asparagine
mutant D133L
2.096
N-acetyl-L-asparagine
mutant D133T
5.613
N-acetyl-L-asparagine
mutant D133I
0.3
succinamic acid
-
pH 8.0, 25°C
18.8
succinamic acid
pH 8, 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
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetics
-
additional information
additional information
kinetics
-
additional information
additional information
-
the Km of the immobilized enzyme is 8fold lower compared to the free enzyme
-
additional information
additional information
-
thermodynamic analysis, kinetic study and molecular modelling
-
additional information
additional information
-
thermodynamics, overview
-
additional information
additional information
-
Michaelis-Menten steady-state kinetics, overview
-
additional information
additional information
-
kinetic parameters of wild-type and chimeric ASPGA1 and -B1, overview
-
additional information
additional information
-
Lineweaver-Burk and Michaelis-Menten kinetic analysis of activity, overview. Thiol compounds reduce the Km and increase the Vmax vlaues
-
additional information
additional information
steady-state enzyme kinetics at different conditions of wild-type and mutant enzymes, overview
-
additional information
additional information
-
steady-state enzyme kinetics at different conditions of wild-type and mutant enzymes, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.8 - 1.98
beta-L-Asp-L-Phe
3378
D-asparagine
at pH 8.5 and 85°C
1362
D-glutamine
at pH 8.5 and 85°C
0.0027 - 5721
L-asparagine
0.004 - 450
L-aspartyl-beta-hydroxamate
0.0108
Nalpha-acetyl-Asn
pH 8, 37°C
4.1
Nalpha-acetyl-L-asparagine
-
pH 8.0, 25°C
0.0239 - 4.1
succinamic acid
additional information
additional information
-
turnover numbers for L-aspartyl-beta-hydroxamate with mutant enzyme G11L and G88I are below 0.01 per sec
-
7
Asn
-
pH 7.0, 25°C, mutant enzyme N248A
24
Asn
-
pH 7.0, 25°C, wild-type enzyme
0.8
beta-L-Asp-L-Phe
wild type enzyme, at pH 7.5 and 37°C
1.98
beta-L-Asp-L-Phe
-
at pH 7.5 and 37°C
0.0027
L-asparagine
-
37°C, pH 8.0, wild-type enzyme and mutant enzyme D178P
0.0128
L-asparagine
pH 8, 37°C
0.025
L-asparagine
pH 7.0, 45°C
0.22
L-asparagine
pH 8.0, 37°C
1.62
L-asparagine
-
wild-type, pH 8.0, 40°C
3.19
L-asparagine
wild type enzyme, at pH 7.5 and 37°C
3.95
L-asparagine
-
at pH 7.5 and 37°C
4.65
L-asparagine
at pH 8.6 and 37°C
4.83
L-asparagine
mutant enzyme M121C, at pH 7.5 and 37°C
4.83
L-asparagine
mutant M121C, pH 7.5, 37°C
6.53
L-asparagine
mutant enzyme Q63E, at pH 7.5 and 37°C
6.53
L-asparagine
mutant Q63E, pH 7.5, 37°C
7.4
L-asparagine
mutant enzyme T169M, at pH 7.5 and 37°C
7.4
L-asparagine
mutant T169M, pH 7.5, 37°C
13.95
L-asparagine
mutant enzyme M121C/T169M, at pH 7.5 and 37°C
13.95
L-asparagine
mutant M121C/T169M, pH 7.5, 37°C
17.98
L-asparagine
pH 7.4, 37°C, wild-type enzyme
19.2
L-asparagine
wild-type, pH 7.5, 37°C
19.26
L-asparagine
wild type enzyme, at pH 7.5 and 37°C
23.8
L-asparagine
pH 7.4, 37°C, mutant T53Q/K274E
24.5
L-asparagine
-
mutant S180N/D289T/E260F/E292S, pH not specified in the publication, 37°C
24.9
L-asparagine
pH 7.4, 37°C, mutant K274E
32.2
L-asparagine
-
mutant E260F, pH not specified in the publication, 37°C
34.5
L-asparagine
-
mutant E292S, pH not specified in the publication, 37°C
35.2
L-asparagine
pH 7.4, 37°C, mutant T53Q
36.8
L-asparagine
at 37°C and pH 8.0
38.6
L-asparagine
at pH 7.5 and 37°C
43.2
L-asparagine
-
mutant D289T, pH not specified in the publication, 37°C
47.9
L-asparagine
-
mutant S180N, pH not specified in the publication, 37°C
48
L-asparagine
presence of 8 mM Gln, pH 8.0, 37°C
48.5
L-asparagine
-
wild-type, pH not specified in the publication, 37°C
52.8
L-asparagine
-
mutant V26A/E30G/D181G/V245G/G276D, pH 8.0, 40°C
55.2
L-asparagine
-
pH 8.0, 25°C
57.7
L-asparagine
-
mutant V26A/E30G/K122N/G276D, pH 8.0, 40°C
58.8
L-asparagine
mutant N24S, pH not specified in the publication, temperature not specified in the publication
59.8
L-asparagine
wild-type, pH not specified in the publication, temperature not specified in the publication
60
L-asparagine
pH 8.0, 37°C
67
L-asparagine
presence of 0.9 mM Gln, pH 8.0, 37°C
72
L-asparagine
presence of 0.3 mM Gln, pH 8.0, 37°C
86.7
L-asparagine
mutant S121P, 37°C, pH not specified in the publication
97.8
L-asparagine
wild-type, 37°C, pH not specified in the publication
106
L-asparagine
pH 7.5, 37°C, recombinant enzyme
160
L-asparagine
-
pH 8.0, 37°C, recombinant AspMP, L-asparaginase II without signal peptide
160
L-asparagine
-
pH 8.0, 37°C, recombinant AspSP, L-asparaginase II with signal peptide
199.2
L-asparagine
pH 8.2, 80°C, mutant K274E
217
L-asparagine
-
K0.5 value, pH 8.8, 37°C
246.7
L-asparagine
pH 8.2, 80°C, mutant T53Q
277.9
L-asparagine
pH 8.2, 80°C, mutant T53Q/K274E
286.3
L-asparagine
-
pH 8.0, 37°C
523
L-asparagine
-
presence of L-glutamine, K0.5 value, pH 8.8, 37°C
565
L-asparagine
-
pH 8.6, 37°C, wild-type enzyme
573
L-asparagine
-
pH 8.6, 37°C, mutant enzyme N281D
657
L-asparagine
-
pH 8.6, 37°C, mutant enzyme N41D
676
L-asparagine
at pH 7.0 and 45°C
694
L-asparagine
at pH 8.0 and 90°C
798
L-asparagine
-
pH 8.6, 37°C, mutant enzyme N41D/N281D
888.6
L-asparagine
pH 8.2, 80°C, wild-type enzyme
2680
L-asparagine
-
in 50 mM Tris-HCl buffer (pH 8.6), at 37°C
4424
L-asparagine
-
pH 7.0, 37°C
5721
L-asparagine
at pH 8.5 and 85°C
0.004
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme G88A
0.11
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme G11V
0.143
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme Q59G
0.2
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme G57L
0.46
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme N248D
0.86
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme G57V
2
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme Q59E
9.7
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme Q59A
10.3
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme V27L
10.8
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme V27M
15.4
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme G57A
21
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme N248Q
23
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme N248G
26
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme N248W
27
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme N248A
29
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, wild-type enzyme
450
L-aspartyl-beta-hydroxamate
-
37°C
0.001
L-Gln
-
pH 7.0, 25°C, mutant enzyme Q59A
0.0024
L-Gln
-
pH 7.0, 25°C, mutant enzyme Q59E
0.0029
L-Gln
-
pH 7.0, 25°C, mutant enzyme N248A
0.0043
L-Gln
pH 8.2, 37°C
0.0046
L-Gln
-
pH 7.0, 25°C, mutant enzyme N248G
0.006
L-Gln
-
pH 7.0, 25°C, mutant enzyme G57V
0.0068
L-Gln
-
pH 7.0, 25°C, mutant enzyme N248D
0.01
L-Gln
-
pH 7.0, 25°C, mutant enzyme G57A
0.01
L-Gln
-
pH 7.0, 25°C, mutant enzyme Q59G
0.019
L-Gln
-
pH 7.0, 25°C, mutant enzyme N248E
0.032
L-Gln
-
pH 7.0, 25°C, mutant enzyme N248Q
0.032
L-Gln
-
pH 7.0, 25°C, mutant enzyme V27M
0.091
L-Gln
-
pH 7.0, 25°C, mutant enzyme V27L
0.33
L-Gln
-
pH 7.0, 25°C, wild-type enzyme
0.42
L-glutamine
-
pH 8.0, 25°C
0.51
L-glutamine
wild-type, pH not specified in the publication, temperature not specified in the publication
0.53
L-glutamine
mutant N24S, pH not specified in the publication, temperature not specified in the publication
1.58
L-glutamine
wild-type, 37°C, pH not specified in the publication
2.1
L-glutamine
wild-type, pH 7.5, 37°C
2.2
L-glutamine
pH 8.0, 37°C
6
L-glutamine
-
pH 8.0, 37°C, recombinant AspSP, L-asparaginase II with signal peptide
7.1
L-glutamine
-
pH 8.0, 37°C, recombinant AspMP, L-asparaginase II without signal peptide
11.33
L-glutamine
mutant S121P, 37°C, pH not specified in the publication
14.5
L-glutamine
mutant enzyme Q63E, at pH 7.5 and 37°C
14.5
L-glutamine
mutant Q63E, pH 7.5, 37°C
22.1
L-glutamine
wild type enzyme, at pH 7.5 and 37°C
2048
L-glutamine
at pH 8.5 and 85°C
0.0239
succinamic acid
pH 8, 37°C
4.1
succinamic acid
-
pH 8.0, 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4.83 - 6.66
beta-L-Asp-L-Phe
140.2
D-asparagine
at pH 8.5 and 85°C
17.6
D-glutamine
at pH 8.5 and 85°C
0.055 - 22580
L-asparagine
8.2
Nalpha-acetyl-L-asparagine
-
pH 8.0, 25°C
13.7
succinamic acid
-
pH 8.0, 25°C
4.83
beta-L-Asp-L-Phe
-
at pH 7.5 and 37°C
6.66
beta-L-Asp-L-Phe
wild type enzyme, at pH 7.5 and 37°C
0.055
L-asparagine
-
wild-type, pH 8.0, 40°C
1.52
L-asparagine
wild type enzyme, at pH 7.5 and 37°C
1.76
L-asparagine
-
at pH 7.5 and 37°C
2.21
L-asparagine
-
mutant V26A/E30G/K122N/G276D, pH 8.0, 40°C
2.44
L-asparagine
-
mutant V26A/E30G/D181G/V245G/G276D, pH 8.0, 40°C
8.6
L-asparagine
-
mutant E260F, pH not specified in the publication, 37°C
9.7
L-asparagine
-
wild-type, pH not specified in the publication, 37°C
10.9
L-asparagine
-
mutant E292S, pH not specified in the publication, 37°C
11.1
L-asparagine
-
mutant D289T, pH not specified in the publication, 37°C
11.9
L-asparagine
-
mutant S180N/D289T/E260F/E292S, pH not specified in the publication, 37°C
