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
1.4.1.21
-
RECOMMENDED NAME
GeneOntology No.
aspartate dehydrogenase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-aspartate + H2O + NAD(P)+ = oxaloacetate + NH3 + NAD(P)H + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
redox reaction
-
-
reduction
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
NAD metabolism
-
-
Nicotinate and nicotinamide metabolism
-
-
Metabolic pathways
-
-
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].
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L-aspartate dehydrogenase
-
-
-
-
L-aspartate dehydrogenase
-
-
L-aspartate dehydrogenase
-
-
L-aspartate dehydrogenase
-
L-aspartate dehydrogenase
Cupriavidus necator JMP134
-
-
L-aspartate dehydrogenase
-
-
L-aspartate dehydrogenase
Klebsiella pneumoniae IFO 13541, Klebsiella pneumoniae MGH 78578
-
-
-
L-aspartate dehydrogenase
-
L-aspartate dehydrogenase
-
-
L-aspartate dehydrogenase
-
L-aspDH
Cupriavidus necator JMP134
-
-
L-aspDH
Klebsiella pneumoniae IFO 13541, Klebsiella pneumoniae MGH 78578
-
-
-
NAD-dependent aspartate dehydrogenase
-
-
NAD-dependent aspartate dehydrogenase
-
-
NAD-dependent aspartate dehydrogenase
Rhizobium lupini 359a
-
-
-
NADH2-dependent aspartate dehydrogenase
-
-
NADH2-dependent aspartate dehydrogenase
-
-
NADH2-dependent aspartate dehydrogenase
Rhizobium lupini 359a
-
-
-
NADP+-dependent aspartate dehydrogenase
-
-
CAS REGISTRY NUMBER
COMMENTARY
37278-97-0
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene B3576
UniProt
Manually annotated by BRENDA team
Cupriavidus necator JMP134
-
-
-
Manually annotated by BRENDA team
Cupriavidus necator JMP134
gene B3576
UniProt
Manually annotated by BRENDA team
; subsp. pneumoniae, gene KPN_03362
-
-
Manually annotated by BRENDA team
vitamin B12-producing strain IFO 13541
-
-
Manually annotated by BRENDA team
Klebsiella pneumoniae IFO 13541
-
-
-
Manually annotated by BRENDA team
subsp. pneumoniae, gene KPN_03362
-
-
Manually annotated by BRENDA team
strain 359a, bacteroids, from nodules of Lupinus luteus
-
-
Manually annotated by BRENDA team
Rhizobium lupini 359a
strain 359a, bacteroids, from nodules of Lupinus luteus
-
-
Manually annotated by BRENDA team
gene nadX
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
L-aspartate dehydrogenase is a rare member of amino acid dehydrogenase superfamily
evolution
-
L-AspDH members and other putative homologs share surprisingly low homology, below 10%, with the other amino acid dehydrogenases
evolution
L-AspDH members and other putative homologs share surprisingly low homology, below 10%, with the other amino acid dehydrogenases
evolution
-
L-AspDH members and other putative homologs share surprisingly low homology, below 10%, with the other amino acid dehydrogenases
evolution
Cupriavidus necator JMP134, Klebsiella pneumoniae IFO 13541, Klebsiella pneumoniae MGH 78578
-
L-AspDH members and other putative homologs share surprisingly low homology, below 10%, with the other amino acid dehydrogenases
-
metabolism
-
proposed pathways of L-Asp metabolism, overview
physiological function
-
the amination activity of the enzyme may be important for the fixation of inorganic nitrogen
physiological function
-
involvement of L-AspDH in NAD biosynthesis, overview
physiological function
involvement of L-AspDH in NAD biosynthesis, overview
physiological function
-
involvement of L-AspDH in NAD biosynthesis, overview
physiological function
the wild-type strain synthesizes 3-hydroxy-polybutyrate from fructose or L-Asp, while the enzyme knockout mutant strain does not. The AspDH cluster might be involved in the biosynthesis of poly-3-hydroxyalkanoates
