Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
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.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3-hydroxy-erythro-L-aspartate + O2
2-amino-3-hydroxy-2-butenedioic acid + H2O2
-
-
-
-
?
DL-aspartate + O2
iminosuccinate + H2O2
-
-
-
?
L-asparagine + H2O + O2
4-amino-2,4-dioxobutanoate + NH3 + H2O2
L-asparagine + O2
4-amino-2-imino-4-oxobutanoate + H2O2
Vmax/Km is 63fold lower compared to L-aspartate
-
-
?
L-aspartate + fumarate
iminoaspartate + succinate
-
-
-
?
L-aspartate + fumarate
iminosuccinate + succinate
-
-
-
-
?
L-aspartate + H2O + fumarate
oxaloacetate + NH3 + succinate
L-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
L-aspartate + O2
alpha-iminosuccinate + H2O2
-
-
-
-
?
L-aspartate + O2
iminoaspartate + H2O2
-
-
-
?
L-aspartate + O2
iminosuccinate + H2O2
L-glutamate + H2O + O2
2-oxopentanedioate + NH3 + H2O2
-
low activity
-
-
?
N-acetyl-L-aspartate + O2
? + H2O2
-
-
-
-
?
N-formyl-L-aspartate + O2
? + H2O2
-
-
-
-
?
additional information
?
-
L-asparagine + H2O + O2

4-amino-2,4-dioxobutanoate + NH3 + H2O2
-
low activity
-
-
?
L-asparagine + H2O + O2
4-amino-2,4-dioxobutanoate + NH3 + H2O2
-
-
-
?
L-aspartate + H2O + fumarate

oxaloacetate + NH3 + succinate
-
-
-
-
?
L-aspartate + H2O + fumarate
oxaloacetate + NH3 + succinate
-
-
-
-
?
L-aspartate + H2O + fumarate
oxaloacetate + NH3 + succinate
-
it is very likely, that fumarate and not O2 is the physiological electron acceptor in vivo
-
-
?
L-aspartate + H2O + fumarate
oxaloacetate + NH3 + succinate
-
can use either molecular oxygen or fumarate to reoxidize the reduced enzyme
-
-
?
L-aspartate + H2O + fumarate
oxaloacetate + NH3 + succinate
-
can use either molecular oxygen or fumarate to reoxidize the reduced enzyme
-
-
?
L-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2
-
-
-
-
?
L-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
-
?
L-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
?
L-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
specific for L-aspartate
-
-
?
L-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
fumarate or succinate can be electron acceptor instead of O2
-
-
?
L-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
first enzyme of quinolinate synthetase system
-
-
?
L-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
oxidation is accelerated in the presence of 0.5 mM fumarate, fumarate appears to be the preferred electron acceptor since its presence inhibits oxygen reduction by 90%
-
-
?
L-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
-
?
L-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
best substrate
-
-
?
L-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
2,6-dichlorophenol-indophenol, ferricyanide and fumarate can be electron acceptor
-
-
?
L-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
2,6-dichlorophenol-indophenol, ferricyanide and fumarate can be electron acceptor
-
-
?
L-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
-
?
L-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
the enzyme oxidizes L-aspartate to iminosuccinate, which is then non-enzymatically hydrolyzed to oxaloacetate
-
-
?
L-aspartate + O2

iminosuccinate + H2O2
-
-
-
-
?
L-aspartate + O2
iminosuccinate + H2O2
-
first enzyme of the de novo biosynthetic pathway of NAD+ in plants
-
-
?
L-aspartate + O2
iminosuccinate + H2O2
-
-
-
-
?
L-aspartate + O2
iminosuccinate + H2O2
-
the first enzyme in the de novo synthesis of NAD+ in bacteria
-
-
?
L-aspartate + O2
iminosuccinate + H2O2
-
can use either molecular oxygen or fumarate to reoxidize the reduced enzyme. The chemistry is similar to that of typical amino acid oxidases in which the transfer of the hydride from C2 of L-aspartate to FAD is rate-limiting and occurs in a concerted manner with respect to deprotonation of the alpha-amine
-
-
?
L-aspartate + O2
iminosuccinate + H2O2
-
the first enzyme in the de novo synthesis of NAD+ in bacteria
-
-
?
L-aspartate + O2
iminosuccinate + H2O2
-
can use either molecular oxygen or fumarate to reoxidize the reduced enzyme. The chemistry is similar to that of typical amino acid oxidases in which the transfer of the hydride from C2 of L-aspartate to FAD is rate-limiting and occurs in a concerted manner with respect to deprotonation of the alpha-amine
-
-
?
L-aspartate + O2
iminosuccinate + H2O2
-
-
-
?
L-aspartate + O2
iminosuccinate + H2O2
KC333624.1
-
-
-
?
L-aspartate + O2
iminosuccinate + H2O2
the enzyme is absolutely stereoselective, since no activity is detected on D-aspartate
-
-
?
L-aspartate + O2
iminosuccinate + H2O2
-
-
-
?
L-aspartate + O2
iminosuccinate + H2O2
highly specific for L-aspartate and does not act on other natural amino acids
-
-
?
L-aspartate + O2
iminosuccinate + H2O2
-
-
-
?
L-aspartate + O2
iminosuccinate + H2O2
highly specific for L-aspartate and does not act on other natural amino acids
-
-
?
additional information