12
L-asparagine
pH 7.5, 37°C, recombinant enzyme
12.3
L-asparagine
-
mutant S180N, pH not specified in the publication, 37°C
13
L-asparagine
-
presence of L-glutamine, K0.5 value, pH 8.8, 37°C
16
L-asparagine
-
K0.5 value, pH 8.8, 37°C
22.1
L-asparagine
pH 7.4, 37°C, wild-type enzyme
29.6
L-asparagine
mutant T169M, cooperative kinetic toward L-Asn, Hill coefficient 1.8, pH 7.5, 37°C
30
L-asparagine
pH 8.2, 80°C, mutant T53Q
30.2
L-asparagine
mutant M121C, cooperative kinetic toward L-Asn, Hill coefficient 1.5, pH 7.5, 37°C
34
L-asparagine
pH 8.2, 80°C, mutant T53Q/K274E
44
L-asparagine
pH 7.4, 37°C, mutant T53Q/K274E
47.2
L-asparagine
pH 7.4, 37°C, mutant T53Q
54
L-asparagine
at 37°C and pH 8.0
57.8
L-asparagine
pH 7.4, 37°C, mutant K274E
60.7
L-asparagine
mutant M121C/T169M, cooperative kinetic toward L-Asn, Hill coefficient 1.7, pH 7.5, 37°C
65.3
L-asparagine
mutant Q63E, pH 7.5, 37°C
66.4
L-asparagine
wild-type, pH 7.5, 37°C
73
L-asparagine
pH 8.2, 80°C, wild-type enzyme
96
L-asparagine
pH 8.2, 80°C, mutant K274E
572.1
L-asparagine
at pH 8.5 and 85°C
710
L-asparagine
using K0.5 value, Hill coefficient 1.0, presence of 8 mM Gln, pH 8.0, 37°C
788.6
L-asparagine
-
pH 8.0, 25°C
800
L-asparagine
at pH 7.5 and 37°C
1503
L-asparagine
-
in 50 mM Tris-HCl buffer (pH 8.6), at 37°C
1782
L-asparagine
mutant N24S, pH not specified in the publication, temperature not specified in the publication
1975
L-asparagine
wild-type, pH not specified in the publication, temperature not specified in the publication
2700
L-asparagine
using K0.5 value, Hill coefficient 1.4, presence of 0.9 mM Gln, pH 8.0, 37°C
3300
L-asparagine
using K0.5 value, Hill coefficient 1.5, pH 8.0, 37°C
3400
L-asparagine
using K0.5 value, Hill coefficient 1.4, presence of 0.3 mM Gln, pH 8.0, 37°C
3700
L-asparagine
mutant S121P, 37°C, pH not specified in the publication
4500
L-asparagine
wild-type, 37°C, pH not specified in the publication
9597
L-asparagine
-
pH 8.6, 37°C, mutant enzyme N281D
14200
L-asparagine
-
pH 8.6, 37°C, mutant enzyme N41D/N281D
19420
L-asparagine
-
pH 8.6, 37°C, wild-type enzyme
22580
L-asparagine
-
pH 8.6, 37°C, mutant enzyme N41D
0.13
L-glutamine
wild-type, pH not specified in the publication, temperature not specified in the publication
0.13
L-glutamine
mutant N24S, pH not specified in the publication, temperature not specified in the publication
0.19
L-glutamine
mutant Q63E, cooperative kinetic toward L-Gln, Hill coefficient 2.3, pH 7.5, 37°C
0.42
L-glutamine
-
pH 8.0, 25°C
0.47
L-glutamine
wild-type, cooperative kinetic toward L-Gln, Hill coefficient 2.0, pH 7.5, 37°C
4.2
L-glutamine
wild-type, 37°C, pH not specified in the publication
35.3
L-glutamine
mutant S121P, 37°C, pH not specified in the publication
51.9
L-glutamine
at pH 8.5 and 85°C
1400
L-glutamine
using K0.5 value, Hill coefficient 1.1, pH 8.0, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.7797
crude enzyme, at 45°C in 50 mM phosphate buffer (pH 7.0)
0.88
crude cell extract, at pH 8.6 and 37°C
0.925
with D-glutamine as substrate, at pH 8.5 and 85°C
1.6
crude enzyme, at pH 8.0 and 37°C
1.985
after 2.6fold purification, at 45°C in 50 mM phosphate buffer (pH 7.0)
1.99
-
Wautersia eutropha grown on medium containing L-asparagine, localized in the periplasm, 37°C, pH 8.6
1017
-
mutant V26A/E30G/K122N/G276D, pH 8.0, 40°C
103
mutant N24S, pH not specified in the publication, temperature not specified in the publication
1034
-
purified enzyme, pH 8.5, 37°C
106
-
purified protein, 37°C, pH not specified in this publication
113.1
after 128.47fold purification, at pH 8.6 and 37°C
1146
-
mutant V26A/E30G/D181G/V245G/G276D, pH 8.0, 40°C
135
crude extract, at 37°C and pH 8.0
14.3
-
cultivar Dokki 331, non-germinating seeds, pH 8.0, 37°C
145
-
substrate L-asparagine, pH 8.0, 37°C
15.36
-
Wautersia eutropha grown on medium containing L-asparagine, localized in the cytoplasm, 37°C, pH 8.6
16.8
-
cultivar Kaha 1, non-germinating seeds, pH 8.0, 37°C
17.9
-
potassium dependent enzyme
18.29
-
Wautersia eutropha grown on medium containing glucose + L-asparagine, localized in the cytoplasm, 37°C, pH 8.6
18.5
-
cultivar Kareem 7, non-germinating seeds, pH 8.0, 37°C
190
-
purified recombinant enzyme
2.11
-
Serratia marcescens NCIM 2919 grown on medium containing L-asparagine, localized in the periplasm, 37°C, pH 8.6
2.52
-
Serratia marcescens MTCC 97 grown on medium containing glucose + L-asparagine, localized in the periplasm, 37°C, pH 8.6
2.926
with L-glutamine as substrate, at pH 8.5 and 85°C
2.94
-
Serratia marcescens MTCC 97 grown on medium containing glucose, localized in the periplasm, 37°C, pH 8.6
2.99
-
Serratia marcescens MTCC 97 grown on medium containing L-asparagine, localized in the periplasm, 37°C, pH 8.6
20
purified recombinant enzyme, pH 7.5, 37°C
200
-
purified native enzyme
204
KC573069
pH not specified in the publication, temperature not specified in the publication
208.1
-
purified AspMP, enzyme without signal peptide, pH 8.0, 37°C
21.6
-
Pectobacterium carotovorum grown on medium containing glucose + L-asparagine, localized in the cytoplasm, 37°C, pH 8.6
22.45
-
Pectobacterium carotovorum grown on medium containing L-asparagine, localized in the cytoplasm, 37°C, pH 8.6
23.7
-
substrate L-glutamine, pH 8.0, 37°C
237.6
-
purified AspSP, enzyme with signal peptide, pH 8.0, 37°C
24.3
-
cultivar Kafer El-Sheikh 1, non-germinating seeds, pH 8.0, 37°C
28.13
-
Serratia marcescens MTCC 97 grown on medium containing L-asparagine, localized in the cytoplasm, 37°C, pH 8.6
3.61
-
Pectobacterium carotovorum grown on medium containing glucose + L-asparagine, localized in the periplasm, 37°C, pH 8.6
3.63
-
Wautersia eutropha grown on medium containing glucose + L-asparagine, localized in the periplasm, 37°C, pH 8.6
3.64
-
Serratia marcescens NCIM 2919 grown on medium containing glucose + L-asparagine, localized in the periplasm, 37°C, pH 8.6
3.753
with D-asparagine as substrate, at pH 8.5 and 85°C
3.81
-
Serratia marcescens NCIM 2919 grown on medium containing glucose, localized in the periplasm, 37°C, pH 8.6
3.9
-
potassium independent enzyme
30.57
-
Serratia marcescens MTCC 97 grown on medium containing glucose + L-asparagine, localized in the cytoplasm, 37°C, pH 8.6
31.45
-
Serratia marcescens NCIM 2919 grown on medium containing glucose + L-asparagine, localized in the cytoplasm, 37°C, pH 8.6
32.3
-
cultivar Fodder, non-germinating seeds, pH 8.0, 37°C
33.73
-
Serratia marcescens NCIM 2919 grown on medium containing L-asparagine, localized in the cytoplasm, 37°C, pH 8.6
4.3
-
Pectobacterium carotovorum grown on medium containing glucose, localized in the periplasm, 37°C, pH 8.6
407.6
after 3.02fold purification, at 37°C and pH 8.0
49
-
cultivar Dokki 331, germinating seeds, pH 8.0, 37°C
5.41
-
Wautersia eutropha grown on medium containing glucose, localized in the periplasm, 37°C, pH 8.6
51.7
-
after Sephadex G-100 gel filtration, 37°C, pH not specified in this publication
541.9
crude enzyme, at pH 8.0 and 90°C
55.7
-
wild-type, pH 8.0, 40°C
5925
-
pH not specified in the publication, temperature not specified in the publication
63
-
cultivar Kaha 1, germinating seeds, pH 8.0, 37°C
662.6
-
purified enzyme, 37°C, pH 8.6
7.25
-
Serratia marcescens NCIM 2919 grown on medium containing glucose, localized in the cytoplasm, 37°C, pH 8.6
7.48
-
Wautersia eutropha grown on medium containing glucose, localized in the cytoplasm, 37°C, pH 8.6
7.622
with L-asparagine as substrate, at pH 8.5 and 85°C
74
-
cultivar Kareem 7, germinating seeds, pH 8.0, 37°C
8.36
-
Serratia marcescens MTCC 97 grown on medium containing glucose, localized in the cytoplasm, 37°C, pH 8.6
87
-
cultivar Kafer El-Sheikh 1, germinating seeds, pH 8.0, 37°C
92
purified recombinant protein, pH 7.0, 37°C
93.28
after 58.44fold purification, at pH 8.0 and 37°C
969
-
ASPG II, from germinating seeds, cultivar Fodder, pH 8.0, 37°C
978.7
after 1.8fold purification, at pH 8.0 and 90°C
1.65
-
-
1.65
-
Pectobacterium carotovorum grown on medium containing L-asparagine, localized in the periplasm, 37°C, pH 8.6
105
wild-type, pH not specified in the publication, temperature not specified in the publication
105
-
cultivar Fodder, non-germinating seeds, pH 8.0, 37°C
3.35
-
Pectobacterium carotovorum grown on medium containing glucose, localized in the cytoplasm, 37°C, pH 8.6
3.35
-
under unoptimized levels of medium components of the production of intracelluar L-asparaginase, pH 8.6, 37°C
62.7
pH 8.0, 37°C, purified enzyme
62.7
-
pH 8.0, 37°C, purified enzyme
additional information
-
-
additional information
-
no glutaminase activity is observed
additional information
-
the production and productivity of L-asparaginase is enhanced by 26.39% (specific activity) and 10.19%, respectively. The individual optimum levels of initial pH of the medium, temperature, rpm of shaking incubator, and inoculum size are found to be 6.90, 29.8°C, 157 rpm, and 2.61% (v/v), respectively, for the production of L-asparaginase.