physiological function
Cupriavidus necator JMP134
-
involvement of L-AspDH in NAD biosynthesis, overview; the wild-type strain synthesizes 3-hydroxy-polybutyrate from fructose or L-Asp, while the enzyme knockout mutant strain does not. The AspDH cluster might be involved in the biosynthesis of poly-3-hydroxyalkanoates
-
physiological function
Klebsiella pneumoniae IFO 13541, Klebsiella pneumoniae MGH 78578
-
involvement of L-AspDH in NAD biosynthesis, overview
-
metabolism
Cupriavidus necator JMP134
-
proposed pathways of L-Asp metabolism, overview
-
additional information
-
three-dimensional structure comparisons, overview
additional information
three-dimensional structure comparisons, overview
additional information
-
three-dimensional structure comparisons, overview
additional information
Cupriavidus necator JMP134, Klebsiella pneumoniae IFO 13541, Klebsiella pneumoniae MGH 78578
-
three-dimensional structure comparisons, overview
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
show the reaction diagram
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
show the reaction diagram
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
show the reaction diagram
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
show the reaction diagram
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
show the reaction diagram
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
show the reaction diagram
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
show the reaction diagram
Klebsiella pneumoniae MGH 78578, Cupriavidus necator JMP134
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
show the reaction diagram
Cupriavidus necator JMP134
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
show the reaction diagram
Klebsiella pneumoniae IFO 13541
-
-
-
r
L-aspartate + H2O + NAD+
oxaloacetate + NH3 + NADH + H+
show the reaction diagram
-
-
-
r
L-aspartate + H2O + NAD+
oxaloacetate + NH3 + NADH + H+
show the reaction diagram
-
-
-
r
L-aspartate + H2O + NAD+
oxaloacetate + NH3 + NADH + H+
show the reaction diagram
-
-
r
L-aspartate + H2O + NAD+
oxaloacetate + NH3 + NADH + H+
show the reaction diagram
-
-
r
L-aspartate + H2O + NAD+
oxaloacetate + NH3 + NADH + H+
show the reaction diagram
-
the enzyme is capable of utilizing both NAD/H and NADP/H as coenzymes
-
r
L-aspartate + H2O + NAD+
oxaloacetate + NH3 + NADH + H+
show the reaction diagram
Klebsiella pneumoniae MGH 78578, Cupriavidus necator JMP134
-
-
-
r
L-aspartate + H2O + NAD+
oxaloacetate + NH3 + NADH + H+
show the reaction diagram
Cupriavidus necator JMP134
-
-
r
L-aspartate + H2O + NAD+
oxaloacetate + NH3 + NADH + H+
show the reaction diagram
Klebsiella pneumoniae IFO 13541
-
-
-
r
L-aspartate + H2O + NADP+
oxaloacetate + NH3 + NADPH + H+
show the reaction diagram
-
-
-
r
L-aspartate + H2O + NADP+
oxaloacetate + NH3 + NADPH + H+
show the reaction diagram
-
-
-
r
L-aspartate + H2O + NADP+
oxaloacetate + NH3 + NADPH + H+
show the reaction diagram
-
-
r
L-aspartate + H2O + NADP+
oxaloacetate + NH3 + NADPH + H+
show the reaction diagram
-
-
r
L-aspartate + H2O + NADP+
oxaloacetate + NH3 + NADPH + H+
show the reaction diagram
-
the enzyme is capable of utilizing both NAD/H and NADP/H as coenzymes
-
r
L-aspartate + H2O + NADP+
oxaloacetate + NH3 + NADPH + H+
show the reaction diagram
Klebsiella pneumoniae MGH 78578, Cupriavidus necator JMP134
-
-
-
r
L-aspartate + H2O + NADP+
oxaloacetate + NH3 + NADPH + H+
show the reaction diagram
Cupriavidus necator JMP134
-
-
r
