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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
iminosuccinate + succinate
-
-
-
-
?
L-aspartate + H2O + fumarate
oxaloacetate + NH3 + succinate
L-aspartate + H2O + O2
alpha-iminosuccinate + H2O2
-
-
-
-
?
L-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
L-aspartate + O2
iminosuccinate + H2O2
L-aspartate + O2
oxaloacetate + NH3 + 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 + 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
-
-
-
-
?
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
-
-
-
-
?
L-aspartate + O2
iminosuccinate + H2O2
the enzyme is absolutely stereoselective, since no activity is detected on D-aspartate
-
-
?
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 (50–100 mM), L-glutamate (50–100 mM), glycine (50–100 mM), L-proline (50–100 mM) and L-alanine (50–100 mM)
-
-
-
additional information
?
-
the enzyme does not show activity on L-phenylalanine (50–100 mM), L-glutamate (50–100 mM), glycine (50–100 mM), L-proline (50–100 mM) and L-alanine (50–100 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
-
-
-
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L-asparagine + H2O + O2
4-amino-2,4-dioxobutanoate + NH3 + H2O2
L-aspartate + fumarate
iminosuccinate + 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
alpha-iminosuccinate + H2O2
-
-
-
-
?
L-aspartate + H2O + O2
oxaloacetate + NH3 + 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
KC333624, Q972D2
-
-
-
?
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
KC333624, Q972D2
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
-
-
-
-
?
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
?
-
Q972D2
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
-
-
-
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4.7
3-hydroxy-erythro-L-aspartate
-
pH 8.0, 25°C, recombinant wild-type enzyme
18.1
L-asparagine
KC333624;
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
0.33
O2
KC333624;
pH 8, 37°C
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
1
L-aspartate
using O2 as electron acceptor
1.3
L-aspartate
-
recombinant enzyme, at 37°C
1.3
L-aspartate
KC333624;
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
13.3
L-aspartate
KC333624;
pH 8, 37°C
14.25
L-aspartate
-
mutant enzyme S389A, at pH 7.5, temperature not specified in the publication
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
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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
0.267
L-aspartate
-
pH 8.0, 25°C, recombinant wild-type enzyme
1.05
L-aspartate
KC333624;
apparent value, at pH 8.0 and 37°C; pH 8, 37°C
2.28
L-aspartate
-
mutant enzyme Q242A, at pH 7.5, temperature not specified in the publication
2.6
L-aspartate
-
oxygen electron acceptor
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
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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
0.036
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
0.18
L-aspartate
using O2 as electron acceptor
0.314
L-aspartate
-
mutant enzyme H244A, at pH 7.5, temperature not specified in the publication
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
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
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E121A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, catalytically inactive against either 3-OH-erythro- or 3-OH-threo-L-aspartate, but is active with N-acetyl- and N-formyl-L-aspartate
E121D
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme, catalytically inactive against either 3-OH-erythro- or 3-OH-threo-L-aspartate
E121K
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme, catalytically inactive against either 3-OH-erythro- or 3-OH-threo-L-aspartate
E121Q
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, catalytically inactive against either 3-OH-erythro- or 3-OH-threo-L-aspartate
H244A
-
binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate
H244S
-
binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate
H351A
-
binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate
H351S
-
binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate
R386L
-
binds substrate analogues with higher dissociation constants and presens lower kcat/Km values in the reduction of fumarate
H244A
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Q242A
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
R290A
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
S389A
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
additional information

-
T-DNA-based disruption of the L-Asp oxidase gene is embryo lethal
additional information
-
mutant reduces affinity to FAD
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Seifert, J.; Kunz, N.; Flachmann, R.; Laufer, A.; Jany, K.D.; Gassen, H.G.
Expression of the E. coli nadB gene and characterization of the gene product L-aspartate oxidase
Biol. Chem. Hoppe-Seyler
371
239-248
1990
Escherichia coli
brenda
Flachmann, R.; Kunz, N.; Seifert, J.; Gutlich, M.; Wientjes, F.J.; Läufer, A.; Gassen, H.G.
Molecular biology of pyridine nucleotide biosynthesis in Escherichia coli. Cloning and characterization of quinolinate synthesis genes nadA and nadB
Eur. J. Biochem.
175
221-229
1988
Escherichia coli
brenda
Hosokawa, Y.; Mitchell, E.; Gholson, R.K.
Higher plants contain L-asparate oxidase, the first enzyme of the Escherichia coli quinolinate synthetase system
Biochem. Biophys. Res. Commun.
111
188-193
1983
Gossypium hirsutum
brenda
Wilder, J.P.; Sae-Lee, J.A.; Mitchell, E.D.; Gholson, R.K.
The L-aspartate oxidase reported to be present in higher plants is actually glutamic oxaloacetic transaminase
Biochem. Biophys. Res. Commun.
