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Information on EC 1.4.1.21 - aspartate dehydrogenase and Organism(s) Archaeoglobus fulgidus and UniProt Accession O28440

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IUBMB Comments
The enzyme is strictly specific for L-aspartate as substrate. It produces the unstable compound 2-iminosuccinate, which, in the presence of water, hydrolyses spontaneously to form oxaloacetate. The enzyme from some archaea and thermophilic bacteria is likely to transfer 2-iminosuccinate directly to EC 2.5.1.72, quinolinate synthase, preventing its hydrolysis and enabling the de novo biosynthesis of NAD+.
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This record set is specific for:
Archaeoglobus fulgidus
UNIPROT: O28440
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The taxonomic range for the selected organisms is: Archaeoglobus fulgidus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
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L-aspartate
+
H2O
+
NAD(P)+
=
oxaloacetate
+
NH3
+
NAD(P)H
+
H+
+
+
=
+
+
+
Synonyms
aspartate dehydrogenase, l-aspdh, aspdh, l-aspartate dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L-aspartate dehydrogenase
-
AspDH
-
-
-
-
L-aspartate dehydrogenase
L-aspartate:NAD(P)+ oxidoreductase (deaminating)
-
-
-
-
NAD-dependent aspartate dehydrogenase
-
-
-
-
NADH2-dependent aspartate dehydrogenase
-
-
-
-
NADP+-dependent aspartate dehydrogenase
-
-
-
-
nadX
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
L-aspartate:NAD(P)+ oxidoreductase (2-iminosuccinate-forming)
The enzyme is strictly specific for L-aspartate as substrate. It produces the unstable compound 2-iminosuccinate, which, in the presence of water, hydrolyses spontaneously to form oxaloacetate. The enzyme from some archaea and thermophilic bacteria is likely to transfer 2-iminosuccinate directly to EC 2.5.1.72, quinolinate synthase, preventing its hydrolysis and enabling the de novo biosynthesis of NAD+.
CAS REGISTRY NUMBER
COMMENTARY hide
37278-97-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-aspartate + NAD+
oxaloacetate + NH4+ + NADH
show the reaction diagram
-
-
-
?
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
show the reaction diagram
-
-
-
-
r
L-aspartate + H2O + NAD+
oxaloacetate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
r
L-aspartate + H2O + NADP+
oxaloacetate + NH3 + NADPH + H+
show the reaction diagram
-
-
-
-
r
L-aspartate + NAD(P)+ + H2O
oxaloacetate + NH4+ + NAD(P)H
show the reaction diagram
-
the enzyme shows pro-R (A-type) stereospecificity for hydrogen transfer from the C4 position of the nicotinamide moiety ofNADH
-
-
?
L-aspartate + NAD+
oxaloacetate + NH4+ + NADH
show the reaction diagram
-
-
-
-
?
oxaloacetate + NH3 + NADH + H+
L-aspartate + H2O + NAD+
show the reaction diagram
-
-
-
-
r
oxaloacetate + NH3 + NADPH + H+
L-aspartate + H2O + NADP+
show the reaction diagram
-
-
-
-
r
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
show the reaction diagram
-
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
L-AspDH can utilize both NAD+ and NADP+ as a coenzyme, albeit at different efficiencies
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
unaffected by EDTA, CaCl2, NiCl2, CoCl2, CuSO4 or ZnCl2
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.19 - 26.6
L-aspartate
0.11 - 0.97
NAD+
0.014 - 0.061
NADH
0.32 - 7.43
NADP+
14.9
NH3
-
pH not specified in the publication, 50°C, with NADH
1.2 - 2.32
oxaloacetate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
L-AspDH members and other putative homologs share surprisingly low homology, below 10%, with the other amino acid dehydrogenases
physiological function
-
involvement of L-AspDH in NAD biosynthesis, overview
additional information
-
three-dimensional structure comparisons, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26000
26208
-
2 * 26000, SDS-PAGE, 2 * 26208, sequence analysis
48000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
x-ray crystallography
homodimer
additional information
-
three-dimensional structure comparisons, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapour diffusion method with 100 mM phosphate-citrate buffer pH 4.2 (60.5 mM, Na2HPO4, 39.5 mM citric acid), 5% (v/v) polyethylene glycol 3000 (PEG 3000), 10% (v/v) glycerol and 22% (v/v) 1,2-propanediol
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 11.5
-
stable
724068
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
the half life at 100°C is 10 min
100
-
half-life is 10 min
additional information
-
thermostability of AfuAspDH is mainly ascribed to the intersubunit ion and aromatic pair interactions in the enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to homogeneity by heat treatment and affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
ligated into the expression vector pET11a, expression in Escherichia coli strain BL21(DE3)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
usage of AspDH in the quantitative measurement of amino acids, 2-oxo acids, and ammonia or urea in studies involving clinical settings, bioprocess control, and nutrition
synthesis
-
potential application of AspDH for cost-effective and efficient L-Asp production via both fermentative and enzymatic systems. The ability to catalyze stereospecific reactions has also stimulated research interest in amino acid dehydrogenases as biocatalysts to produce synthons for pharmaceutical and food industries, e.g., enantiomerically pure non-natural amino acids as drug precursors
additional information
-
first report of an archaeal L-aspartate dehydrogenase, within the archaeal domain, homologues in many methanogenic species, but not in Thermococcales or Sulfolobales species
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yoneda, K.; Kawakami, R.; Tagashira, Y.; Sakuraba, H.; Goda, S.; Ohshima, T.
The first archaeal L-aspartate dehydrogenase from the hyperthermophile Archaeoglobus fulgidus: Gene cloning and enzymological characterization
Biochim. Biophys. Acta
1764
1087-1093
2006
Archaeoglobus fulgidus
Manually annotated by BRENDA team
Yoneda, K.; Sakuraba, H.; Tsuge, H.; Katunuma, N.; Ohshima, T.
Crystal structure of archaeal highly thermostable L-aspartate dehydrogenase/NAD/citrate ternary complex
FEBS J.
274
4315-4325
2007
Archaeoglobus fulgidus (O28440), Archaeoglobus fulgidus, Thermotoga maritima (Q9X1X6), Thermotoga maritima
Manually annotated by BRENDA team
Li, Y.; Ogola, H.J.; Sawa, Y.
L-aspartate dehydrogenase: features and applications
Appl. Microbiol. Biotechnol.
93
503-516
2012
Archaeoglobus fulgidus, Cupriavidus necator, Cupriavidus necator JMP 134-1, Klebsiella pneumoniae, Klebsiella pneumoniae IFO 13541, Klebsiella pneumoniae MGH 78578, Pseudomonas aeruginosa (Q9HYA4), Thermotoga maritima
Manually annotated by BRENDA team