?
-
-
the enzyme oxidizes L-aspartate both under aerobic and anaerobic conditions using oxygen as well as fumarate as electron acceptor. No activity with 3-hydroxy-threo-L-aspartate
-
-
?
additional information
?
-
-
the enzyme oxidizes L-aspartate both under aerobic and anaerobic conditions using oxygen as well as fumarate as electron acceptor. Catalytic role of the active site residue E121, substrate specificity of wild-type and mutant enzymes, molecular docking studies, role of R290, overview. E121 interacts favourably with the charged amino group of the substrate and different ligands might assume different orientations in the active site of the enzyme, binding modes for L-aspartate, overview
-
-
?
additional information
?
-
KC333624
the enzyme does not show activity on L-phenylalanine (50100 mM), L-glutamate (50100 mM), glycine (50100 mM), L-proline (50100 mM) and L-alanine (50100 mM)
-
-
?
additional information
?
-
the enzyme does not show activity on L-phenylalanine (50100 mM), L-glutamate (50100 mM), glycine (50100 mM), L-proline (50100 mM) and L-alanine (50100 mM)
-
-
?
additional information
?
-
-
the enzyme does not show activity on L-phenylalanine (50100 mM), L-glutamate (50100 mM), glycine (50100 mM), L-proline (50100 mM) and L-alanine (50100 mM)
-
-
?
additional information
?
-
KC333624
the enzyme is absolutely stereoselective, since no activity is detected on D-aspartate. The enzyme shows no activity with L-phenylalanine, L-glutamate, glycine, L-proline, and L-alanine
-
-
?
additional information
?
-
the enzyme is absolutely stereoselective, since no activity is detected on D-aspartate. The enzyme shows no activity with L-phenylalanine, L-glutamate, glycine, L-proline, and L-alanine
-
-
?
additional information
?
-
-
the enzyme is absolutely stereoselective, since no activity is detected on D-aspartate. The enzyme shows no activity with L-phenylalanine, L-glutamate, glycine, L-proline, and L-alanine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L-asparagine + H2O + O2
4-amino-2,4-dioxobutanoate + NH3 + H2O2
L-aspartate + fumarate
iminosuccinate + succinate
-
-
-
-
?
L-aspartate + H2O + fumarate
oxaloacetate + NH3 + succinate
L-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
L-aspartate + O2
alpha-iminosuccinate + H2O2
-
-
-
-
?
L-aspartate + O2
iminosuccinate + H2O2
L-glutamate + H2O + O2
2-oxopentanedioate + NH3 + H2O2
-
low activity
-
-
?
additional information
?
-
L-asparagine + H2O + O2

4-amino-2,4-dioxobutanoate + NH3 + H2O2
-
low activity
-
-
?
L-asparagine + H2O + O2
4-amino-2,4-dioxobutanoate + NH3 + H2O2
-
-
-
?
L-aspartate + H2O + fumarate

oxaloacetate + NH3 + succinate
-
-
-
-
?
L-aspartate + H2O + fumarate
oxaloacetate + NH3 + succinate
-
it is very likely, that fumarate and not O2 is the physiological electron acceptor in vivo
-
-
?
L-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2
-
first enzyme of quinolinate synthetase system
-
-
?
L-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
best substrate
-
-
?
L-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
the enzyme oxidizes L-aspartate to iminosuccinate, which is then non-enzymatically hydrolyzed to oxaloacetate
-
-
?
L-aspartate + O2

