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Information on EC 1.4.1.21 - aspartate dehydrogenase and Organism(s) Thermotoga maritima and UniProt Accession Q9X1X6

for references in articles please use BRENDA:EC1.4.1.21
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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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Thermotoga maritima
UNIPROT: Q9X1X6
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The taxonomic range for the selected organisms is: Thermotoga maritima
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
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
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 + H2O + NAD+
oxaloacetate + NH3 + NADH + H+
show the reaction diagram
-
-
-
r
L-aspartate + NAD(P)+
oxaloacetate + NH4+ + NAD(P)H
show the reaction diagram
L-aspartate + NAD+
oxaloacetate + NH4+ + NADH
show the reaction diagram
-
-
-
?
oxaloacetate + NAD(P)H + NH4+
L-aspartate + NAD(P)+
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
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 + NAD(P)+
oxaloacetate + NH4+ + NAD(P)H
show the reaction diagram
-
-
-
?
oxaloacetate + NAD(P)H + NH4+
L-aspartate + NAD(P)+
show the reaction diagram
-
-
-
?
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
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-malate
competitive
NH4+
competitive
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.067 - 1.2
L-Asp
0.067 - 1.2
L-aspartate
0.25
NAD+
0.72
NADP+
0.067 - 1.2
L-aspartate
0.25
NAD+
-
pH and temperature not specified in the publication
0.72
NADP+
-
pH and temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.78 - 4.9
L-Asp
0.78 - 4.9
L-aspartate
1.2
NAD+
7.2
NADP+
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.02
L-malate
+/- 0.48
32.5
NH4+
+/- 4.9
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.63
+/- 0.15, L-aspartate with NAD+
12.32
+/- 0.88, NADP+ with L-aspartate
3.36
+/- 0.25, NAD+ with L-aspartate
9.51
+/- 0.17, L-aspartate with NADP+
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 10.5
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
27000
-
2 * 27000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
homodimer
-
2 * 27000
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
the half life at 100°C is 10.7 min
100
-
half-life is 10.7 min
80
-
above, Tm of purified enzyme
additional information
-
thermostability of TmaAspDH is mainly ascribed to the intersubunit ion and aromatic pair interactions in the enzyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 5% glycerol, 0.5 M NaCl, pH 7.5, no loss in activity after several months
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression of N-terminally His-tagged and GFP-tagged enzyme, using the flexible GGSGG linker, in Escherichia coli. The recombinant tagged aspartate dehydrogenase functions as the biorecognition element, and aspartate-induced conformational change is converted to a fluorescence signal by GFP, method, overview
-
gene nadX, the gene forms an operon with the NAD biosynthesis genes nadA and nadC
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yang, Z.; Savchenko, A.; Yakunin, A.; Zhang, R.; Edwards, A.; Arrowsmith, C.; Tong, L.
Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643
J. Biol. Chem.
278
8804-8808
2003
Thermotoga maritima (Q9X1X6), Thermotoga maritima
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
Ozyurt, C.; Evran, S.; Telefoncu, A.
Development of a novel fluorescent protein construct by genetically fusing green fluorescent protein to the N-terminal of aspartate dehydrogenase
Biotechnol. Appl. Biochem.
60
399-404
2013
Thermotoga maritima
Manually annotated by BRENDA team