Information on EC 1.4.3.16 - L-aspartate oxidase:
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

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EC NUMBERCOMMENTARY
1.4.3.16-

RECOMMENDED NAMEGeneOntology No.
L-aspartate oxidaseGO:0044318

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
L-aspartate + O2 = iminosuccinate + H2O2
show the reaction diagram		----

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
oxidation----
oxidative deamination----
redox reaction----
reduction----

PATHWAYKEGG LinkMetaCyc Link
Alanine, aspartate and glutamate metabolism00250 -
Metabolic pathways01100 -
NAD biosynthesis I (from aspartate)-PYRIDNUCSYN-PWY
Nicotinate and nicotinamide metabolism00760 -
nicotine biosynthesis-PWY-5316

SYSTEMATIC NAMEIUBMB Comments
L-aspartate:oxygen oxidoreductase (deaminating)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].

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
AOArabidopsis thaliana--676612
L-Asp oxidaseArabidopsis thaliana--676612
L-aspartate oxidaseBacillus subtilisP38032-686712
LAOSulfolobus tokodaii--685396
LASPO----
nadBBacillus subtilisP38032gene name686712
oxidase, L-aspartate----
LASPOEscherichia coli--711324
additional informationEscherichia coli-LASPO belongs to the succinate dehydrogenase/fumarate reductase family711324

CAS REGISTRY NUMBERCOMMENTARY
69106-47-4-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Arabidopsis thaliana-676612--Manually annotated by BRENDA team
Bacillus subtilis-686712P38032UniProtManually annotated by BRENDA team
Escherichia coli-391756, 391757, 391760, 391764, 656090, 711324--Manually annotated by BRENDA team
Escherichia coli-391763P10902UniprotManually annotated by BRENDA team
Escherichia colifumarate reductase in anaerobic conditions391761, 391762--Manually annotated by BRENDA team
Gossypium hirsutum-391758--Manually annotated by BRENDA team
Gossypium hirsutumactually glutamic oxaloacetic transaminase391759--Manually annotated by BRENDA team
Pyrococcus horikoshiiOT-3391765--Manually annotated by BRENDA team
Pyrococcus horikoshii OT-3OT-3391765--Manually annotated by BRENDA team
Sulfolobus tokodaii-685396--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
physiological functionBacillus subtilisP38032NadB and NadA (quinolinate synthase) interact with each other. The interaction is not species-specific and both proteins are not tightly bound to one another, indicating a function as a reversible multienzyme complex; NadB shows three enzymatic activities: L-aspartate-oxygen oxidoreductase activity, fumarate reductase activity, and L-aspartate-fumarate oxidoreductase activity686712
physiological functionEscherichia coli-LASPO is a flavoenzyme catalyzing the first step in the de novo biosynthesis of NAD+. The enzyme oxidizes L-aspartate both under aerobic and anaerobic conditions using oxygen as well as fumarate as electron acceptor711324
additional informationEscherichia coli-LASPO displays strong primary and tertiary structure similarity with the flavin containing subunit of the proteins belonging to the succinate dehydrogenase/fumarate reductase family. The similarity extends to the active site residues, with LASPO differing from the other enzymes of the family only for the presence of a conserved glutamate 121, which is substituted by apolar amino acids in the other enzymes711324

