1.4.3.16: L-aspartate oxidase
This is an abbreviated version!
For detailed information about L-aspartate oxidase, go to the full flat file.
Word Map on EC 1.4.3.16
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1.4.3.16
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quinolinate
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nada
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fumarate
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pyridine
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flavoproteins
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iminoaspartate
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dihydroxyacetone
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flavoenzyme
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fad-binding
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biotechnology
- 1.4.3.16
- quinolinate
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nada
- fumarate
- pyridine
- flavoproteins
- iminoaspartate
- dihydroxyacetone
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flavoenzyme
-
fad-binding
- biotechnology
Reaction
Synonyms
AO, At5g14760, FIN4, L-Asp oxidase, L-aspartate oxidase, LAO, LASPO, More, nadB, oxidase, L-aspartate, StLASPO, Tl-LASPO
ECTree
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Substrates Products
Substrates Products on EC 1.4.3.16 - L-aspartate oxidase
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REACTION DIAGRAM
3-hydroxy-erythro-L-aspartate + O2
2-amino-3-hydroxy-2-butenedioic acid + H2O2
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?
L-asparagine + O2
4-amino-2-imino-4-oxobutanoate + H2O2
KC333624, Q972D2
Vmax/Km is 63fold lower compared to L-aspartate
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?
L-glutamate + H2O + O2
2-oxopentanedioate + NH3 + H2O2
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low activity
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?
4-amino-2,4-dioxobutanoate + NH3 + H2O2
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low activity
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?
L-aspartate + H2O + fumarate
oxaloacetate + NH3 + succinate
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it is very likely, that fumarate and not O2 is the physiological electron acceptor in vivo
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?
L-aspartate + H2O + fumarate
oxaloacetate + NH3 + succinate
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can use either molecular oxygen or fumarate to reoxidize the reduced enzyme
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?
L-aspartate + H2O + fumarate
oxaloacetate + NH3 + succinate
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can use either molecular oxygen or fumarate to reoxidize the reduced enzyme
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?
L-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
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specific for L-aspartate
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?
L-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
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fumarate or succinate can be electron acceptor instead of O2
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?
L-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
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first enzyme of quinolinate synthetase system
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?
L-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
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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%
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?
L-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
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2,6-dichlorophenol-indophenol, ferricyanide and fumarate can be electron acceptor
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?
L-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
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2,6-dichlorophenol-indophenol, ferricyanide and fumarate can be electron acceptor
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?
L-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
KC333624, Q972D2
the enzyme oxidizes L-aspartate to iminosuccinate, which is then non-enzymatically hydrolyzed to oxaloacetate
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?
L-aspartate + O2
iminosuccinate + H2O2
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first enzyme of the de novo biosynthetic pathway of NAD+ in plants
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?
L-aspartate + O2
iminosuccinate + H2O2
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the first enzyme in the de novo synthesis of NAD+ in bacteria
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?
L-aspartate + O2
iminosuccinate + H2O2
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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
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?
L-aspartate + O2
iminosuccinate + H2O2
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the first enzyme in the de novo synthesis of NAD+ in bacteria
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?
L-aspartate + O2
iminosuccinate + H2O2
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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
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?
L-aspartate + O2
iminosuccinate + H2O2
KC333624, Q972D2
the enzyme is absolutely stereoselective, since no activity is detected on D-aspartate
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?
L-aspartate + O2
iminosuccinate + H2O2
highly specific for L-aspartate and does not act on other natural amino acids
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?
L-aspartate + O2
iminosuccinate + H2O2
highly specific for L-aspartate and does not act on other natural amino acids
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?
?
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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
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additional information
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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
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?
additional information
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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)
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?
additional information
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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)
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?
additional information
?
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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)
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?
additional information
?
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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
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?
additional information
?
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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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-
?
additional information
?
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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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-
?