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Information on EC 1.4.3.16 - L-aspartate oxidase
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1.4.3.16 L-aspartate oxidaseIUBMB Comments
A flavoprotein (FAD). L-Aspartate oxidase catalyses the first step in the de novo biosynthesis of NAD+ in some bacteria. O2 can be replaced by fumarate as electron acceptor, yielding succinate . The ability of the enzyme to use both O2 and fumarate in cofactor reoxidation enables it to function under both aerobic and anaerobic conditions . Iminosuccinate can either be hydrolysed to form oxaloacetate and NH3 or can be used by EC 2.5.1.72, quinolinate synthase, in the production of quinolinate. The enzyme is a member of the succinate dehydrogenase/fumarate-reductase family of enzymes .
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Word Map
- 1.4.3.16
- quinolinate
-
nada
- fumarate
- pyridine
- flavoproteins
- iminoaspartate
- dihydroxyacetone
-
flavoenzyme
-
fad-binding
- biotechnology
The enzyme appears in viruses and cellular organisms
Synonyms
l-aspartate oxidase, laspo, tl-laspo, stlaspo, l-asp oxidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L-aspartate oxidase
LASPO
nadB
oxidase, L-aspartate
-
-
-
-
Tl-LASPO
additional information
-
LASPO belongs to the succinate dehydrogenase/fumarate reductase family
LASPO
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-aspartate + O2 = iminosuccinate + H2O2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidative deamination
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
L-aspartate:oxygen oxidoreductase
A flavoprotein (FAD). L-Aspartate oxidase catalyses the first step in the de novo biosynthesis of NAD+ in some bacteria. O2 can be replaced by fumarate as electron acceptor, yielding succinate [5]. The ability of the enzyme to use both O2 and fumarate in cofactor reoxidation enables it to function under both aerobic and anaerobic conditions [5]. Iminosuccinate can either be hydrolysed to form oxaloacetate and NH3 or can be used by EC 2.5.1.72, quinolinate synthase, in the production of quinolinate. The enzyme is a member of the succinate dehydrogenase/fumarate-reductase family of enzymes [5].
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CAS REGISTRY NUMBER
COMMENTARY
69106-47-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-hydroxy-erythro-L-aspartate + O2
2-amino-3-hydroxy-2-butenedioic acid + H2O2
-
-
-
-
?
L-asparagine + O2
4-amino-2-imino-4-oxobutanoate + H2O2
KC333624, Q972D2
Vmax/Km is 63fold lower compared to L-aspartate
-
-
?
L-glutamate + H2O + O2
2-oxopentanedioate + NH3 + H2O2
-
low activity
-
-
?
L-asparagine + H2O + O2
4-amino-2,4-dioxobutanoate + NH3 + H2O2
-
low activity
-
-
?
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
-
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
-
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
KC333624, Q972D2
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
-
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
KC333624, Q972D2
the enzyme is absolutely stereoselective, since no activity is detected on D-aspartate
-
-
?
L-aspartate + O2
iminosuccinate + H2O2
highly specific for L-aspartate and does not act on other natural amino acids
-
-
?
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
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-glutamate + H2O + O2
2-oxopentanedioate + NH3 + H2O2
-
low activity
-
-
?
L-asparagine + H2O + O2
4-amino-2,4-dioxobutanoate + NH3 + H2O2
-
low activity
-
-
?
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
KC333624, Q972D2
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
-
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
-
-
?
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
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
E121 belongs to a polypeptide stretch, residues 119-127, involved in the interdomain contact between the FAD and the capping domains and is hydrogen bound to G51, itself belonging to a loop of residues 49-57 playing a key role in coenzyme binding
FAD
the enzyme utilized fumaric acid, 2,6-dichlorophenolindophenol, and ferricyanide in addition to FAD as a cofactor under anaerobic conditions
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
-
inhibits the enzyme at physiological concentrations by competing with the flavin for binding to the apoprotein
NADP+
-
inhibits the enzyme at physiological concentrations by competing with the flavin for binding to the apoprotein
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.7
3-hydroxy-erythro-L-aspartate
-
pH 8.0, 25°C, recombinant wild-type enzyme
2.26
L-aspartate
-
wild type enzyme, at pH 7.5, temperature not specified in the publication
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
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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.173
3-hydroxy-erythro-L-aspartate
-
pH 8.0, 25°C, recombinant wild-type enzyme
0.23
L-aspartate
-
mutant enzyme R290A, at pH 7.5, temperature not specified in the publication
2.28
L-aspartate
-
mutant enzyme Q242A, at pH 7.5, temperature not specified in the publication
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
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0368
3-hydroxy-erythro-L-aspartate
-
pH 8.0, 25°C, recombinant wild-type enzyme
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
0.314
L-aspartate
-
mutant enzyme H244A, at pH 7.5, temperature not specified in the publication
0.549
L-aspartate
-
mutant enzyme S389A, at pH 7.5, temperature not specified in the publication
4.69
L-aspartate
-
wild type enzyme, at pH 7.5, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the specific activity of the purified enzyme is estimated to be 0.7 units/mg at 37°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 12
-
pH 7.0: about 55% of maximal activity, pH 12.0: about 80% of maximal activity
8.8 - 12
KC333624, Q972D2
pH 8.8: about 50% of maximal activity, pH 12.0: about 70% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25