additional information
-
L-asparaginase activity depends on buffers and ions and ranges from 386 I.U/mg in 50 mM sodium phosphate buffer pH 6.0, 375 mM NaCl up to 510 I.U/mg in 50 mM Tris-HCl pH 7.5, 500 mM NaCl
additional information
-
-
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-
-
brenda
activity is highest in sink tissues, especially in flowers and siliques
brenda
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-
brenda
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developing
brenda
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-
brenda
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sediment samples obtained from Tamilnadu and Kerala in India, production of the enzyme in three different media, solid-State media, tryptone glucose yeast extract, and tryptone fructose yeast extract broth. 10 isolates (S1, S2, S3, S4, S5, S6, S8. K2, K4, K5, and K8), only S3, S4 and K8 show L-asparaginase activity
brenda
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activity in all tested varieties is significantly higher in roots than in spears and leaves
brenda
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solid state, production evaluation and optimization of culture conditions using factorial designs
brenda
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solid state, production evaluation and optimization of culture conditions using factorial designs
-
brenda
optimal conditions of induction are: inductor concentration of 0.1-0.2%, its addition during the middle of the logphase at 1.45-2.3 OU600, and culturing temperature of 28°C. The optimal duration of culturing after induction is 7-16 h
brenda
-
optimal conditions of induction are: inductor concentration of 0.1-0.2%, its addition during the middle of the logphase at 1.45-2.3 OU600, and culturing temperature of 28°C. The optimal duration of culturing after induction is 7-16 h
-
brenda
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optimization of production of L-asparaginase by strain MK-VL_113. Optimal production at pH 7.0 and 30°C in a 72 h old culture in modified ISP-5 medium containing yeast extract, tryptone, or L-asparagine at 1-1.5% w/v as nitrogen source and 2% glycerol as carbon source, overview
brenda
-
optimization of production of L-asparaginase by strain MK-VL_113. Optimal production at pH 7.0 and 30°C in a 72 h old culture in modified ISP-5 medium containing yeast extract, tryptone, or L-asparagine at 1-1.5% w/v as nitrogen source and 2% glycerol as carbon source, overview
-
brenda
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-
brenda
-
-
brenda
-
high L-asparaginase activity is found in cells cultured on L-fructose, D-galactose, sucrose or maltose, and in cells cultured on L-asparagine as the sole nitrogen source
brenda
-
sabourand dextrose broth yields maximum growth and maximum L-asparaginase production
brenda
L-asparaginase-I is constitutive
brenda
L-asparaginase-II is secreted in response to N starvation
brenda
-
carbon sources such as sucrose, maltose, galactose, lactose, mannitol and mannose inhibit enzyme production. Exogenous cAMP in presence of carbon sources stimulates L-asparaginase enzyme production
brenda
-
study of the effect of various carbon sources on pH of the broth and L-asparaginase production
brenda
-
study of the effect of various carbon sources on pH of the broth and L-asparaginase production
brenda
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study of the effect of various carbon sources on pH of the broth and L-asparaginase production
brenda
-
study of the effect of various carbon sources on pH of the broth and L-asparaginase production
-
brenda
-
study of the effect of various carbon sources on pH of the broth and L-asparaginase production
-
brenda
-
study of the effect of various carbon sources on pH of the broth and L-asparaginase production
brenda
-
study of the effect of various carbon sources on pH of the broth and L-asparaginase production
brenda
-
study of the effect of various carbon sources on pH of the broth and L-asparaginase production
brenda
-
study of the effect of various carbon sources on pH of the broth and L-asparaginase production
-
brenda
-
study of the effect of various carbon sources on pH of the broth and L-asparaginase production
-
brenda
-
study of the effect of various carbon sources on pH of the broth and L-asparaginase production
brenda
-
study of the effect of various carbon sources on pH of the broth and L-asparaginase production
brenda
-
study of the effect of various carbon sources on pH of the broth and L-asparaginase production
brenda
-
study of the effect of various carbon sources on pH of the broth and L-asparaginase production
-
brenda
-
study of the effect of various carbon sources on pH of the broth and L-asparaginase production
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
activity in all tested varieties is significantly higher in roots than in spears and leaves
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
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-
brenda
-
activity in all tested varieties is significantly higher in roots than in spears and leaves
brenda
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tips
brenda
-
tips
brenda
-
-
brenda
-
-
brenda
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developing
brenda
-
-
brenda
-
testa
brenda
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-
brenda
-
germinating and non-germinating seeds are studied, highest specific activity in germinating seeds in all cultivars
brenda
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-
brenda
-
brenda
additional information
-
comprehensive comparison shows that the Asparagus officinalis A7 variety has the highest asparaginase activity, while A1 has the lowest, regardless of the tissue type
brenda
additional information
-
production of high levels of L-asparaginase in solid state fermentation, using agro-wastes from three leguminous crops (bran of Cajanus cajan, Phaseolus mungo, and Glycine max)
brenda
additional information
-
highest L-asparaginase production in 2% proline medium, the lowest L-asparaginase production levels is found in the presence of glutamine and urea as nitrogen sources
brenda
additional information
-
the lowest L-asparaginase production levels is found in the presence of glutamine and urea as nitrogen sources
brenda
additional information
-
the synthesis of L-asparaginase in Escherichia coli W and Escherichia coli K-12 is almost completely suppressed if glucose is added at a concentration of 0.5% to the growth medium. Organic acids and amino acids such as L-leucine and L-methionine enhance production of L-asparaginase. n-Dodecane at 6% increases cell concentration by 12.7% and production of L-asparaginase by 21% to give 60.8 IU/ml in the fermentation medium
brenda
additional information
-
a pH of 7.9, casein hydrolysate (3.11%) and corn-steep liquor (3.68%) are the most significant factors improving the enzyme production process
brenda
additional information
-
a pH of 7.9, casein hydrolysate (3.11%) and corn-steep liquor (3.68%) are the most significant factors improving the enzyme production process
-
brenda
additional information
-
enzyme activity is highest during the exponential phase of growth
brenda
additional information
-
incubation temperature, inoculum level and medium pH, among all fermentation factors, are major influential parameters at their individual level, and contributed to more than 60% of total L-asparaginase production
brenda
additional information
-
incubation temperature, inoculum level and medium pH, among all fermentation factors, are major influential parameters at their individual level, and contributed to more than 60% of total L-asparaginase production
-
brenda
additional information
-
isolated from laterite soil samples of Guntar region
brenda
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100000 - 120000
-
gel filtration
1000000
-
L-asparaginase I, gel filtration
102000
recombinant His-tagged enzyme, native PAGE
108000
Erwinia aroidea
-
gel filtration
12000
1 * 20000 + 1 * 12000, uncleaved inactive form, SDS-PAGE
122000
-
ultracentrifugation
138000
-
ultracentrifugation
14200
x * 27000 + x * 14200, SDS-PAGE
144400
-
native PAGE, gel filtration, and MALDI-TOF mass spectrophotometry analysis
15000
-
1 * 20000 + 1 * 15000, active, cleaved enzyme
160000 - 171000
-
sucrose density gradient centrifugation
165000
-
sucrose density gradient centrifugation
25000
-
4 * 25000, SDS-PAGE
27000
x * 27000 + x * 14200, SDS-PAGE
275000
Chlamydomonas sp.
-
-
33700
-
4 * 33700, SDS-PAGE
36100
-
4 * 36100, MALDI-TOF mass spectrophotometry analysis
37500
2 * 37500, SDS-PAGE
37860
-
2 * 37000, SDS-PAGE, 2 * 37860, mass spectrometry
38000
-
x * 38000, SDS-PAGE
39000
-
x * 34500, about, sequence calculation, x * 39000, SDS-PAGE
45000
-
x * 45000, SDS-PAGE, recombinant protein
50000
-
x * 50000, L-asparaginase I, SDS-PAGE
543000
-
4 * 543000, SDS-PAGE
61000
-
potassium dependent enzyme, gel filtration
75316
2 * 75316, calculated from amino acid sequence
75450
-
gel filtration, Superdex-200 column, single peak
83900
-
sucrose density gradient centrifugation
93000
-
x * 93000, L-asparaginase II, SDS-PAGE
96000
Stenotrophomonas geniculata
-
enzyme A
120000
-
-
130000
-
-
130000
-
ultracentrifugation
130000
-
ultracentrifugation
135000
-
ultracentrifugation
135000
Stenotrophomonas geniculata
-
enzyme AG
140000
-
-
147000
-
ultracentrifugation
147000
-
equilibrium sedimentation
150000
-
gel filtration
150000
-
sucrose density gradient centrifugation
150000
-
ultracentrifugation
150000
-
recombinant enzyme, gel filtration
150000
-
about, native PAGE
160000
-
gel filtration
185000
-
gel filtration
20000
1 * 20000 + 1 * 12000, uncleaved inactive form, SDS-PAGE
20000
-
1 * 20000 + 1 * 15000, active, cleaved enzyme
200000
-
gel filtration
200000
-
L-asparaginase II, gel filtration
33000
SDS-PAGE, intact precursor molecule, 19000 + 14000 (native protein) after autoproteolysis
33000
-
1 * 33000, SDS-PAGE
33000
-
x * 33000, SDS-PAGE
33000
-
6 * 33000, SDS-PAGE
34000
-
gel filtration
34000
-
4 * 34000, SDS-PAGE
34000
-
x * 34000, SDS-PAGE
34500
-
4 * 34500, SDS-PAGE
34500
-
x * 34500, about, sequence calculation, x * 39000, SDS-PAGE
35000
-
SDS-PAGE
35000
2 * 35000, SDS-PAGE
35000
-
2 * 35000, SDS-PAGE, indicates this enzyme has two similar subunits
36000
-
2 * 36000, SDS-PAGE, gel filtration
36000
-
x * 36000, recombinant His6-tagged enzyme, SDS-PAGE
36500
-
1 * 36500, SDS-PAGE, MALDI mass spectrometry
36500
2 * 36500, predicted from amino acid sequence
37000
gel filtration
37000
subunit molecular weight, determined by SDS-PAGE
37000
-
4 * 37000, SDS-PAGE
37000
-
4 * 37000, SDS-PAGE
37000
1 * 37000, SDS-PAGE
37000
-
x * 37000, SDS-PAGE
37000
-
x * 37000, SDS-PAGE
37000
x * 37000, SDS-PAGE
37000
2 * 37000, SDS-PAGE
37000
-
4 * 37000, recombinant enzyme, SDS-PAGE
37000
-
2 * 37000, SDS-PAGE, 2 * 37860, mass spectrometry
37000
-
2 * 37000 + 1 * 47000, SDS-PAGE
47000
2 * 47000, recombinant His-tagged enzyme, SDS-PAGE
47000
-
2 * 37000 + 1 * 47000, SDS-PAGE
71000
gel filtration
71000
-
potassium independent enzyme, gel filtration
72000
-
sucrose density gradient centrifugation
72000
-
gel filtration, PAGE
72000
2 * 72000, SDS-PAGE
75000
-
gel filtration
85000
-
-
85000
-
sucrose density gradient centrifugation
additional information
-
-
additional information
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
dimer of dimers
x-ray crystallography
heterotrimer
-
2 * 37000 + 1 * 47000, SDS-PAGE
?
KC573069
x * 57000, SDS-PAGE
?
-
x * 57000, SDS-PAGE
-
?
x * 27000 + x * 14200, SDS-PAGE
?
-
x * 25000, SDS-PAGE
-
?
-
x * 30000, SDS-PAGE
-
?
-
x * 25000, SDS-PAGE
-
?
-
x * 30000, SDS-PAGE
-
?
