Information on EC 1.4.1.21 - aspartate dehydrogenase

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The expected taxonomic range for this enzyme is: Archaea, Bacteria

EC NUMBER
COMMENTARY hide
1.4.1.21
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RECOMMENDED NAME
GeneOntology No.
aspartate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-aspartate + H2O + NAD(P)+ = oxaloacetate + NH3 + NAD(P)H + H+
show the reaction diagram
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
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redox reaction
-
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reduction
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
-
-
NAD metabolism
-
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Nicotinate and nicotinamide metabolism
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SYSTEMATIC NAME
IUBMB Comments
L-aspartate:NAD(P)+ oxidoreductase (deaminating)
The enzyme is strictly specific for L-aspartate as substrate. Catalyses the first step in NAD biosynthesis from aspartate. The enzyme has a higher affinity for NAD+ than NADP+ [1].
CAS REGISTRY NUMBER
COMMENTARY hide
37278-97-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
subsp. pneumoniae, gene KPN_03362
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Manually annotated by BRENDA team
Rhizobium lupini
strain 359a, bacteroids, from nodules of Lupinus luteus
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Manually annotated by BRENDA team
Rhizobium lupini 359a
strain 359a, bacteroids, from nodules of Lupinus luteus
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
physiological function
additional information
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(P)+
oxaloacetate + NH3 + NAD(P)H + H+
show the reaction diagram
L-aspartate + H2O + NAD+
oxaloacetate + NH3 + NADH + H+
show the reaction diagram
L-aspartate + H2O + NADP+
oxaloacetate + NH3 + NADPH + H+
show the reaction diagram
L-aspartate + NAD(P)+
oxaloacetate + NH4+ + NAD(P)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
L-aspartate + NADP+ + H2O
oxaloacetate + NH4+ + NADPH
show the reaction diagram
-
-
-
?
oxaloacetate + NAD(P)H + NH4+
L-aspartate + NAD(P)+
show the reaction diagram
-
-
-
-
oxaloacetate + NH3 + NADH + H+
L-aspartate + H2O + NAD+
show the reaction diagram
oxaloacetate + NH3 + NADPH + H+
L-aspartate + H2O + NADP+
show the reaction diagram
oxaloacetate + NH4+ + NADH
L-aspartate + NAD+ + H2O
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
L-aspartate + NAD(P)+
oxaloacetate + NH4+ + NAD(P)H
show the reaction diagram
Q9X1X6
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-
-
-
L-aspartate + NADP+ + H2O
oxaloacetate + NH4+ + NADPH
show the reaction diagram
-
-
-
?
oxaloacetate + NAD(P)H + NH4+
L-aspartate + NAD(P)+
show the reaction diagram
Q9X1X6
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oxaloacetate + NH4+ + NADH
L-aspartate + NAD+ + H2O
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
K+
-
potassium ion in phosphate buffer may be inhibitory
L-Malate
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competitive
NH4+
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competitive
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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unaffected by EDTA, CaCl2, NiCl2, CoCl2, CuSO4 or ZnCl2
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.067 - 1.2
L-Asp
0.19 - 27
L-aspartate
0.11 - 10
NAD+
0.014 - 4.5
NADH
0.102 - 7.43
NADP+
0.032 - 0.21
NADPH
4.3 - 167
NH3
1.2 - 21
oxaloacetate
additional information
additional information
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Michaelis-Menten kinetics
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.78 - 4.9
L-Asp
2.86 - 59.7
L-aspartate
0.78
L-aspartate with NAD
Thermotoga maritima
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+/- 0.02, with NAD+
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1.2 - 62.9
NAD+
5.2 - 70.5
NADH
2.33 - 46.1
NADP+
19 - 80.2
NADPH
10.3 - 77.6
NH3
14.2 - 71.6
oxaloacetate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.21 - 12.3
L-aspartate
0.23 - 133.8
NAD+
1.1 - 1567
NADH
23 - 98.1
NADP+
90 - 1542
NADPH
0.91 - 6.14
NH3
1.5 - 32.3
oxaloacetate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.02
L-Malate
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+/- 0.48
32.5
NH4+
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+/- 4.9
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.75
Rhizobium lupini
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bacteroid extract of Lupinus luteus nodules
1.63
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+/- 0.15, L-aspartate with NAD+
3.1
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purified recombinant enzyme, with L-aspartate and NADP+, pH 9.8, 28C
3.36
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+/- 0.25, NAD+ with L-aspartate
4.2
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purified recombinant enzyme, with L-aspartate and NADP+, pH 9.8, 28C
9.51
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+/- 0.17, L-aspartate with NADP+
12.32
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+/- 0.88, NADP+ with L-aspartate
147
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purified enzyme, substrate oxaloacetate, pH 8.2, 37C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
Rhizobium lupini
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7
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in Tris-HCl buffer, oxidative deamination of L-aspartate
8 - 9
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amination
8
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in potassium phosphate buffer, oxidative deamination of L-aspartate
8
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oxaloacetate amination; oxaloacetate animation
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 10.5
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L-aspartate oxidation; L-Asp oxidation
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 60
activity range, profile overview
PDB
SCOP
CATH
ORGANISM
UNIPROT
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48000
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gel filtration
60000
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gel filtration
124000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
tetramer
x-ray crystallography
additional information
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
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stable
724068
5.8 - 7.2
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stable
724068, 724591
5.8 - 6.6
stable
724068
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
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up to 20C, 10 min, Tris-HCl buffer, pH 7.5, stable
35
20 min, fully stable up to
50
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10 min, Tris-HCl buffer, pH 7.5, 70% loss of activity
55
20 min, inactivation
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme activity in Tris-HCl buffer is about 7fold higher than in potassium phosphate buffer
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, 5% glycerol, 0.5 M NaCl, pH 7.5, no loss in activity after several months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
about 500fold
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recombinant enzyme from Escherichia coli strain BL21 (DE3) to homogeneity
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recombinant His-tagged enzyme 28fold from Escherichia coli by nickel affinity chromatography
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recombinant His-tagged enzyme 5fold from Escherichia coli by nickel affinity chromatography
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recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
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to homogeneity by heat treatment and affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
AspDH gene cluster, gene AspDH expression in Escherichia coli strain BL21(DE3), quantitative real-time PCR expression analysis
DNA and amino acid sequence determination and analysis, expression of His-tagged enzyme in Escherichia coli
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
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gene KPN_03362, DNA and amino acid sequence determination and analysis
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gene nadX, phylogenetic analysis
gene nadX, the gene forms an operon with the NAD biosynthesis genes nadA and nadC
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ligated into the expression vector pET11a, expression in Escherichia coli strain BL21(DE3)
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ORF PA3505, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli strain BL21 (DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
synthesis
additional information
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first report of an archaeal L-aspartate dehydrogenase, within the archaeal domain, homologues in many methanogenic species, but not in Thermococcales or Sulfolobales species
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