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
3-hydroxy-erythro-L-aspartate + O22-amino-3-hydroxy-2-butenedioic acid + H2O2
show the reaction diagram		Escherichia coli--711324--?
L-aspartate + fumarateiminosuccinate + succinate
show the reaction diagram		Escherichia coli--711324--?
L-aspartate + H2O + fumarateoxaloacetate + NH3 + succinate
show the reaction diagram		Escherichia coli--656090--?
L-aspartate + H2O + fumarateoxaloacetate + NH3 + succinate
show the reaction diagram		Bacillus subtilisP38032-686712--?
L-aspartate + H2O + fumarateoxaloacetate + NH3 + succinate
show the reaction diagram		Escherichia coli-it is very likely, that fumarate and not O2 is the physiological electron acceptor in vivo656090--?
L-aspartate + H2O + O2oxaloacetate + NH3 + H2O2
show the reaction diagram		Escherichia coli--391756, 391760--?
L-aspartate + H2O + O2oxaloacetate + NH3 + H2O2
show the reaction diagram		Escherichia coliP10902-391763--?
L-aspartate + H2O + O2oxaloacetate + NH3 + H2O2
show the reaction diagram		Escherichia coli--391764--?
L-aspartate + H2O + O2oxaloacetate + NH3 + H2O2
show the reaction diagram		Arabidopsis thaliana--676612--?
L-aspartate + H2O + O2oxaloacetate + NH3 + H2O2
show the reaction diagram		Gossypium hirsutum--391758, 391759--?
L-aspartate + H2O + O2oxaloacetate + NH3 + H2O2
show the reaction diagram		Sulfolobus tokodaii--685396--?
L-aspartate + H2O + O2oxaloacetate + NH3 + H2O2
show the reaction diagram		Escherichia coli-specific for L-aspartate391757--?
L-aspartate + H2O + O2oxaloacetate + NH3 + H2O2
show the reaction diagram		Pyrococcus horikoshii-2,6-dichlorophenol-indophenol, ferricyanide and fumarate can be electron acceptor391765--?
L-aspartate + H2O + O2oxaloacetate + NH3 + H2O2
show the reaction diagram		Escherichia coli-fumarate or succinate can be electron acceptor instead of O2391761, 391762--?
L-aspartate + H2O + O2oxaloacetate + NH3 + H2O2
show the reaction diagram		Escherichia coli-first enzyme of quinolinate synthetase system391756, 391757, 391760--?
L-aspartate + H2O + O2oxaloacetate + NH3 + H2O2
show the reaction diagram		Escherichia coli-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%656090--?
L-aspartate + O2oxaloacetate + NH3 + H2O2
show the reaction diagram		Bacillus subtilisP38032-686712--?
N-acetyl-L-aspartate + O2? + H2O2
show the reaction diagram		Escherichia coli--711324--?
N-formyl-L-aspartate + O2? + H2O2
show the reaction diagram		Escherichia coli--711324--?
L-aspartate + O2iminosuccinate + H2O2
show the reaction diagram		Escherichia coli--711324--?
additional information?-Escherichia coli-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, 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, overview711324---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
L-aspartate + fumarateiminosuccinate + succinate
show the reaction diagram		Escherichia coli--711324--
L-aspartate + H2O + fumarateoxaloacetate + NH3 + succinate
show the reaction diagram		Escherichia coli-it is very likely, that fumarate and not O2 is the physiological electron acceptor in vivo656090--
L-aspartate + H2O + O2oxaloacetate + NH3 + H2O2
show the reaction diagram		Escherichia coli-first enzyme of quinolinate synthetase system391756, 391757, 391760--
L-aspartate + O2iminosuccinate + H2O2
show the reaction diagram		Escherichia coli--711324--
additional information?-Escherichia coli-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-aspartate711324--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
FADEscherichia coli-1 mol of FAD covalently bound per mol of enzyme; flavoprotein391756 2D-image
FADEscherichia coli-flavoprotein391760 2D-image
FADEscherichia coli-1 mol of FAD covalently bound per mol of enzyme391761, 391764 2D-image
FADEscherichia coli--391762, 391763, 656090 2D-image
FADSulfolobus tokodaii--685396 2D-image
FADBacillus subtilisP38032-686712 2D-image
FADEscherichia coli-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 binding711324 2D-image

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
No entries in this field

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
D-AspartateEscherichia coli--711324 2D-image
iodoacetateEscherichia coli--391756 2D-image
L-aspartateEscherichia coli-substrate inactivation391756 2D-image
meso-tartrateEscherichia coli--391756 2D-image
NAD+Gossypium hirsutum-50% at 1 mM391758 2D-image
NAD+Escherichia coli-competitive to FAD391756, 391760 2D-image
TetranitromethaneEscherichia coli--391756 2D-image
UreaEscherichia coli--391756 2D-image