-
x * 37000, SDS-PAGE
-
?
x * 34100, mass spectrometry
?
-
x * 35000-36000, SDS-PAGE
?
-
x * 34500, about, sequence calculation, x * 39000, SDS-PAGE
?
-
x * 34000, SDS-PAGE
-
?
-
x * 36000, SDS-PAGE
-
?
-
x * 34000, SDS-PAGE
-
?
-
x * 21000 + x * 35000 + x * 40000 + x * 45000, SDS-PAGE
?
-
x * 45000, SDS-PAGE, recombinant protein
?
-
x * 41400, calculated from sequence, x * 45000, His-tagged recombinant protein, SDS-PAGE
?
-
x * 41400, calculated from sequence, x * 45000, His-tagged recombinant protein, SDS-PAGE
-
?
-
x * 53000, SDS-PAGE
-
?
-
x * 93000, L-asparaginase II, SDS-PAGE
?
-
x * 50000, L-asparaginase I, SDS-PAGE
dimer
-
2 * 36300, SDS-PAGE, 2 * 36276, calculated from sequence
dimer
-
2 * 37000, SDS-PAGE, 2 * 37860, mass spectrometry
dimer
-
the enzyme functions as a dimer with each monomer consisting of distinct N- and C-terminal domains (NPfA and CPfA, respectively), connected by a linker
dimer
the linker of the two-domain dimeric enzyme is found to be dispensable. Domains of this enzyme assemble without the linker into a conjoined tetrameric form that exhibits higher activity than the parent enzyme.The global shape and quaternary structure of the conjoined enzyme are also similar to the wild-type enzyme, as observed by their solution scattering profiles and X-ray crystallographic data. Comparison of the crystal structures of substrate-bound and unbound enzymes reveal an altogether new active-site composition and mechanism of action
dimer
-
homodimer, crystal structure
dimer
2 * 75316, calculated, 2 * 72000, SDS-PAGE
dimer
-
1 * 62000 + 1 * 39000, SDS-PAGE
dimer
-
2 * 35000, SDS-PAGE, indicates this enzyme has two similar subunits
heterodimer
-
1 * 20000 + 1 * 15000, active, cleaved enzyme
heterodimer
1 * 20000 + 1 * 12000, uncleaved inactive form, SDS-PAGE
hexamer
-
-
hexamer
6 * 34000, SDS-PAGE
hexamer
-
6 * 33000, SDS-PAGE
homodimer
-
homodimer
2 * 47000, recombinant His-tagged enzyme, SDS-PAGE
homodimer
2 * 72000, SDS-PAGE
homodimer
2 * 75316, calculated from amino acid sequence
homodimer
-
2 * 72000, SDS-PAGE
-
homodimer
-
2 * 75316, calculated from amino acid sequence
-
homodimer
2 * 37500, SDS-PAGE
homodimer
-
2 * 37500, SDS-PAGE
-
homodimer
2 * 35000, SDS-PAGE
homodimer
2 * 36500, predicted from amino acid sequence
homodimer
-
2 * 35000, SDS-PAGE
-
homodimer
-
2 * 36500, predicted from amino acid sequence
-
homodimer
2 * 37000, SDS-PAGE
homodimer
-
2 * 36000, SDS-PAGE, gel filtration
homotetramer
-
4 * 33700, SDS-PAGE
homotetramer
4 * 37000, SDS-PAGE
homotetramer
-
4 * 37000, SDS-PAGE
-
homotetramer
crystal structure
homotetramer
-
4 * 36100, MALDI-TOF mass spectrophotometry analysis
monomer
1 * 37000, SDS-PAGE
monomer
-
1 * 37000, SDS-PAGE
-
monomer
-
1 * 79000, SDS-PAGE
monomer
-
1 * 160000, SDS-PAGE
monomer
-
1 * 160000, SDS-PAGE
-
monomer
-
1 * 33000, SDS-PAGE
monomer
-
1 * 33000, SDS-PAGE
-
monomer
-
1 * 36500, SDS-PAGE, MALDI mass spectrometry
oligomer
-
x * 37000, SDS-PAGE
oligomer
-
x * 36000, recombinant His6-tagged enzyme, SDS-PAGE
tetramer
-
4 * 25000, SDS-PAGE
tetramer
-
4 * 37000, recombinant enzyme, SDS-PAGE
tetramer
-
homotetramer with one active center
tetramer
-
4 * 37000, SDS-PAGE
tetramer
-
(alphabeta)2, a dimer of heterodimers, quarternary structure, crystal structure, overview
tetramer
-
4 * 543000, SDS-PAGE
tetramer
-
4 * 543000, SDS-PAGE
-
tetramer
-
4 * 34000, SDS-PAGE
tetramer
-
4 * 47000, SDS-PAGE
tetramer
-
4 * 47000, SDS-PAGE
-
tetramer
-
4 * 35000, SDS-PAGE
tetramer
-
4 * 35000, SDS-PAGE
-
tetramer
-
4 * 37000, SDS-PAGE
tetramer
-
4 * 34500, SDS-PAGE
tetramer
-
4 * 36600, SDS-PAGE
additional information
-
a divergent sequence between the two enzymes forms a variable loop at the C-terminal of the alpha subunit, the variable loop itself spans positions 169-182 of ASPGA1 and 168-194 of ASPGB1
additional information
-
-
additional information
-
potential rapid pepscan technique for antigen epitope mapping
additional information
-
residues 195RKH197 are critical for enzyme antigenicity
additional information
-
-
-
additional information
-
the polypeptides of 14000 Da and 19000 Da are fragmentation products of the 36000 Da subunit
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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hanging drop vapor diffusion method, using 0.2 M ammonium sulfate, 0.1 M MES at pH 6.0, and 13-15% (w/v) PEG 3350
-
sitting drop vapor diffusion method, using 0.1 M HEPES, pH 7.0, 15% (w/v) PEG 4000
atomic resolution structure
complexed with the L- and D-stereoisomers of the suicide inhibitor L-6-diazo-5-oxy-norleucine and D-6-diazo-5-oxynorleucine solved using X-ray crystallography and refined with data extending to 1.7 A
crystal structures in complex with L-aspartic acid and with L-glutamic acid. The enzyme conformations open and closed correspond to the inactive and active states, respectively. The binding of ligands induces the positioning of the catalytic Thr15 into its active conformation, which in turn allows for the ordering and closure of the flexible N-terminal loop. L-Aspartic acid is more efficient than L-glutamic acid in inducing the active positioning of Thr15
high-resultion crystal structures of the complex of L-asparaginase with L-Glu, D-Asp and succinic acid
comparison between the crystal and solution structures
-
hanging-drop vapour-diffusion method, X-ray structure of the enzyme, crystallized in a new form, space group C2 and refined to 1.95 A resolution, is compared with that of the previously determined crystal for, space group P2(1)
-
L-asparaginase II, S58A mutant of L-asparaginase II
mutant enzyme D90E, hanging drop vapor diffusion method, using 25% PEG MME 550, 100 mM MES pH 6.5, 10 mM ZnSO4 or 30% (w/v) PEG MME 550, 100 mM bicine pH 9.0, 100 mM NaCl or 100 mM HEPES pH 7.5, saturated solution of tribasic sodium citrate mixed with buffer, at citrate:buffer ratio of 9:1
mutant enzyme Y25F, untreated crystals and crystals soaked with L-hydroxylysine. Comparison with previously reported structures. The loop acting as a gate over the active site is very flexible. Its structure in the native enzyme is primarily controlled by the occupancy of the active site
the aspartate product in the crystal structure of L-ASP exists in an unusual alpha-COOH protonation state. The crystal structures may represent intermediate steps rather than initial binding. The substrate's alpha-carboxyl may serve as a proton acceptor and activate one of the catalytic threonines during L-ASP's nucleophilic attack on the amide carbon
resolution of 1.4 A. There are major differences in the active site flexible loop and in the 286-297 loop from the second subunit, which is involved in active-site formation. Accordingly, Glu289, Asn255, and Gln63 are suggested to play roles in modulating the accessibility of the active site
hanging drop vapor diffusion method, using 2.2-2.5 M sodium malonate (pH 7.0)
purified recombinant enzyme, protein solution at 10 mg/ml is mixed in 2:1 ratio with a solution containing 25% w/v PEG 4000, 100 mM HEPES, pH 6.5, and 200 mM MgCl2, incubation overnight at room temperature, the precipitate is centrifuged and the supernatant is diluted 1:1 with water, was used for hanging-drop vapor diffusion, 0.003 ml solution is mixed with 0.001 ml of reservoir solution containing 20% PEG 4000, 100 mM HEPES, pH 6.5, and 200 mM MgCl2, 200 mM MgCl2, streak-seeding with nuclei, room temperature, one day, X-ray diffraction structure determination and analysis at 2.6 A resolution, structure modelling
-
crystals are grown by the hanging-drop vapour-diffusion technique at 22°C. The crystal structures of Erwinia carotovora L-asparaginase complexed with L-aspartate and L-glutamate are determined at 1.9 A and 2.2 A, respectively
-
purified recombinant L-asparaginase in the presence of L-glutamate, hanging drop vapour diffusion method, 10 mg ml protein with 10 mM glutamate, in 1618% w/v PEG 3350, 10 mM phosphate, pH 7.0, and 0.2 M NaF, 20°C, X-ray diffraction structure determination and analysis at 2.6 A resolution using an in-house rotating-anode generator, crystals of monoclinic P21 space group, molecular-replacement
-
molecular modeling of structure
-
purified recombinant enzyme, hanging drop vapour diffusion method, 0.002 ml or protein solution is mixed with 0.001 ml reservoir solution containing 0.1 M Tris-HCl, pH 8.5, 12% v/v PEG 400, and 30 mM NaCl, soaking of crystals in 25% v/v PEG 400 and flash-cooling, X-ray difraction structure determination and analysis at 2.16 A resolution
-
wild-type and mutant S121P. Residue 121 impacts the conformation of the conserved tyrosine 27, a component of the catalytically-important flexible N-terminal loop
-
-
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F162L
-
site-directed mutagenesis of ASPGB1, mutation of Phe162 immediately preceding the variable loop in K+-dependent ASPGB1 specifically affects catalytic activity with Asn, the mutant shows an 8.4fold decrease in Vmax value with Asn, whereas the Vmax with beta-Asp-His is similar to that of the wild-type enzyme
F162W
-
site-directed mutagenesis of ASPGB1, mutation of Phe162 immediately preceding the variable loop in K+-dependent ASPGB1 specifically affects catalytic activity with Asn, the mutant shows a 4fold decrease in Vmax value with Asn, whereas the Vmax with beta-Asp-His is similar to that of the wild-type enzyme
L163F
-
site-directed mutagenesis of ASPGA1, introduction of the more bulky residue in the ASPGA1 mutant only affects Km and Vmax values with beta-Asp-His and not those with Asn, with beta-Asp-His, the Vmax value of the L163F mutant is reduced by approximately fivefold and the Km value by twofold, compared to the wild-type enzyme
N184A
-
site-directed mutagenesis of ASPGB1, the mutant shows a 3fold decrease in Vmax value with Asn as substrate
N184D
-
site-directed mutagenesis of ASPGB1, the mutant shows altered kinetics with substrate compared to the wild-type enzyme
N184Q
-
site-directed mutagenesis of ASPGB1, the mutant shows a Vmax value with Asn as substrate that is similar or slightly higher than that of the wild-type ASPGB1
R165T
-
site-directed mutagenesis of ASPGB1, the mutant shows altered kinetics with substrate compared to the wild-type enzyme
S189A
-
site-directed mutagenesis of ASPGB1, the mutant shows a 3fold decrease in Vmax value with Asn as substrate
S189C
-
site-directed mutagenesis of ASPGB1, the mutant shows altered kinetics with substrate compared to the wild-type enzyme
S189T
-
site-directed mutagenesis of ASPGB1, the mutant shows a Vmax value with Asn as substrate that is similar or slightly higher than that of the wild-type ASPGB1
T166R
-
site-directed mutagenesis of ASPGA1, introduction of the more bulky residue in the ASPGA1 mutant only affects Km and Vmax values with beta-Asp-His and not those with Asn
D289T
-
highly stabilized mutant
E260F
-
thermodynamically stabilized mutant
E292S
-
thermodynamically stabilized mutant
S180N
-
highly stabilized mutant
S180N/D289T/E260F/E292S
-
mutant exhibits a 8.1-fold increase in half-life at 65°C and a 5.56 degrees increase in melting temperature and also displays a substantial increase in the transition state energy barrier and a clear decrease in folding free energy relative to the wild-type
D289T
-
highly stabilized mutant
-
E260F
-
thermodynamically stabilized mutant
-
E292S
-
thermodynamically stabilized mutant
-
S180N
-
highly stabilized mutant
-
S180N/D289T/E260F/E292S
-
mutant exhibits a 8.1-fold increase in half-life at 65°C and a 5.56 degrees increase in melting temperature and also displays a substantial increase in the transition state energy barrier and a clear decrease in folding free energy relative to the wild-type
-
D133I