123
836-841
1984
Gossypium hirsutum
brenda
Nasu, S.; Wicks, F.D.; Gholson, R.K.
L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase
J. Biol. Chem.
257
626-632
1982
Escherichia coli
brenda
Tedeschi, G.; Negri, A.; Mortarino, M.; Ceciliani, F.; Simonic, T.; Faotto, L.; Ronchi, S.
L-Aspartate oxidase from Escherichia coli. II. Interaction with C4 dicarboxylic acids and identification of a novel L-aspartate:fumarate oxidoreductase activity
Eur. J. Biochem.
239
427-433
1996
Escherichia coli
brenda
Tedeschi, G.; Ronchi, S.; Simonic, T.; Treu, C.; Mattevi, A.; Negri, A.
Probing the active site of L-aspartate oxidase by site-directed mutagenesis: Role of basic residues in fumarate reduction
Biochemistry
40
4738-4744
2001
Escherichia coli
brenda
Bossi, R.T.; Negri, A.; Tedeschi, G.; Mettevi, A.
Structure of FAD-bound L-aspartate oxidase: Insight into substrate specificity and catalysis
Biochemistry
41
3018-3024
2002
Escherichia coli (P10902)
brenda
Mortarino, M.; Negri, A.; Tedeschi, G.; Simonic, T.; Duga, S.; Gassen, H.G.; Ronchi, S.
L-aspartate oxidase from Escherichia coli. I. Characterization of coenzyme binding and product inhibition
Eur. J. Biochem.
239
418-426
1996
Escherichia coli
brenda
Sakuraba, H.; Satomura, T.; Kawakami, R.; Yamamoto, S.; Kawarabayasi, Y.; Kikuchi, H.; Ohshima, T.
L-Aspartate oxidase is present in the anaerobic hyperthermophilic archaeon Pyrococcus horikoshii OT-3: characteristics and role in the de novo biosynthesis of nicotinamide adenine dinucleotide proposed by genome sequencing
Extremophiles
6
275-281
2002
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
brenda
Messner, K.R.; Imlay, J.A.
Mechanism of superoxide and hydrogen peroxide formation by fumarate reductase, succinate dehydrogenase, and aspartate oxidase
J. Biol. Chem.
277
42563-42571
2002
Escherichia coli
brenda
Katoh, A.; Uenohara, K.; Akita, M.; Hashimoto, T.
Early steps in the biosynthesis of NAD in Arabidopsis start with aspartate and occur in the plastid
Plant Physiol.
141
851-857
2006
Arabidopsis thaliana
brenda
Sakuraba, H.; Yoneda, K.; Asai, I.; Tsuge, H.; Katunuma, N.; Ohshima, T.
Structure of L-aspartate oxidase from the hyperthermophilic archaeon Sulfolobus tokodaii
Biochim. Biophys. Acta
1784
563-571
2008
Sulfolobus tokodaii
brenda
Marinoni, I.; Nonnis, S.; Monteferrante, C.; Heathcote, P.; Haertig, E.; Boettger, L.H.; Trautwein, A.X.; Negri, A.; Albertini, A.M.; Tedeschi, G.
Characterization of L-aspartate oxidase and quinolinate synthase from Bacillus subtilis
FEBS J.
275
5090-5107
2008
Bacillus subtilis, Bacillus subtilis (P38032)
brenda
Tedeschi, G.; Nonnis, S.; Strumbo, B.; Cruciani, G.; Carosati, E.; Negri, A.
On the catalytic role of the active site residue E121 of E. coli L-aspartate oxidase
Biochimie
92
1335-1342
2010
Escherichia coli
brenda
Bifulco, D.; Pollegioni, L.; Tessaro, D.; Servi, S.; Molla, G.
A thermostable L-aspartate oxidase: a new tool for biotechnological applications
Appl. Microbiol. Biotechnol.
97
7285-7295
2013
Sulfolobus tokodaii (KC333624), Sulfolobus tokodaii (Q972D2)
brenda
Leese, C.; Fotheringham, I.; Escalettes, F.; Speight, R.; Grogan, G.
Cloning, expression, characterisation and mutational analysis of L-aspartate oxidase from Pseudomonas putida
J. Mol. Catal. B
85-86
17-22
2013
Pseudomonas putida
-
brenda
Macho, A.; Boutrot, F.; Rathjen, J.; Zipfel, C.
Aspartate oxidase plays an important role in Arabidopsis stomatal immunity
Plant Physiol.
159
1845-1856
2012
Arabidopsis thaliana
brenda
D'Arrigo, P.; Allegretti, C.; Fiorati, A.; Piubelli, L.; Rosini, E.; Tessaro, D.; Valentino, M.; Pollegioni, L.
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