iminosuccinate + H2O2
-
first enzyme of the de novo biosynthetic pathway of NAD+ in plants
-
-
?
L-aspartate + O2
iminosuccinate + H2O2
-
-
-
-
?
L-aspartate + O2
iminosuccinate + H2O2
-
the first enzyme in the de novo synthesis of NAD+ in bacteria
-
-
?
L-aspartate + O2
iminosuccinate + H2O2
-
the first enzyme in the de novo synthesis of NAD+ in bacteria
-
-
?
L-aspartate + O2
iminosuccinate + H2O2
-
-
-
?
L-aspartate + O2
iminosuccinate + H2O2
-
-
-
?
L-aspartate + O2
iminosuccinate + H2O2
-
-
-
?
additional information

?
-
-
the enzyme oxidizes L-aspartate both under aerobic and anaerobic conditions using oxygen as well as fumarate as electron acceptor. No activity with 3-hydroxy-threo-L-aspartate
-
-
?
additional information
?
-
KC333624
the enzyme is absolutely stereoselective, since no activity is detected on D-aspartate. The enzyme shows no activity with L-phenylalanine, L-glutamate, glycine, L-proline, and L-alanine
-
-
?
additional information
?
-
the enzyme is absolutely stereoselective, since no activity is detected on D-aspartate. The enzyme shows no activity with L-phenylalanine, L-glutamate, glycine, L-proline, and L-alanine
-
-
?
additional information
?
-
-
the enzyme is absolutely stereoselective, since no activity is detected on D-aspartate. The enzyme shows no activity with L-phenylalanine, L-glutamate, glycine, L-proline, and L-alanine
-
-
?
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.
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.
4.7
3-hydroxy-erythro-L-aspartate
-
pH 8.0, 25°C, recombinant wild-type enzyme
18.1
L-asparagine
apparent value, at pH 8.0 and 37°C
0.038 - 75.44
L-aspartate
3.2 - 17
N-acetyl-L-aspartate
3.7 - 17.5
N-formyl-L-aspartate
0.038
L-aspartate

-
pH 8.0, 25°C, recombinant mutant E121A
0.048
L-aspartate
-
pH 8.0, 25°C, recombinant wild-type enzyme
0.5
L-aspartate
-
at aspartate concentration 1-20 mM
0.61
L-aspartate
-
pH 8.0, 25°C, recombinant mutant E121Q
0.79
L-aspartate
-
pH 8.0, 20°C
1
L-aspartate
using O2 as electron acceptor
1.3
L-aspartate
-
recombinant enzyme, at 37°C
1.3
L-aspartate
apparent value, at pH 8.0 and 37°C
2.26
L-aspartate
-
wild type enzyme, at pH 7.5, temperature not specified in the publication
2.9
L-aspartate
-
pH 8.0, 25°C, recombinant mutant E121K
4.1
L-aspartate
-
at L-aspartate concentration 0.2-1 mM
7.5
L-aspartate
pH 7.0, 70°C
10.2
L-aspartate
pH 7.0, 60°C
13.3
L-aspartate
pH 8, 37°C
14.25
L-aspartate
-
mutant enzyme S389A, at pH 7.5, temperature not specified in the publication
14.4
L-aspartate
pH 7.0, 50°C
21.1
L-aspartate
pH 7.0, 37°C
26.11
L-aspartate
-
mutant enzyme R290A, at pH 7.5, temperature not specified in the publication
26.8
L-aspartate
-
pH 8.0, 25°C, recombinant mutant E121D
63.27
L-aspartate
-
mutant enzyme Q242A, at pH 7.5, temperature not specified in the publication
75.44
L-aspartate
-
mutant enzyme H244A, at pH 7.5, temperature not specified in the publication
3.2
N-acetyl-L-aspartate

-
pH 8.0, 25°C, recombinant mutant E121A
17
N-acetyl-L-aspartate
-
pH 8.0, 25°C, recombinant wild-type enzyme
3.7
N-formyl-L-aspartate

-
pH 8.0, 25°C, recombinant wild-type enzyme
17.5
N-formyl-L-aspartate
-
pH 8.0, 25°C, recombinant mutant E121A
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.173
3-hydroxy-erythro-L-aspartate
-
pH 8.0, 25°C, recombinant wild-type enzyme
0.0333 - 23.69
L-aspartate
0.0035 - 0.0055
N-acetyl-L-aspartate
0.0013 - 0.0077
N-formyl-L-aspartate
0.0333
L-aspartate