analysis of the contribution of this position on thermostability
D133L
analysis of the contribution of this position on thermostability
D133T
analysis of the contribution of this position on thermostability
D133V
analysis of the contribution of this position on thermostability
N281D
-
mutant has approximately the same specific activity as the wild-type enzyme. Mutation results in a lower glutaminase activity compared with wild-type and the N41D mutant. Mutation imparts less stability to the enzyme at elevated temperatures. The N281D mutation causes a decrease in substrate affinity as well as a decrease in the stability profile. The deamidation at the N281 site should not be a concern during processing, storage or clinical use. The deamidated variant is active and stable under normal storage conditions
N41D
-
mutant has approximately the same specific activity as the wild-type enzyme. Mutation conferrs a slight increase in kcat. Charge differences to the wild-type enzyme, at -1 per monomer or -4 per tetramer. The deamidation at the N41 site should not be a concern during processing, storage or clinical use. These deamidated variant is active and stable under normal storage conditions
N41D/N281D
-
mutant enzyme has increased specific activity. Charge differences to the wild-type enzyme, at -1 per monomer or -4 per tetramer. The N281D mutation causes a decrease in substrate affinity as well as a decrease in the stability profile. The deamidation at the N41 and N281 sites should not be a concern during processing, storage or clinical use. These deamidated variant is active and stable under normal storage conditions
N281D
-
mutant has approximately the same specific activity as the wild-type enzyme. Mutation results in a lower glutaminase activity compared with wild-type and the N41D mutant. Mutation imparts less stability to the enzyme at elevated temperatures. The N281D mutation causes a decrease in substrate affinity as well as a decrease in the stability profile. The deamidation at the N281 site should not be a concern during processing, storage or clinical use. The deamidated variant is active and stable under normal storage conditions
-
N41D
-
mutant has approximately the same specific activity as the wild-type enzyme. Mutation conferrs a slight increase in kcat. Charge differences to the wild-type enzyme, at -1 per monomer or -4 per tetramer. The deamidation at the N41 site should not be a concern during processing, storage or clinical use. These deamidated variant is active and stable under normal storage conditions
-
N41D/N281D
-
mutant enzyme has increased specific activity. Charge differences to the wild-type enzyme, at -1 per monomer or -4 per tetramer. The N281D mutation causes a decrease in substrate affinity as well as a decrease in the stability profile. The deamidation at the N41 and N281 sites should not be a concern during processing, storage or clinical use. These deamidated variant is active and stable under normal storage conditions
-
D178P
-
mutation enhances the thermostability of the enzyme without changing the activity of the enzyme and thus the therapeutical use of L-asparaginase II might be benefit from these result
D90E
active site mutation
G11V
-
518fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value
G57A
-
3.8fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 5.2fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value
G57L
-
346fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value
G57V
-
48.8fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 37fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value
G88A
-
8300fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value
K196A/H197A
-
investigation of antigenicity, purification of mutant protein
N248A
-
5.9fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 4657fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value. Loss in transition state stabilization is 15 kJ per mol for L-glutamine, 4 kJ per mol for L-aspartic beta-hydroxamate and 7 kJ per mol for L-asparagine
N248D
-
10.18fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 49fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value. Loss in transition state stabilization is 10 kJ per mol for L-glutamine and 6 kJ per mol for L-aspartic beta-hydroxamate
N248E
-
4.4fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 34.4fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value. Loss in transition state stabilization is 9 kJ per mol for L-glutamine and 4 kJ per mol for L-aspartic beta-hydroxamate
N248G
-
7.5fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 116fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value. Loss in transition state stabilization is 12 kJ per mol for L-glutamine and 5 kJ per mol for L-aspartic beta-hydroxamate
N248Q
-
5.9fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 6.2fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value. Loss in transition state stabilization is 10 kJ per mol for L-glutamine and 4 kJ per mol for L-aspartic beta-hydroxamate
N24A
-
increase in activity compared to wild-type, a unique hydrogen bond network contributes to higher activity
N24A/R195S
-
activity similar to wild-type
N24A/Y250L
-
about 75% of wild-type activity. Mutation Y250L is an interface mutation selected to stablize the active tetramer
N24G
-
mutant has a much higher loop flexibility compared with those of wild-type and the other mutants, and a decreased catalytic activity
N24H
-
mutant displays low flexibility in the central part of the loop; the C-terminal region of the loop shows high RMSF values that are likely to cause stability problems
N24S
mutant shows completely preserved asparaginase and glutaminase activities, long-term storage stability, improved thermal parameters, and good resistance to proteases derived from leukaemia cells. The mutant displays a modification in the hydrogen bond network related to residue 24, and a general rigidification of the monomer as compared to wild-type
N24S/D281E
-
RMSF profile similar to that of WT, with a slight increase in flexibility for residues 20-24
N24T
-
increase in activity compared to wild-type. Mutant has very stable lid-loops, resulting in a tightly locked substrate molecule in the active site, stabilized for the catalytic reaction
N24T/R195S
-
about 85% of wild-type activity. Mutation R195S is an interface mutation selected to stablize the active tetramer
N24T/Y250L
-
about 70% of wild-type activity. Mutation Y250L is an interface mutation selected to stablize the active tetramer
Q59A
-
163fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 930fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value. Loss in transition state stabilization is 17 kJ per mol for L-glutamine and 13 kJ per mol for L-aspartic beta-hydroxamate
Q59E
-
15.4fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 93fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value. Loss in transition state stabilization is 7 kJ per mol for L-glutamine and 11 kJ per mol for L-aspartic beta-hydroxamate
Q59G
-
105fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 465fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value. Loss in transition state stabilization is 15 kJ per mol for L-glutamine and 12 kJ per mol for L-aspartic beta-hydroxamate
R195A/H197A
-
investigation of antigenicity, purification of mutant protein
R195A/K196A
-
investigation of antigenicity, purification of mutant protein
R240A
-
mutation increases the [S]0.5 value to 5.9 mM, presumably by reducing the affinity of the site for L-asparagine, although the enzyme retains cooperativity
S58A
-
crystallization of the mutant L-asparaginase II
T162A
-
mutation results in an active enzyme with no cooperativity
T179A
does not undergo autoprocessing
V27L
-
1.13fold increase in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 4.4fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value
V27M
-
1.5fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 11.6fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value
T95D
replacement of catalytic threonine, depletes the enzyme of its catalytic activities with L-asparagine and L-glutamine
M121C
-
about 2.5fold reduced activtiy
-
M121C/T169M
-
mutant has a preserved efficiency vs L-asparagine but is completely unable to carry out L-glutamine hydrolysis. The mutant does not exert any cytotoxic effect on HL-60 cells
-
Q63E
-
mutant displays similar catalytic efficiency versus asparagine and halved glutaminase efficiency with respect to the wild type enzyme, is able to exert a cytotoxic effect comparable to, or higher than, the one of the wild type enzyme
-
T169M
-
about 4fold reduced catalytic activity
-
T16D
-
replacement of catalytic threonine, depletes the enzyme of its catalytic activities with L-asparagine and L-glutamine
-
M121C
-
mutants has nearly 2.5fold reduced catalytic activity compared to the wild type enzyme
-
M121C/T169M
-
the mutant has a preserved efficiency versus L-asparagine but is completely unable to carry out L-glutamine hydrolysis
-
T169M
-
mutants has nearly 4fold reduced catalytic activity compared to the wild type enzyme
-
T168S
the mutant shows no self-cleavage
T186V
the inactive mutant shows partial (45%) self-cleavage
T219A
the inactive mutant shows a complete, albeit slow self-cleavage
T219V
the inactive mutant displays partial (50%) self-cleavage
R206H
-
Arg206 to histidine followed by covalent coupling of mPEG-SNHS [methoxypoly(ethyene glycol) succinate N-hydroxysuccinimide ester] to the mutant enzyme results in an improved modified form of EcaL-ASNase that retains 82% of the original catalytic activity, exhibits enhanced resistance to trypsin degradation, and has higher thermal stability compared with the wild-type enzyme
V26A/E30G/D181G/V245G/G276D
-
21fold increase in catalytic efficiency, mutant shows tolerance toward wider range of pH values and higher temperatures than its wild-type counterpart
V26A/E30G/K122N/G276D
-
20fold increase in catalytic efficiency
V26A/E30G/D181G/V245G/G276D
-
21fold increase in catalytic efficiency, mutant shows tolerance toward wider range of pH values and higher temperatures than its wild-type counterpart
-
V26A/E30G/K122N/G276D
-
20fold increase in catalytic efficiency
-
K274E
site-directed mutagenesis, the active site mutant shows improved enzymatic properties at physiological conditions compared to the wild-type. The mutant is thermodynamically stable and resistant to proteolytic digestion, displays no glutaminase activity, and shows increased and more significant killing of human cell lines HL60, MCF7, and K562 as compared to the Escherichia coli L-asparaginase
T53Q
site-directed mutagenesis, the active site mutant shows improved enzymatic properties at physiological conditions compared to the wild-type. The mutant is thermodynamically stable and resistant to proteolytic digestion, displays no glutaminase activity, and shows increased and more significant killing of human cell lines HL60, MCF7, and K562 as compared to the Escherichia coli L-asparaginase
T53Q/K274E
site-directed mutagenesis, the active site mutant shows improved enzymatic properties at physiological conditions compared to the wild-type. The mutant is thermodynamically stable and resistant to proteolytic digestion, displays no glutaminase activity, and shows increased and more significant killing of human cell lines HL60, MCF7, and K562 as compared to the Escherichia coli L-asparaginase
W301F
-
mutation has no effect on secondary and tertiary structure of the protein. Initiation of unfolding transition of the W301F protein happens at a higher GdnCl concentration compared to W60F, indicated that the N-domain is more stable compared to the C-domain
W60F
-