L-aspartate + H2O + NADP+
oxaloacetate + NH3 + NADPH + H+
show the reaction diagram
Klebsiella pneumoniae IFO 13541
-
-
-
r
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 + NAD+
oxaloacetate + NH4+ + NADH
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
-
-
-
oxaloacetate + NH3 + NADH + H+
L-aspartate + H2O + NAD+
show the reaction diagram
-
-
-
r
oxaloacetate + NH3 + NADH + H+
L-aspartate + H2O + NAD+
show the reaction diagram
-
-
-
r
oxaloacetate + NH3 + NADH + H+
L-aspartate + H2O + NAD+
show the reaction diagram
-
-
r
oxaloacetate + NH3 + NADH + H+
L-aspartate + H2O + NAD+
show the reaction diagram
-
-
r
oxaloacetate + NH3 + NADH + H+
L-aspartate + H2O + NAD+
show the reaction diagram
-
the enzyme is capable of utilizing both NAD/H and NADP/H as coenzymes
-
r
oxaloacetate + NH3 + NADH + H+
L-aspartate + H2O + NAD+
show the reaction diagram
Klebsiella pneumoniae MGH 78578, Cupriavidus necator JMP134
-
-
-
r
oxaloacetate + NH3 + NADH + H+
L-aspartate + H2O + NAD+
show the reaction diagram
Cupriavidus necator JMP134
-
-
r
oxaloacetate + NH3 + NADH + H+
L-aspartate + H2O + NAD+
show the reaction diagram
Klebsiella pneumoniae IFO 13541
-
-
-
r
oxaloacetate + NH3 + NADPH + H+
L-aspartate + H2O + NADP+
show the reaction diagram
-
-
-
r
oxaloacetate + NH3 + NADPH + H+
L-aspartate + H2O + NADP+
show the reaction diagram
-
-
-
r
oxaloacetate + NH3 + NADPH + H+
L-aspartate + H2O + NADP+
show the reaction diagram
-
-
r
oxaloacetate + NH3 + NADPH + H+
L-aspartate + H2O + NADP+
show the reaction diagram
-
-
r
oxaloacetate + NH3 + NADPH + H+
L-aspartate + H2O + NADP+
show the reaction diagram
-
the enzyme is capable of utilizing both NAD/H and NADP/H as coenzymes
-
r
oxaloacetate + NH4+ + NADH
L-aspartate + NAD+ + H2O
show the reaction diagram
-
strictly specific for oxaloacetate and NADH, not NADPH, biosynthesis of aspartate
-
?
oxaloacetate + NH4+ + NADH
L-aspartate + NAD+ + H2O
show the reaction diagram
Rhizobium lupini 359a
-
strictly specific for oxaloacetate and NADH, not NADPH, biosynthesis of aspartate
-
?
L-aspartate + NADP+ + H2O
oxaloacetate + NH4+ + NADPH
show the reaction diagram
-
-
-
?
additional information
?
-
-
not: D-aspartate, L-glutamate, L-glycine, L-alanine, L-threonine, L-serine, L-leucine, L-isoleucine, L-methionine, L-cysteine, L-proline, L-valine, L-phenylalanine, L-tyrosine, L-tryptophan, L-lysine, L-histidine, L-arginine
-
-
?
additional information
?
-
-
no activity with D-aspartate, L-glutamate, L-alanine, L-leucine, L-phenylalanine, L-proline, glycine, L-serine, L-lysine, L-norvaline, L-norleucine, L-homoserine and L-2-amino-n-butyrate
-
-
-
additional information
?
-
the wild-type strain synthesizes 3-hydroxy-polybutyrate from fructose or L-Asp, while the enzyme knockout mutant strain does not
-
-
-
additional information
?
-
-
AspDH catalysis involves the transfer of pro-R (A-type) hydrogen from the nicotinamide moiety of the reduced coenzyme. AspDHs exhibit a characteristically narrow substrate range, with exclusive activity for L-Asp and oxaloacetate
-
-
-
additional information
?
-
AspDH catalysis involves the transfer of pro-R (A-type) hydrogen from the nicotinamide moiety of the reduced coenzyme. AspDHs exhibit a characteristically narrow substrate range, with exclusive activity for L-Asp and oxaloacetate
-
-
-
additional information
?
-
-
high substrate specificity of aspartate dehydrogenase enzyme
-
-
-
additional information
?
-
-
the enzyme catalyzes in vitro the reductive amination of oxaloacetate to L-aspartate by an order faster than the deamination reaction
-
-
-
additional information
?