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
2-oxoglutarateGossypium hirsutum, Gossypium hirsutum TM-1, Gossypium hirsutum Zhongmian 35--391759 2D-image
L-aspartateEscherichia coli-substrate activation above 1.0 mM391760 2D-image

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
4.7-3-hydroxy-erythro-L-aspartateEscherichia coli-pH 8.0, 25°C, recombinant wild-type enzyme711324-
1.43-fumarateBacillus subtilisP38032-686712 2D-image
0.038-L-aspartateEscherichia coli-pH 8.0, 25°C, recombinant mutant E121A711324 2D-image
0.048-L-aspartateEscherichia coli-pH 8.0, 25°C, recombinant wild-type enzyme711324 2D-image
0.5-L-aspartateEscherichia coli-at aspartate concentration 1-20 mM391756 2D-image
0.61-L-aspartateEscherichia coli-pH 8.0, 25°C, recombinant mutant E121Q711324 2D-image
0.66-L-aspartateGossypium hirsutum, Gossypium hirsutum TM-1, Gossypium hirsutum Zhongmian 35--391758 2D-image
1-L-aspartateBacillus subtilisP38032using O2 as electron acceptor686712 2D-image
1.3-L-aspartateSulfolobus tokodaii-recombinant enzyme, at 37°C685396 2D-image
2.9-L-aspartateEscherichia coli-pH 8.0, 25°C, recombinant mutant E121K711324 2D-image
4.1-L-aspartateEscherichia coli-at L-aspartate concentration 0.2-1 mM391756 2D-image
26.8-L-aspartateEscherichia coli-pH 8.0, 25°C, recombinant mutant E121D711324 2D-image
3.2-N-acetyl-L-aspartateEscherichia coli-pH 8.0, 25°C, recombinant mutant E121A711324 2D-image
17-N-acetyl-L-aspartateEscherichia coli-pH 8.0, 25°C, recombinant wild-type enzyme711324 2D-image
3.7-N-formyl-L-aspartateEscherichia coli-pH 8.0, 25°C, recombinant wild-type enzyme711324 2D-image
17.5-N-formyl-L-aspartateEscherichia coli-pH 8.0, 25°C, recombinant mutant E121A711324 2D-image

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.173-3-hydroxy-erythro-L-aspartateEscherichia coli-pH 8.0, 25°C, recombinant wild-type enzyme711324-
0.5-fumarateBacillus subtilisP38032-686712 2D-image
0.0333-L-aspartateEscherichia coli--391756 2D-image
0.173-L-aspartateEscherichia coli-pH 8.0, 25°C, recombinant mutant E121A711324 2D-image
0.18-L-aspartateBacillus subtilisP38032using O2 as electron acceptor686712 2D-image
0.202-L-aspartateEscherichia coli-pH 8.0, 25°C, recombinant mutant E121Q711324 2D-image
0.215-L-aspartateEscherichia coli-pH 8.0, 25°C, recombinant mutant E121D711324 2D-image
0.223-L-aspartateEscherichia coli-pH 8.0, 25°C, recombinant mutant E121K711324 2D-image
0.267-L-aspartateEscherichia coli-pH 8.0, 25°C, recombinant wild-type enzyme711324 2D-image
2.6-L-aspartateEscherichia coli-oxygen electron acceptor391761 2D-image
5.55-L-aspartateEscherichia coli-fumarate electron acceptor391761 2D-image
0.0035-N-acetyl-L-aspartateEscherichia coli-pH 8.0, 25°C, recombinant wild-type enzyme711324 2D-image
0.0055-N-acetyl-L-aspartateEscherichia coli-pH 8.0, 25°C, recombinant mutant E121A711324 2D-image
0.0013-N-formyl-L-aspartateEscherichia coli-pH 8.0, 25°C, recombinant mutant E121A711324 2D-image
0.0077-N-formyl-L-aspartateEscherichia coli-pH 8.0, 25°C, recombinant wild-type enzyme711324 2D-image