mutation has no effect on secondary and tertiary structure of the protein. Initiation of unfolding transition of the W301F protein happens at a higher GdnCl concentration compared to W60F, indicated that the N-domain is more stable compared to the C-domain
K215A
-
99.9% loss of activity
T141A
-
99.9% loss of activity
T64A
-
99.9% loss of activity
Y78A
-
99.9% loss of activity
K215A
-
99.9% loss of activity
-
T141A
-
99.9% loss of activity
-
T64A
-
99.9% loss of activity
-
Y78A
-
99.9% loss of activity
-
R195A/K196A/H197A
-
alanine-scanning mutagenesis for determination of amino acid residues critical for antigenicity, construction of four mutants, the mutants' antigenicity is greatly reduced
R195A/K196A/H197A
-
investigation of antigenicity, purification of mutant protein
M121C
mutants has nearly 2.5fold reduced catalytic activity compared to the wild type enzyme
M121C
about 2.5fold reduced activtiy
M121C/T169M
the mutant has a preserved efficiency versus L-asparagine but is completely unable to carry out L-glutamine hydrolysis
M121C/T169M
mutant has a preserved efficiency vs L-asparagine but is completely unable to carry out L-glutamine hydrolysis. The mutant does not exert any cytotoxic effect on HL-60 cells
Q63E
the mutant endows with a similar catalytic efficiency versus L-asparagine and halved glutaminase efficiency with respect to the wild type enzyme
Q63E
mutant displays similar catalytic efficiency versus asparagine and halved glutaminase efficiency with respect to the wild type enzyme, is able to exert a cytotoxic effect comparable to, or higher than, the one of the wild type enzyme
T169M
mutants has nearly 4fold reduced catalytic activity compared to the wild type enzyme
T169M
about 4fold reduced catalytic activity
T16D
inactive
T16D
replacement of catalytic threonine, depletes the enzyme of its catalytic activities with L-asparagine and L-glutamine
S121P
mutant gains L-glutaminase activity, but retains L-asparaginase activity comparable to wild-type
S121P
-
mutant gains L-glutaminase activity, but retains L-asparaginase activity comparable to wild-type
-
additional information
-
construction of chimeras of the variable loop at the C-terminal of the alpha subunit of ASPGA1 and ASPGB1, substrate specificities and kinetics compared to the wild-type enzyme, overview
additional information
-
immobilization of the purified recombinant enzyme on epoxy-activated resin, the immobilized enzyme retains 60% of maximal activity and is highly stable at 4°C, utilization as bioreactor
additional information
immobilization of the purified recombinant enzyme on epoxy-activated resin, the immobilized enzyme retains 60% of maximal activity and is highly stable at 4°C, utilization as bioreactor
additional information
-
immobilization of the purified recombinant enzyme on epoxy-activated resin, the immobilized enzyme retains 60% of maximal activity and is highly stable at 4°C, utilization as bioreactor
-
additional information
-
applicated to mice, the enzyme abolishes serum asparagine and glutamine, and reduces protein synthesis in liver, and spleen, but not in pancreas via increase dephosphorylation of the translation factor eIF2, overview
additional information
-
construction of a chimeric enzyme composed of asparaginase, a tetanus toxin peptide spacer, fragment 831-854, and the foreign cholesteryl ester transfer protein C-terminal fragment, targeting to and expression in the periplasm of Escherichia coli
additional information
-
covalent immobilization of L-asparaginase on poorly soluble microparticles of the natural silk sericin protein, MW 50-200 kDa, from Bomby mori, best at 0.15% glutaraldehyde in 50 mM citrate buffer, pH 8.6, method optimization and biochemical properties of the enzyme-conjugate, overview
additional information
-
reduction of the allergenic potential of the enzyme as therapeutic agent by chemical modification of the enzyme with 2,4-bis(O-methoxypolyethyleneglycol)-6-chloro-S-triazine, mPEG2, in presence of L-asparagine, optimally with a mPEG2/-NH2 molar ratio of 10, the modified enzyme retains 33% of initial enzymatic activity with complete abolishment of immunogenicity, in vitro half-life increments from 4.6 h to 33 h is obtained, method overview
additional information
-
recombinant expression of Vitreoscilla hemoglobin, VHb, in Pseudomonas aeruginosa strain PaJC, the L-asparaginase expression in the recombinant strain is stimulated by glucose, while it is slightly repressed in the wild-type strain NRRL B771, and shows increased enzyme production due to increased oxygen uptake caused by VHb and preference for glucose to other sugars as growth carbon source, optimization of L-asparaginase production, overview
additional information
-
recombinant expression of Vitreoscilla hemoglobin, VHb, in Pseudomonas aeruginosa strain PaJC, the L-asparaginase expression in the recombinant strain is stimulated by glucose, while it is slightly repressed in the wild-type strain NRRL B771, and shows increased enzyme production due to increased oxygen uptake caused by VHb and preference for glucose to other sugars as growth carbon source, optimization of L-asparaginase production, overview
-
additional information
-
residues T64, Y78, T141, K15 are involved in catalysis
additional information
-
residues T64, Y78, T141, K15 are involved in catalysis
-
additional information
-
applicated to mice, the enzyme abolishes serum asparagine, but not glutamine, the enzyme does not alter protein synthesis, overview
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34
-
melting temperature, 50 mM sodium phosphate buffer, pH 6.0, 375 mM NaCl
37 - 50
the enzyme shows no loss of activity after 30 min at 37°C and 40% loss of activity after 30 min at 50°C
41.5
-
melting temperature, 50 mM Tris-HCl pH 9.0
43
-
Tm-value of wild-type enzyme covalently coupled to methoxypoly(ethyene glycol) succinate N-hydroxysuccinimide ester is 42.9°C, Tm-value of mutant enzyme R206H covalently coupled to methoxypoly(ethyene glycol) succinate N-hydroxysuccinimide ester is 43.1°C
46
enzyme shows higher thermal stability at acidic to neutral pH values, lower stability is observed at alkaline pH. The inactivation profiles at pH 5.5 and 7 are biphasic and shows two clear transitions with inflection points corresponding to Tm values of 46.6°C and 62.5°C at pH 5.5, and 46.4 and 57.2°C at pH 7, respectively
46.4
wild type, half-inactivation temperature, 7.5 min
47
enzyme shows higher thermal stability at acidic to neutral pH values, lower stability is observed at alkaline pH. The inactivation profiles at pH 5.5 and 7 are biphasic and shows two clear transitions with inflection points corresponding to Tm values of 46.6°C and 62.5°C at pH 5.5, and 46.4 and 57.2°C at pH 7, respectively
50 - 60
-
the enzyme exhibits about 14.7 and 9.0% retention of activity following 2 h incubation at 50 or 60°C, respectively
53
the wild type enzyme shows 50% activity after 10 min incubation at 53°C
55.8
mutant D133V, half-inactivation temperature, 7.5 min
57
enzyme shows higher thermal stability at acidic to neutral pH values, lower stability is observed at alkaline pH. The inactivation profiles at pH 5.5 and 7 are biphasic and shows two clear transitions with inflection points corresponding to Tm values of 46.6°C and 62.5°C at pH 5.5, and 46.4 and 57.2°C at pH 7, respectively
59
melting temperature, mutant N24S
63
enzyme shows higher thermal stability at acidic to neutral pH values, lower stability is observed at alkaline pH. The inactivation profiles at pH 5.5 and 7 are biphasic and shows two clear transitions with inflection points corresponding to Tm values of 46.6°C and 62.5°C at pH 5.5, and 46.4 and 57.2°C at pH 7, respectively
70 - 95
the enzyme retains more than 60% of its initial activityafter 30 min at 7095°C, and retains 66%, 60%, 54%, 53%, and 43% of its initial activity after 2 h of exposure at 70, 80, 85, 90, and 95°C, respectively
70.6
-
melting temperature, mutant E260F
70.9
-
melting temperature, mutant E292S
71.4
-
melting temperature, mutant D289T
72.5
-
melting temperature, mutant S180N
75.5
-
melting temperature, mutant S180N/D289T/E260F/E292S
85
-
5 min, 30% loss of activity
95
-
5 min, 90% loss of activity
additional information
-
D178P mutation enhances the thermostability of the enzyme without changing the activity of the enzyme and thus the therapeutical use of L-asparaginase II might be benefit from these result
30
-
3 h, stable
30
-
30 min, no loss of activity
37
-
half-life 34.6 min
37
-
pH 4.0-10.0, 20 h, stable
37
particularly stable at
37
-
activities of wild-type and mutant enzyme D178P are stable for 0-4 h. Thereafter, the residual activity of wild type decreases rapidly. After 6 h incubation, wild type enzyme loses 35% activity. The mutant D178P loses 19% activity
37
20 min, almost 80% residual activity, 30 min, almost 60% residual activity
37
-
in presence of 1.0 mg/ml serum albumin, 42% of the activity remains after 72 h
39
-
Tm-value of wild-type enzyme is 38.9°C, Tm-value of mutant enzyme is 38.8°C
39
-
melting temperature, 50 mM MES pH 6.0
40
-
30 min, 20% loss of activity
40
-
half-life is 16.9 h at pH 8.6 and 40°C
40
-
60 min, no significant loss of activity
40
-
stable up to 40°C followed by sharp decline
45
-
60 min, 97% of activity of mutant enzyme D178P remains, 79% of wild-type activity remains
45
-
native enzyme, 50 min, complete loss of activity. Enzyme conjugated to glycol-chitosan, 50 min, 40% residual activity
45
the recombinant enzyme is stable at 45°C for 30 min
49
-
3 min, 50% loss of activity of mutant enzyme N281D and double mutant enzyme N41D/N281D, no loss of activity of wild-type enzyme and mutant enzyme N41D
49
melting temperature, wild-type
50
-
3 h, little loss of activity
50
-
1 h, 99% residual activity
50
-
pH 4.0-10.0, 10 min, stable
50
mutant D133V, half-inactivation after 159.7 h
50
wild type, half-inactivation after 2.7 h
50
-
30 min, about 20% reduced activity, immobilized enzyme and free enzyme
50
-
60 min, 90% of activity of mutant enzyme D178P remains, 71% of wild-type activity remains
50
absolutely stable up to 50°C (10 min incubation time), 50% activity after 10 min at 53°C
50
-
30 min, complete loss of activity
50
-
60 min, about 25% loss of activity
50
purified recombinnat enzyme, loss of 60% activity after 20 min, inactivation within 30 min
50
-
the purified recombinant enzyme retains 38% of its initial activity after 10 min, 33% after 30 and 45 min, and 28% after 60 min of incubation
55
-
10 min, stable
55
mutant D133V, after 7.5 min 87.3% remaining activity
55
wild type, after 7.5 min 37.2% remaining activity
55
-
60 min, 72% of activity of mutant enzyme D178P remains, 56% of wild-type activity remains
55
-
wild type, after 7.5 min 19.9% remaining activity
60
-
5 min, complete inactivation
60
-
pH 5.0-7.0, 10 min, stable
60
-
30 min, about 70% reduced activity, immobilized enzyme and free enzyme
60
-
60 min, 52% of activity of mutant enzyme D178P remains, 43% of wild-type activity remains
60
-
30 min, at least 40% residual activity
60
purified enzyme, pH 5.0-9.0, 15% activity remaining after 3 min, 6% after 5 min
65
-
inactivation at
65
-
pH 7.0, 10 min, 50% loss of activity
70
-
melting temperature, wild-type
70
-
30 min, about 80% reduced activity, immobilized enzyme and free enzyme
80
-
5 min, stable
80
-
30 min, inactivation of immobilized enzyme and free enzyme
80
-
the enzyme retains 55% of the activity at 80°C for 60 min in alkaline pH. Overview of effect of various pH and temperature on L-asparaginase production
80
purified enzyme, pH 5.0-9.0, below 1% activity remaining after 10 min
90
the enzyme retains almost 90% of its activity after 32 h incubation at 90°C
90
-
loses about 95% activity at 90°C