-
-
the enzyme exhibits a very high specific activity for L-aspartate and oxaloacetate
-
-
-
additional information
?
-
Klebsiella pneumoniae MGH 78578, Cupriavidus necator JMP134
-
AspDH catalysis involves the transfer of pro-R (A-type) hydrogen from the nicotinamide moiety of the reduced coenzyme. AspDHs exhibit a characteristically narrow substrate range, with exclusive activity for L-Asp and oxaloacetate
-
-
-
additional information
?
-
Cupriavidus necator JMP134
the wild-type strain synthesizes 3-hydroxy-polybutyrate from fructose or L-Asp, while the enzyme knockout mutant strain does not
-
-
-
additional information
?
-
Klebsiella pneumoniae IFO 13541
-
AspDH catalysis involves the transfer of pro-R (A-type) hydrogen from the nicotinamide moiety of the reduced coenzyme. AspDHs exhibit a characteristically narrow substrate range, with exclusive activity for L-Asp and oxaloacetate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
show the reaction diagram
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
show the reaction diagram
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
show the reaction diagram
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
show the reaction diagram
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
show the reaction diagram
Q9HYA4
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
show the reaction diagram
Q46VA0
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
show the reaction diagram
Klebsiella pneumoniae MGH 78578, Cupriavidus necator JMP134
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
show the reaction diagram
Cupriavidus necator JMP134
Q46VA0
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
show the reaction diagram
Klebsiella pneumoniae IFO 13541
-
-
-
r
L-aspartate + NAD(P)+
oxaloacetate + NH4+ + NAD(P)H
show the reaction diagram
Q9X1X6
-
-
-
oxaloacetate + NAD(P)H + NH4+
L-aspartate + NAD(P)+
show the reaction diagram
Q9X1X6
-
-
-
oxaloacetate + NH4+ + NADH
L-aspartate + NAD+ + H2O
show the reaction diagram
Rhizobium lupini, Rhizobium lupini 359a
-
biosynthesis of aspartate
-
?
L-aspartate + NADP+ + H2O
oxaloacetate + NH4+ + NADPH
show the reaction diagram
-
-
-
?
additional information
?
-
Cupriavidus necator, Cupriavidus necator JMP134
Q46VA0
the wild-type strain synthesizes 3-hydroxy-polybutyrate from fructose or L-Asp, while the enzyme knockout mutant strain does not
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
-
specific for NADH
NADP+
-
requires NADP+ as coenzyme
additional information
-
not: NAD+, FMN, FAD
-
additional information
-
not: NADPH
-
additional information
-
the enzyme is capable of utilizing both NAD/H and NADP/H as coenzymes
-
additional information
-
L-AspDH can utilize both NAD+ and NADP+ as a coenzyme, albeit at different efficiencies
-
additional information
-
L-AspDH can utilize both NAD+ and NADP+ as a coenzyme, albeit at different efficiencies, the L-AspDH of Klebsiella pneumoniae shows a higher specificity for NADP+ but inactive with NAD+
-
additional information
L-AspDH can utilize both NAD+ and NADP+ as a coenzyme, albeit at different efficiencies, similar Km values for NADP+ and NAD+
-
additional information
-
L-AspDH can utilize both NAD+ and NADP+ as a coenzyme, albeit at different efficiencies
-
additional information
-
