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Information on EC 1.4.3.16 - L-aspartate oxidase and Organism(s) Escherichia coli and UniProt Accession P10902
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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 taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
l-aspartate oxidase, laspo, tl-laspo, stlaspo, l-asp oxidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
LASPO
oxidase, L-aspartate
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additional information
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LASPO belongs to the succinate dehydrogenase/fumarate reductase family
LASPO
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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-
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oxidation
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-
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reduction
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oxidative deamination
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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].
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
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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 + 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 + 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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?
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. 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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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-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
-
-
?
L-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
first enzyme of quinolinate synthetase system
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-
?
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
-
-
?
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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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
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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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.7
3-hydroxy-erythro-L-aspartate
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pH 8.0, 25°C, recombinant wild-type enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.173
3-hydroxy-erythro-L-aspartate
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pH 8.0, 25°C, recombinant wild-type enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0368
3-hydroxy-erythro-L-aspartate
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pH 8.0, 25°C, recombinant wild-type enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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NadB has structurally evolved from succinate dehydrogenase/fumarate reductase-type enzymes to gain the new functionality of oxidizing amino acids while retaining the ability to reduce fumarate
physiological function
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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
additional information
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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
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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three dimensional structure of holo-wild-type-LASPO, modelling, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E121A
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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
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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
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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
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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
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binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate
H244S
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binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate
H351A
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binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate
H351S
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binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate
R386L
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binds substrate analogues with higher dissociation constants and presens lower kcat/Km values in the reduction of fumarate
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Flachmann, R.; Kunz, N.; Seifert, J.; Gutlich, M.; Wientjes, F.J.; Lufer, 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
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
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
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
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)
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
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
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
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