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56% yield, purity is more than 95%
-
82.12fold using ammonium sulfate precipitation, gel filtration on Sephacryl and CM Sephadex C-50 gel filtration, 32% yield
-
acetone precipitation, DEAE cellulose column chromatography, and Sephadex G-100 gel filtration
-
after heat treatment to denature most of the native Escherichia coli proteins, the enzyme is purified by an immobilized metal ion affinity chromatography method
-
all three forms ASPG I, ASPG II, and ASPG II are purified, ASPG II shows highest specific activity, purity 9.27% and 36% recovery
-
ammonium sulfate precipitation and hydrophobic interaction column chromatography
-
further purification of the commercial preparation by gel filtration to remove endotoxin
-
HisTrap column chromatography and Superdex S200 gel filtration
HisTrap HP Ni Sepharose column chromatography and Superdex 200 gel filtration
-
L-asparaginase I and II
-
mutants containing Asn to Asp changes
-
native enzyme 752.9fold by ammonium sulfate fractionation, gel filtration, cation and anion exchange chromatography
-
native enzyme by ammonium sulfate fractionation, anion-exchange chromatography, and gel filtration to homogeneity
-
native enzyme from strain 50071, grown on solid-state fermentation, 106fold to homogeneity by ammonium sulfate fractionation, gel filtration, and ion exchange chromatography
-
native wild-type and recombinant mutant chimeric enzyme from the periplasm of strain BL21(DE3) by periplasm preparation through osmotic shock, and anion exchange chromatography
-
Ni Sepharose column chromatography
-
Ni-IDA column chromatography
Ni-NTA column chromatography
Ni-NTA column chromatography, and gel filtration
Ni-Sepharose column chromatography
Ni-Sepharose column chromatography and Superdex 200 gel filtration
nickel affinity column chromatography
partially purified by ammonium sulfate precipitation and Q-Sepharose column chromatography
recombinant enzyme 3.3fold from strain BLR(DE3) culture supernatant by nickel affinity chromatography
-
recombinant enzyme from Escherichia coli strain BL21(DE3) in a single step procedure to homogeneity by cation exchange
recombinant enzyme from Escherichia coli to homogeneity by cation exchange and L-asparagine affinity chromatography
-
recombinant enzyme, changes in the solubilization conditions of the L-asparaginase may increase by up to 25% its enzymatic activity
-
recombinant His-tagged AnsA 18fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to homogeneity
recombinant His-tagged enzyme, removal of His-tag by thrombin, anion exchange chromatography and gel filtration
-
recombinant His-tagged mutant enzymes from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography
recombinant L-asparaginase II with signal peptide, AspSP, by cation exchange chromatography and gel filtration, and recombinant L-asparaginase II without signal peptide, AspMP, by a single-step cation exchange chromatography, to homogeneity
-
recombinant mutant enzymes from Escherichia coli
-
recombinant PhA from Escherichia coli strain BL21 by anion exchange chromatography and gel filtration, followed by hydrophobic interaction chromatography and ultrafiltration
-
recombinant protein, purified 1.8fold: sonication for preparation of cell free extract, soluble fraction of cell free extract, pH 7.2 and 5.8, chromatography on SP-Sepharose, more than 60% yield
recombinant soluble His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
-
recombinant YpA from Escherichia coli strain BL21 (DE3) by two different steps of anion exchange chromatography
three steps purification process
-
to homogeneity by ammonium sulfate precipitation, dialysis, gel filtration on Sephadex G-100 and SDS-PAGE
-
to homogeneity by ammonium sulfate precipitation, Sephadex G-100, and CM-Sephadex G-50 gel filtration, 87.2fold purity with 25.7% recovery
-
-
-
Ni-NTA column chromatography
Ni-NTA column chromatography
partial
-
recombinant protein
-
recombinant YpA from Escherichia coli strain BL21 (DE3) by two different steps of anion exchange chromatography
recombinant YpA from Escherichia coli strain BL21 (DE3) by two different steps of anion exchange chromatography
-
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cloned and expressed in Escherichia coli
-
cloned and expressed in Escherichia coli BL21 (DE3) cells
expressed in Bacillus subtilis strain 168
-
expressed in Escherichia coli BL21(DE3) C41 cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) pLysS cells
expressed in Escherichia coli BLR(DE3) cells
expressed in Escherichia coli JM109 cells
expressed in Pichia pastoris under the control of the AOX1 gene promoter. High cell density cultures performed with Pichia pastoris harbouring the ASP3 gene using a 2 l instrumented bioreactor, where biomass concentration reached 107 g/l, results in a dramatic increase in volumetric yield (85600 U/l) and global volumetric productivity (1083 U/l)
-
expressed in Pichia pastoris, haboring the ASP3 gene of asparaginase from Saccharomyces cervisiae
-
expression in Escherichia coli
expression in Escherichia coli as a fusion protein with a polyhistidine tail
-
expression in Escherichia coli as N-terminal His-tagged protein
expression in Escherichia coli BL21(DE3)pLysS
expression in Escherichia coli GJ1158. The enzyme is produced intracellularly. There is a marked improvement in the activity of L-asparaginase, obtained from recombinant cells, which is 5fold higher than the native enzyme
-
expression in Escherichia coli strain BL21(DE3)
expression of His-tagged enzyme
-
expression of His-tagged mutant enzymes in Escherichia coli strain Rosetta (DE3)
expression of mutant enzymes in Escherichia coli
-
expression of the mutant chimeric enzyme in the periplasm of strain BL21(DE3)
-
expression of the N-terminally His-tagged enzyme fused to the pelB leader sequence under control of the T7lac promoter in strain BLR(DE3), the recombinant enzyme is secreted to the cell culture medium
-
gene ansA, phylogenetic analysis, expression of His-tagged AnsA in Escherichia coli strain BL21(DE3)
gene ansB, cloning in Escherichia coli strain DH5alpha and expression as His6-tagged protein in Escherichia coli strain BL21(DE3)
-
gene ansB, expression in Escherichia coli strain BL21 (DE3)
gene ansB, expression in Escherichia coli strain BL21 (DE3), method evaluation, overview
gene PH0066, expression in Escherichia coli strain BL21
-
grown by the hanging-drop vapor-diffusion method from protein solutions in a HEPES buffer (pH 6.5) and PEG MME 5000 solutions in a cacodylate buffer (pH 6.5) as the precipitant. Three-dimensional X-ray diffraction data are collected up to 3 A resolution from one crystal at room temperature
-
mutants containing Asn to Asp changes
-
recombinant expression of L-asparaginase II with signal peptide, AspSP, in Escherichia coli strain BL21(DE3) in the periplasmic space and extracellular, and of L-asparaginase II without signal peptide, AspMP, in Escherichia coli strain C41(DE3) in the cytoplasm
-
Streptomyces library screening and cloning, overexpression without artificial signal peptide in Streptomyces lividans using a hyperexpression vector pTONA5a is not successful
Streptomyces library screening, cloning, and functional overexpression without artificial signal peptide in Streptomyces lividans using a hyperexpression vector pTONA5a
-
-
cloned and expressed in Escherichia coli BL21 (DE3) cells
-
cloned and expressed in Escherichia coli BL21 (DE3) cells
expressed in Escherichia coli BL21(DE3) C41 cells
expressed in Escherichia coli BL21(DE3) C41 cells
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
expression in Escherichia coli
-
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
Streptomyces library screening and cloning, overexpression without artificial signal peptide in Streptomyces lividans using a hyperexpression vector pTONA5a is not successful
-
Streptomyces library screening and cloning, overexpression without artificial signal peptide in Streptomyces lividans using a hyperexpression vector pTONA5a is not successful
-
Streptomyces library screening, cloning, and functional overexpression without artificial signal peptide in Streptomyces lividans using a hyperexpression vector pTONA5a
-
Streptomyces library screening, cloning, and functional overexpression without artificial signal peptide in Streptomyces lividans using a hyperexpression vector pTONA5a
-
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diagnostics
-
the enzyme is a marker of chemotherapy dose modification during the induction phase in children with acute lymphoblastic leukemia, overview
analysis
-
direct measurement of L-asparagine in human plasma samples through the use of Escherichia coli Lasparaginase in the soluble form is a major clinical application of this system
analysis
-
biosensor for asparagine using a thermostable recombinant asparaginase from Archaeoglobus fulgidus immobilized in front of an ammonium-selective electrode. The biosensor has a detection limit of 0.06 mM for L-asparagine. It shows high stability
analysis
-
assembly a microplate-based biosensor for the determination of L-asparagine in biological samples. The enzyme is immobilized by crosslinking with glutaraldehyde in a microplate in 96-well format. The sensing is based on the colorimetric measurement of ammonia formation using the Nessler's reagent. The sensor enables monitoring of L-asparagine levels in serum and foods samples in the concentration range 10-200 microM, with a detection limit of 10 microM for L-asparagine
analysis
-
method based on IR spectroscopy to determine PEG-chitosan copolymer composition as well as composition of copolymer-enzyme conjugates. The method is reagentx02free and allows fast and reliable determination of parameters
biotechnology
-
development of a MCE method (micellar electrokinetic electrophoresis) that is sufficiently sensitive and selective for the separation of amino amides and determination of enzyme kinetic constants of L-Asnase
biotechnology
-
statistically based experimental design to maximize the production of glutaminase-free L-asparaginase. The individual optimum levels of initial pH of the medium, temperature, rpm of shaking incubator, and inoculum size are found to be 6.90, 29.8°C, 157 rpm, and 2.61% (v/v), respectively, for the production of L-asparaginase. After physical process parameters optimization, the production and productivity of L-asparaginase is enhanced by 26.39% (specific activity) and 10.19%, respectively. Maximization of L-asparaginase production is achieved at 12 h under optimal levels of physical process parameters in shake flask level
food industry
reduction of acrylamide level in biscuits and bread
food industry
the acrylamide contents in baked dough were reduced to sixty percent after treatment with recombinant enzyme as compared to the untreated control
food industry
-
the enzyme is used for reducing acrylamide formation during the potato frying process
food industry
-
the enzyme reduces acrylamide content in starchy fried food commodities
food industry
the final level of acrylamide in biscuits and bread is decreased by about 81.6% and 94.2%, respectively, upon treatment with 10 U asnase per mg flour
food industry
-
addition of partially purified L-asparaginase to potato products followed by incubation of the mixture at 37°C for 30 min leads to 92% reduction of acrylamide content
food industry
-
approximately 88.5% (0.978 mg/kg) acrylamide can be removed from fried potato chips by mutant V26A/E30G/D181G/V245G/G276D pre-treatment
food industry
pretreatment of potato chips and mooncakes with Asnase significantly decreases their acrylamide by 86% and 52%, respectively
food industry
