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Enzyme Nomenclature
Information on EC 1.4.3.16 - L-aspartate oxidase
for references in articles please use BRENDA:EC1.4.3.16
Word Map on EC 1.4.3.16
- 1.4.3.16
- quinolinate
- dinucleotide
- fumarate
-
nada
- iminoaspartate
- nicotinamide
- pyridine
-
flavoproteins
- dihydroxyacetone
-
flavoenzyme
-
fad-binding
- biotechnology
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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EC NUMBER 
COMMENTARY 
1.4.3.16
-
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RECOMMENDED NAME
GeneOntology No.
L-aspartate oxidase
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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
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
although the enzyme mutation dramatically affects NADPH oxidase RBOHD function, it does not affect functions carried out by other members of the RBOH family, such as RBOHC and RBOHF
metabolism
-
the enzyme catalyzes the first irreversible step in the de novo biosynthesis of NAD+
physiological function
additional information
physiological function
NadB 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 activity
physiological function
-
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 acceptor
physiological function
-
the enzyme is required for the reactive oxygen species burst mediated by the NADPH oxidase RBOHD triggered by the perception of several unrelated pathogen-associated molecular patterns. The enzyme is also required for RBOHD-dependent stomatal closure. The enzyme is required for stomatal immunity against the bacterium Pseudomonas syringa
additional information
-
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 enzymes
additional information
-
full enzyme activity is not required for flg22-induced responses that are NADPH oxidase RBOHD-independent
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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
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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
-
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
KC333624, Q972D2
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
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-
-
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
?
-
-
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
-
-
-
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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-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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-aspartate + H2O + fumarate
oxaloacetate + NH3 + succinate
-
it is very likely, that fumarate and not O2 is the physiological electron acceptor in vivo
-
-
?
L-glutamate + H2O + O2
2-oxopentanedioate + NH3 + H2O2
-
low activity
-
-
?
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
KC333624, Q972D2
the enzyme oxidizes L-aspartate to iminosuccinate, which is then non-enzymatically hydrolyzed to oxaloacetate
-
-
?
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
-
-
-
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
KC333624
contains 1 FAD per protein monomer; FAD-containing flavoprotein, tight binding of the FAD cofactor
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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
8.8 - 12
KC333624
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
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 95
KC333624
40°C: about 50% of maximal activity, 95°C: about 60% of maximal activity
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
51000
60000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
trimer
additional information
-
three dimensional structure of holo-wild-type-LASPO, modelling, overview
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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)
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.7 - 10.3
-
when heated at 50 °C for 30 min, the enzyme does not lose activity at pH values from 3.7 to 10.3
685396
7 - 10
KC333624
60 min, stable; no significant change in activity is observed up to 400 min of incubation at pH 7.5. More than 70% of the initial activity is recovered after 60 min at 37°C. Below pH 8.0 and above pH 10.0, a significant time-dependent inactivation is apparent
721394
8 - 11
-
when compared to the free enzyme form, the immobilized enzyme shows a full stability at pH values 9.0-11.0 after 60 min of incubation, while for the free enzyme the stability strongly decreases at pH above 8.0
743783
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
KC333624
more than 70% of the initial activity is recovered after 60 min at 37°C
40 - 50
-
the enzyme is stable for 60 min at up to 40°C, but rapid losses in activity are observed at 50°C after 5 min
80
80
-
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°C
80
KC333624
stable up to; the enzyme is fully stable up to 80°C (400 min). When the temperature is increased to above 85°C, a sharp decrease in enzyme stability is apparent and the activity is lost in about 100 min at 100°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
after 96 h of incubation, 82% of the initial enzymatic activity is maintained in the presence of 1 or 10 mM H2O2 vs. 86% in the absence of hydrogen
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°, purified enzyme at pH 7.5, several months, nploss of activity
KC333624
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; HiTrap nickel chelating affinity column chromatography, and Superdex 200 gel filtration
KC333624
ammonium sulfate precipitation and Butyl Toyopearl column chromatography
-
HiTrap nickel chelating column chromatography and Superdex 75 gel filtration
-
overexpression in Escherichia coli
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells; expression in Escherichia coli in the active form as holoenzyme
KC333624
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 terminus
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
-
T-DNA-based disruption of the L-Asp oxidase gene is embryo lethal
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
KC333624
StLASPO represents an appropriate biocatalyst for the resolution of racemic solutions of D,L-aspartate and a well-suited protein scaffold to evolve a L-amino acid oxidase activity by protein engineering
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