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(1-aminopropyl)-phosphonate
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(3-aminopropyl)-phosphonate
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(aminomethyl)-phosphonate
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2,3-diphosphoglycerate
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2-hydroxy-3-nitropropionate
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-
5,5'-dithiobis(2-nitrobenzoate)
aspartate beta-semialdehyde
Ba2+
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2 mM, 98% inhibition
beta-aspartylhydrazine
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-
Ca2+
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10 mM, 18% loss of activity
CTP
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allosteric inhibition, moderate decrease in activity
cytidine
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allosteric inhibition, moderate decrease in activity
D-Aspartate
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competitive
diethyldicarbonate
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reactivated by hydroxylamine
diethylpyrocarbonate
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inactivation, reactivation with NH2OH, aspartate, fumarate and chloride protect
dimethyl sulfoxide
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nonspecific
DL-2-amino-3-phosphonopropionate
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-
DL-2-amino-4-phosphonobutyrate
DL-2amino-3-phosphonopropanoate
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ethanol
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moderate, nonspecific
fumaric acid aldehyde
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fumaric acid aldehyde ethyl ester
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-
guanidine hydrochloride
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at concentrations lower than 1 M, activity is gradually decreased suggesting the existence of the native tetrameric form with denaturation intermediates such as dimeric and monomeric forms of the enzyme. At higher concentrations above 1 M, the enzyme completely lost the activity, suggesting that the enzyme structure is completely denatured
HgCl2
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1 mM, 89.5% inhibition
hydroxylamine
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competitive
iodoacetate
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1 mM, 94% inhibition
K+
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2 mM, 98% inhibition
methanol
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moderate, nonspecific
MgCl2
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inhibitor at high concentrations (above 10 mM)
NaCN
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1 mM, 42% inhibition
Ni2+
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2 mM, 98% inhibition
O-phospho-L-serine
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competitive
p-chloromercuribenzoate
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0.1 mM, 100% inhibition
Semicarbazide hydrochloride
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1 mM, 30% inhibition
Zn2+
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0.0005 mM, 40% loss of activity
3-nitropropionate
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competitive
3-nitropropionate
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competitive
5,5'-dithiobis(2-nitrobenzoate)
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complete
5,5'-dithiobis(2-nitrobenzoate)
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-
aspartate beta-semialdehyde
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i.e. aspartic beta-semialdehyde.Inactivates as an active-site directed agent
aspartate beta-semialdehyde
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-
D-malate
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competitive
DL-2-amino-4-phosphonobutyrate
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-
DL-2-amino-4-phosphonobutyrate
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competitive
EDTA
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complete
fumarate
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-
fumarate
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50% inhibition at a concentration of 0.2 to 0.6 mM, pH 6.2, 50% inhibition at a concentration of 1.1 to 2.5 mM, pH 7.5
Hg2+
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2 mM, 98% inhibition
KCl
aspartase activity is severely inhibited by potassium chloride
N-ethylmaleimide
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1 mM, 100% inhibition
Na+
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2 mM, 98% inhibition
o-phospho-D-serine
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-
o-phospho-D-serine
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competitive
p-hydroxymercuribenzoate
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complete
p-hydroxymercuribenzoate
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-
succinate
-
competitive
additional information
enzyme is upregulated by oxygen limitation
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additional information
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enzyme is upregulated by oxygen limitation
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additional information
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additional information
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additional information
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additional information
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overview on inhibitors
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additional information
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additional information
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