-
the enzyme is used for reducing acrylamide formation during the potato frying process
-
food industry
-
reduction of acrylamide level in biscuits and bread
-
food industry
-
approximately 88.5% (0.978 mg/kg) acrylamide can be removed from fried potato chips by mutant V26A/E30G/D181G/V245G/G276D pre-treatment
-
medicine
-
enzyme has antitumor activity
medicine
-
enzyme has antitumor activity
medicine
-
enzyme has antitumor activity
medicine
-
enzyme has antitumor activity
medicine
-
enzyme has antitumor activity
medicine
Erwinia aroidea
-
enzyme has antitumor activity
medicine
-
enzyme is used in the treatment of acute lymphomic leukemia
medicine
-
a prospective therapeutic enzyme for leukemia treatment
medicine
-
the use of asparaginase II as a drug for the treatment of acute lymphoblastic leukemia is complicated by the significant glutaminase side activity of the enzyme. Selective reduction in glutaminase activity in variant B248A and other N248 variants
medicine
-
potent antineoplastic agent in animals which has given complete remission in some human leukemias
medicine
-
used for treatment of acute lymphoblastic leukemia, pancreatic carcinoma, and bovine lymphosarcoma
medicine
-
L-asparaginase is an anti-leukemic enzyme
medicine
-
L-asparaginase is important in the induction regimen for treating human acute lymphoblastic leukemia, cytotoxic complications are clinically significant problems lacking mechanistic insight, the enzyme is used in the treatment of both pediatric and adult forms of acute lymphoblastic leukemia, ALL
medicine
-
L-asparaginase is important in the induction regimen for treating human acute lymphoblastic leukemia, cytotoxic complications are clinically significant problems lacking mechanistic insight, the enzyme is used in the treatment of both pediatric andadult forms of acute lymphoblastic leukemia, ALL
medicine
-
the enzyme is a potential therapeutic agent in acute lymphocytic leukemia, acute lymphoblastic leukemia, and chromic myelogenyous leukemia, but causes high allergic reactions
medicine
-
the enzyme is used as therapeutic agent in the treatment of acute childhood lymphoblastic leukemia
medicine
-
the enzyme is used for acute lymphoblastic leukemia treatment, the enzyme does not reduces alpha-antiplasmin and plasminogen levels in human patients, overview
medicine
-
the enzyme is used for acute lymphoblastic leukemia treatment, the enzyme reduces alpha-antiplasmin and plasminogen levels in human patients, this together with the elevated level of thrombin activity in the patients lead to an enhanced risk for thrombosis due to delay in fibrin elimination in Escherichia coli L-asparaginase-treated patients, overview
medicine
-
the enzyme is widely used in chemotherapy for treatment of children with acute lymphoblastic leukemia, in vivo and in vitro resistance of the cells to the enzyme can occur
medicine
-
asparaginase is used in the treatment of acute lymphoblastic leukemia. It depletes plasma asparagine and glutamine, killing leukemic lymphoblasts but also causing immunosuppression. Asparaginase reduces maturing populations of normal B and T cells in thymus, bone marrow, and spleen of mice. Oral consumption of alanyl-glutamine mitigates metabolic stress in spleen, supporting the peripheral immune system and cell-mediated immunity during asparaginase chemotherapy
medicine
-
L-asparaginase is an anticancer agent. Developing an asparaginase production process based on bran of Glycine max as a substrate in solid state fermentation is economically attractive as it is a cheap and readily available raw material in agriculture-based countries
medicine
the enzyme can be efficiently immobilized on epoxy-activated Sepharose CL-6B. The immobilized enzyme retains most of its activity (60%) and shows high stability at 4°C. The approach offers the possibility of designing an L-asparaginase from Erwinia chrysanthemi bioreactor that can be operated over a long period of time with high efficiency, which can be used in leukaemia therapy
medicine
-
the enzyme is important to the treatment of acute lymphoblastic leukemia. Intravenous PEG-asparaginase (L-asparaginase covalently linked to polyethylene glycol) will eliminate painful injection, and achieve rapid peak levels and asparagine depletion
medicine
chemotherapeutic agent
medicine
-
treatment of lymphoma
medicine
-
asparaginase is one of the important bioactive compounds, which have curative effects in cancer treatment
medicine
-
L-asparaginase II from Erwinia carotovora may represent an important alternative therapy in the treatment of acute childhood lymphoblastic leukaemia, despite its promising lower glutaminase activity than Escherichia coli and Erwinia chrysanthemi L-asparaginases II
medicine
-
the enzyme is an important biopharmaceutical product used in the treatment of acute lymphoblastic leukaemia
medicine
-
anticancer drug
medicine
the enzyme is an important drug in the treatment of childhood acute lymphoblastic leukemia
medicine
the recombinant enzyme potentiate a lectin's induction of leukemic K562 cell apoptosis
medicine
enzyme potentiates a lectin's induction of leukemic K562 cell apoptosis, allowing lowering of the drug dosage and shortening of the incubation time
medicine
-
covalent immobilization of enzyme on functionalized aluminium oxide nanoparticles (AONP) and titanium oxide nanoparticles (TONP) for anticancer therapy. The nano-bioconjugates are optimally active at pH 7.0 and 40°C. TONP-asparaginase activity is enhanced in the presence of NH4+ (160%) and Mn2+ (165%) while AONP-asparaginase bioconjugates show increased relative activity with ethyl acetate (142%) and toluene (160%). The nano-bioconjugates display good reusability and maintain over 90% average activity after nine successive cycles. Maximum cytotoxicity (61%) is noticed with AONP-asparaginase against human leukemia MOLT-4 cells. AONP-asparaginase shows better affinity to L-asparagine as compared to free enzyme
medicine
-
enzyme shows antitumor proterties with IC50 values 0.036 mg/ml for MCF-7 cells, 0.037 mM/ml for HCT-116 cells, 0.046 mg/ml for Hep-G2 cells, respectively
medicine
-
L-asparaginase may significantly alter the interactions between microvascular endothelial cells, colon cancer cells, and components, resulting in colon cancer cell injury
medicine
-
purified L-asparaginase does not show hemolysis effect on blood erythrocytes. Recombinant L-asparaginase retains 50% of its initial activity after 90 and 60 min incubation in serum and trypsin separately
medicine
recombinant enzyme is able to inhibit the proliferation of K-562 and Jurkat cell lines
medicine
the anticancer activity of purified asparaginase is comparable or higher than that of commercial Escherichia coli asparaginase. The purified enzyme induces apoptotic cell death in dose-dependent manner, probybly via activation of anintrinsic apoptotic pathway. The purified enzyme is nontoxic for human noncancerous FR-2 cells and human blood lymphocytes
medicine
-
the purified enzyme inhibits the growth of human cell lines Hep-G2, MCF-7 and PC-3 with IC50 values of 14 microg/ml, 12.5 microg/ml and 37 microg/ml, respectively
medicine
-
the purified enzyme shows cytotoxicity for the MOLT-4 leukemic cell lineage
medicine
-
enzyme has antitumor activity
-
medicine
-
the purified enzyme shows cytotoxicity for the MOLT-4 leukemic cell lineage
-
medicine
-
the enzyme can be efficiently immobilized on epoxy-activated Sepharose CL-6B. The immobilized enzyme retains most of its activity (60%) and shows high stability at 4°C. The approach offers the possibility of designing an L-asparaginase from Erwinia chrysanthemi bioreactor that can be operated over a long period of time with high efficiency, which can be used in leukaemia therapy
-
medicine
-
the enzyme is used as therapeutic agent in the treatment of acute childhood lymphoblastic leukemia
-
medicine
-
chemotherapeutic agent
-
medicine
-
the enzyme is an important biopharmaceutical product used in the treatment of acute lymphoblastic leukaemia
-
medicine
-
the recombinant enzyme potentiate a lectin's induction of leukemic K562 cell apoptosis
-
medicine
-
used for treatment of acute lymphoblastic leukemia, pancreatic carcinoma, and bovine lymphosarcoma
-
medicine
-
L-asparaginase may significantly alter the interactions between microvascular endothelial cells, colon cancer cells, and components, resulting in colon cancer cell injury
-
medicine
-
enzyme shows antitumor proterties with IC50 values 0.036 mg/ml for MCF-7 cells, 0.037 mM/ml for HCT-116 cells, 0.046 mg/ml for Hep-G2 cells, respectively
-
medicine
-
potent antineoplastic agent in animals which has given complete remission in some human leukemias
-
pharmacology
-
L-asparaginase is a cancer chemotherapeutically important enzyme
pharmacology
-
L-asparaginase is a cancer chemotherapeutically important enzyme
-
synthesis
-
production of L-asparaginase from Serratia marcescens SK-07 in a batch bioreactor. The optimal levels of L-asparagine, glucose, yeast extract and peptone are 0.93, 3.81, 3.65 and 1.47 g/l, respectively, and maximal L-asparaginase production of 25.02 U mg/1 can be obtained. L-asparagine is the most favourable carbon source for enhanced production of L-asparaginase
synthesis
-
conjugation of enzyme to PEG-chitosan and glycol-chitosan imoproves catalytic efficiency 3- to 6fold under physiological conditions and enhances its resistance to thermal inactivation
synthesis
optimization of production and process conditions for recombinant human enzyme. The maximum biomass yield of 6.7 g/l of enzyme is achieved with fed-batch fermentation. The refolding efficiency is optimal at pH 8.5 (84%) and temperature 25°C (86%)
synthesis
KC573069
production and optimization of growth conditions results in submerged fermentation in modified M9 medium with yeast extract and fructose as carbon and nitrogen sources, respectively, at pH 8.0, incubated for 120 h at 30°C
synthesis
recombinant asparaginase isozyme AnsB fused with the pelB signal sequence and a five aspartate tag is secreted efficiently into culture medium at 34.6 U/mg cell of specific activity. By batch fermentation, recombinant Escherichia coli produces 40.8 U/ml asparaginase isozyme II in the medium. Deletion of the gspDE gene reduces extracellular production of asparaginase isozyme II
synthesis
-
strain is potent extracellular producer of L-asparaginase (347.42 IU) and shows 15fold enhancement of L-asparaginase production (5,205 U/gds) under submerged fermentation condition in 5 days in presence of inducers and activators. Red gram husk is the best substrate in solid state fermentation supporting maximum enzyme activity of 246.32 IU after 5 days of incubation
synthesis
-
strain is potent extracellular producer of L-asparaginase (347.42 IU) and shows 15fold enhancement of L-asparaginase production (5,205 U/gds) under submerged fermentation condition in 5 days in presence of inducers and activators. Red gram husk is the best substrate in solid state fermentation supporting maximum enzyme activity of 246.32 IU after 5 days of incubation
-
synthesis
-
production of L-asparaginase from Serratia marcescens SK-07 in a batch bioreactor. The optimal levels of L-asparagine, glucose, yeast extract and peptone are 0.93, 3.81, 3.65 and 1.47 g/l, respectively, and maximal L-asparaginase production of 25.02 U mg/1 can be obtained. L-asparagine is the most favourable carbon source for enhanced production of L-asparaginase
-
synthesis
-
production and optimization of growth conditions results in submerged fermentation in modified M9 medium with yeast extract and fructose as carbon and nitrogen sources, respectively, at pH 8.0, incubated for 120 h at 30°C
-