-
-
0.173
L-aspartate
-
pH 8.0, 25°C, recombinant mutant E121A
0.18
L-aspartate
using O2 as electron acceptor
0.202
L-aspartate
-
pH 8.0, 25°C, recombinant mutant E121Q
0.215
L-aspartate
-
pH 8.0, 25°C, recombinant mutant E121D
0.223
L-aspartate
-
pH 8.0, 25°C, recombinant mutant E121K
0.23
L-aspartate
-
mutant enzyme R290A, at pH 7.5, temperature not specified in the publication
0.25
L-aspartate
-
pH 8.0, 20°C
0.267
L-aspartate
-
pH 8.0, 25°C, recombinant wild-type enzyme
0.7
L-aspartate
pH 7.0, 37°C
1.05
L-aspartate
pH 8, 37°C
1.05
L-aspartate
apparent value, at pH 8.0 and 37°C
1.61
L-aspartate
pH 7.0, 50°C
2.28
L-aspartate
-
mutant enzyme Q242A, at pH 7.5, temperature not specified in the publication
2.53
L-aspartate
pH 7.0, 60°C
2.6
L-aspartate
-
oxygen electron acceptor
4.26
L-aspartate
pH 7.0, 70°C
5.55
L-aspartate
-
fumarate electron acceptor
7.83
L-aspartate
-
mutant enzyme S389A, at pH 7.5, temperature not specified in the publication
10.6
L-aspartate
-
wild type enzyme, at pH 7.5, temperature not specified in the publication
23.69
L-aspartate
-
mutant enzyme H244A, at pH 7.5, temperature not specified in the publication
0.0035
N-acetyl-L-aspartate

-
pH 8.0, 25°C, recombinant wild-type enzyme
0.0055
N-acetyl-L-aspartate
-
pH 8.0, 25°C, recombinant mutant E121A
0.0013
N-formyl-L-aspartate

-
pH 8.0, 25°C, recombinant mutant E121A
0.0077
N-formyl-L-aspartate
-
pH 8.0, 25°C, recombinant wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0368
3-hydroxy-erythro-L-aspartate
-
pH 8.0, 25°C, recombinant wild-type enzyme
0.00021 - 0.0017
N-acetyl-L-aspartate
0.00007 - 0.00208
N-formyl-L-aspartate
0.008
L-aspartate

-
pH 8.0, 25°C, recombinant mutant E121D
0.00884
L-aspartate
-
mutant enzyme R290A, at pH 7.5, temperature not specified in the publication
0.03
L-aspartate
pH 7.0, 37°C
0.036
L-aspartate
-
mutant enzyme Q242A, at pH 7.5, temperature not specified in the publication
0.077
L-aspartate
-
pH 8.0, 25°C, recombinant mutant E121K
0.11
L-aspartate
pH 7.0, 50°C
0.18
L-aspartate
using O2 as electron acceptor
0.25
L-aspartate
pH 7.0, 60°C
0.314
L-aspartate
-
mutant enzyme H244A, at pH 7.5, temperature not specified in the publication
0.32
L-aspartate
-
pH 8.0, 20°C
0.331
L-aspartate
-
pH 8.0, 25°C, recombinant mutant E121Q
0.549
L-aspartate
-
mutant enzyme S389A, at pH 7.5, temperature not specified in the publication
0.57
L-aspartate
pH 7.0, 70°C
4.55
L-aspartate
-
pH 8.0, 25°C, recombinant mutant E121A
4.69
L-aspartate
-
wild type enzyme, at pH 7.5, temperature not specified in the publication
5.56
L-aspartate
-
pH 8.0, 25°C, recombinant wild-type enzyme
0.00021
N-acetyl-L-aspartate

-
pH 8.0, 25°C, recombinant wild-type enzyme
0.0017
N-acetyl-L-aspartate
-
pH 8.0, 25°C, recombinant mutant E121A
0.00007
N-formyl-L-aspartate

-
pH 8.0, 25°C, recombinant mutant E121A
0.00208
N-formyl-L-aspartate
-
pH 8.0, 25°C, recombinant wild-type enzyme
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.
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.