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.0368-3-hydroxy-erythro-L-aspartateEscherichia coli-pH 8.0, 25°C, recombinant wild-type enzyme7113240
0.35-fumarateBacillus subtilisP38032-68671210622
0.008-L-aspartateEscherichia coli-pH 8.0, 25°C, recombinant mutant E121D71132412113
0.077-L-aspartateEscherichia coli-pH 8.0, 25°C, recombinant mutant E121K71132412113
0.18-L-aspartateBacillus subtilisP38032using O2 as electron acceptor68671212113
0.331-L-aspartateEscherichia coli-pH 8.0, 25°C, recombinant mutant E121Q71132412113
4.55-L-aspartateEscherichia coli-pH 8.0, 25°C, recombinant mutant E121A71132412113
5.56-L-aspartateEscherichia coli-pH 8.0, 25°C, recombinant wild-type enzyme71132412113
0.00021-N-acetyl-L-aspartateEscherichia coli-pH 8.0, 25°C, recombinant wild-type enzyme71132413554
0.0017-N-acetyl-L-aspartateEscherichia coli-pH 8.0, 25°C, recombinant mutant E121A71132413554
7e-05-N-formyl-L-aspartateEscherichia coli-pH 8.0, 25°C, recombinant mutant E121A71132413883
0.00208-N-formyl-L-aspartateEscherichia coli-pH 8.0, 25°C, recombinant wild-type enzyme71132413883

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
3.2-Pyrococcus horikoshii--391765
additional information-Escherichia coli--391756, 391760
additional information-Sulfolobus tokodaii-the specific activity of the purified enzyme is estimated to be 0.7 units/mg at 37°C685396

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
8-Escherichia coli-assay at391757
8-Sulfolobus tokodaii-around pH 8.0685396
8-Bacillus subtilisP38032assay at686712
8-Escherichia coli-assay at711324
8.6-Pyrococcus horikoshii--391765

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
25-Bacillus subtilisP38032assay at686712
25-Escherichia coli-assay at711324
40-Escherichia coli-at pH 8.0391756
90-Pyrococcus horikoshii--391765

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
callusGossypium hirsutum--391758Manually annotated by BRENDA team
seedlingArabidopsis thaliana--676612Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
chloroplastArabidopsis thaliana--9507676612Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
1knp, downloadSCOP (1knp)CATH (1knp)Escherichia coli (strain K12)
1knr, downloadSCOP (1knr)CATH (1knr)Escherichia coli (strain K12)
2e5v, downloadSCOP (2e5v)CATH (2e5v)Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
1j5p, downloadSCOP (1j5p)CATH (1j5p)Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
47000-Sulfolobus tokodaii-gel filtration685396
52000-Sulfolobus tokodaii-recombinant enzyme, SDS-PAGE685396
52580-Sulfolobus tokodaii-calculated from the amino acid sequence685396
55000-Bacillus subtilisP38032monomer, gel filtration686712
60280-Escherichia coli-sequence analysis391757
83000-Gossypium hirsutum, Gossypium hirsutum TM-1, Gossypium hirsutum Zhongmian 35-gel filtration391758
115000-Bacillus subtilisP38032dimer, gel filtration686712
151000-Pyrococcus horikoshii-gel filtration391765

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
dimerBacillus subtilisP38032gel filtration, 2 * 55000 Da, dimer in the absence of NaCl686712
monomerEscherichia coli-1 * 60000, SDS-PAGE391756
monomerSulfolobus tokodaii-1 * 47000, gel filtration685396
trimerPyrococcus horikoshii-3 * 51000, SDS-PAGE391765
monomerBacillus subtilisP38032gel filtration, monomer in the presence of 150 mM NaCl686712
additional informationEscherichia coli-three dimensional structure of holo-wild-type-LASPO, modelling, overview711324

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
Laspo R386LEscherichia coliP10902391763
sitting drop vapour diffusion method with 23% (w/v) polyethylene glycol 8000, 0.2 M MgCl2 and 0.1 M Tris/HCl buffer (pH 8.6)Sulfolobus tokodaii-685396

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
3.710.3Sulfolobus tokodaii-when heated at 50 °C for 30 min, the enzyme does not lose activity at pH values from 3.7 to 10.3685396

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
80-Sulfolobus tokodaii-the enzyme retains more than 90% of its activity when heated for 10 min at 80°C, the enzyme retains 70% of its activity after incubation for 1 h at 80°C685396

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
urea, 7 M, denaturationEscherichia coli-391756
stable at 4°C for at least 2 months without loss of activityPyrococcus horikoshii, Pyrococcus horikoshii ATCC 700860D-5TM, Pyrococcus horikoshii OT-3-391765

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
using NH4SO4 precipitation and using a DEAE-sepharose columnBacillus subtilisP38032686712
-Escherichia coli-391756, 391757, 391760
overexpression in Escherichia coliEscherichia coli-391761, 391762, 391764
-Gossypium hirsutum-391758
overexpression in Escherichia coliPyrococcus horikoshii-391765
ammonium sulfate precipitation and Butyl Toyopearl column chromatographySulfolobus tokodaii-685396

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
expressed in Escherichia coli mutants deficient in AO, transformation of the heterozygous plants with a vector that constitutively expresses the wild-type AO protein fused to GFP at the C terminusArabidopsis thaliana-676612
expressed in Escherichia coliBacillus subtilisP38032686712
-Escherichia coli-391757
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)Escherichia coli-711324
expressed in Escherichia coli strain BL21(DE3) codon plus RILSulfolobus tokodaii-685396

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
E121AEscherichia coli-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-aspartate711324
E121DEscherichia coli-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-aspartate711324
E121KEscherichia coli-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-aspartate711324
E121QEscherichia coli-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-aspartate711324
H244AEscherichia coli-binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate391762
H244SEscherichia coli-binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate391762
H351AEscherichia coli-binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate391762
R386LEscherichia coli-binds substrate analogues with higher dissociation constants and presens lower kcat/Km values in the reduction of fumarate391762
additional informationArabidopsis thaliana-T-DNA-based disruption of the L-Asp oxidase gene is embryo lethal676612
H351SEscherichia coli-binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate391762
additional informationEscherichia coli-mutant reduces affinity to FAD391764

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
additional informationArabidopsis thaliana-is essential for plant growth and development676612

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISM (UNIPROT ACCESSION NO.)LINK TO PUBMEDSOURCE
391756Seifert, 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 oxidaseBiol. Chem. Hoppe-Seyler371239-2481990Escherichia coli PubMed
391757Flachmann, 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 nadBEur. J. Biochem.175221-2291988Escherichia coli PubMed
391758Hosokawa, Y.; Mitchell, E.; Gholson, R.K.Higher plants contain L-asparate oxidase, the first enzyme of the Escherichia coli quinolinate synthetase systemBiochem. Biophys. Res. Commun.111188-1931983Gossypium hirsutum PubMed
391759Wilder, 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 transaminaseBiochem. Biophys. Res. Commun.123836-8411984Gossypium hirsutum PubMed
391760Nasu, S.; Wicks, F.D.; Gholson, R.K.L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetaseJ. Biol. Chem.257626-6321982Escherichia coli PubMed
391761Tedeschi, 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 activityEur. J. Biochem.239427-4331996Escherichia coli PubMed
391762Tedeschi, 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 reductionBiochemistry404738-47442001Escherichia coli PubMed
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LINKS TO OTHER DATABASES (specific for EC-Number 1.4.3.16)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)