L-AspDH can utilize both NAD+ and NADP+ as a coenzyme, albeit at different efficiencies, approximately 8fold higher Km value for NADP+ over NAD+
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
K+
-
potassium ion in phosphate buffer may be inhibitory
L-Malate
-
competitive
NH4+
-
competitive
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
unaffected by EDTA, CaCl2, NiCl2, CoCl2, CuSO4 or ZnCl2
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.067
L-Asp
-
cofactor NAD+
1.2
L-Asp
-
cofactor: NADP+
0.067
L-aspartate
-
+/- 0.008, with NAD+
0.067
L-aspartate
-
pH and temperature not specified in the publication, with NAD+
0.19
L-aspartate
-
with NAD+ as the electron acceptor
0.19
L-aspartate
-
pH 10.2, 37C, with NAD+
1.2
L-aspartate
-
+/- 0.05, with NADP+
1.2
L-aspartate
-
pH and temperature not specified in the publication, with NADP+
2.3
L-aspartate
-
pH 11.6, 50C, with NAD+
4.3
L-aspartate
-
with NADP+ as the electron acceptor
4.3
L-aspartate
-
pH 10.2, 37C, with NADP+
4.74
L-aspartate
-
pH 9.8, 37C, with NADP+
4.87
L-aspartate
-
pH 9.8, 37C, with NAD+
13.4
L-aspartate
-
pH 9.8, 28C, recombinant enzyme
26.6
L-aspartate
-
pH 11.6, 50C, with NADP+
0.11
NAD+
-
pH 10.2, 37C
0.25
NAD+
-
; +/- 0.02
0.25
NAD+
-
pH and temperature not specified in the publication
0.47
NAD+
-
pH 9.8, 37C
0.97
NAD+
-
pH 11.6, 50C
7
NAD+
-
pH 9.8, 28C, recombinant enzyme
10
NAD+
-
pH 9.8, 28C, recombinant enzyme
0.014
NADH
-
pH not specified in the publication, 37C
0.014
NADH
pH 8.2, 37C
0.045
NADH
-
pH 8.2, 37C
0.061
NADH
-
pH not specified in the publication, 50C
0.25
NADH
-
pH 9.0, 28C, recombinant enzyme
4.5
NADH
-
pH 9.0, 28C, recombinant enzyme
0.102
NADP+
-
pH 9.8, 28C, recombinant enzyme
0.12
NADP+
-
pH 9.8, 28C, recombinant enzyme
0.32
NADP+
-
pH 10.2, 37C
0.47
NADP+
-
pH 9.8, 37C
0.72
NADP+
-
; +/- 0.04
0.72
NADP+
-
pH and temperature not specified in the publication
7.43
NADP+
-
pH 11.6, 50C
0.032
NADPH
-
pH 9.0, 28C, recombinant enzyme
0.052
NADPH
-
pH 8.2, 37C
0.21
NADPH
-
pH 9.0, 28C, recombinant enzyme
4.3
NH3
-
pH 9.0, 28C, recombinant enzyme
10.1
NH3
-
pH 8.2, 37C, with NADH
11.3
NH3
-
pH 9.0, 28C, recombinant enzyme
12.7
NH3
-
pH 8.2, 37C, with NADPH
14.9
NH3
-
pH not specified in the publication, 50C, with NADH
167
NH3
-
pH not specified in the publication, 37C, with NADH
167
NH3
pH 8.2, 37C, with NADH
1.2
oxaloacetate
-
-
1.2
oxaloacetate
-
pH not specified in the publication, 37C, with NADH
1.2
oxaloacetate
pH 8.2, 37C, with NADH
2.12
oxaloacetate
-
pH 8.2, 37C, with NADH
2.32
oxaloacetate
-
pH not specified in the publication, 50C, with NADH
3.14
oxaloacetate
-
pH 8.2, 37C, with NADPH
9.2
oxaloacetate
-
pH 9.0, 28C, recombinant enzyme
21
oxaloacetate
-
pH 9.0, 28C, recombinant enzyme
27
L-aspartate
-
pH 9.8, 28C, recombinant enzyme
additional information
additional information
-
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.78
L-Asp
Thermotoga maritima
-
cofactor NAD+
4.9
L-Asp
Thermotoga maritima
-
cofactor NADP+
2.86
L-aspartate
Rhodopseudomonas palustris
-
pH 9.8, 28C, recombinant enzyme
4.9
L-aspartate
Thermotoga maritima
-
+/- 0.09, with NADP+
7.3
L-aspartate
Bradyrhizobium japonicum
-
pH 9.8, 28C, recombinant enzyme
42.7
L-aspartate
Pseudomonas aeruginosa
-
pH 9.8, 37C, with NADP+
59.7
L-aspartate
Pseudomonas aeruginosa
-
pH 9.8, 37C, with NAD+
0.78
L-aspartate with NAD
Thermotoga maritima
-
+/- 0.02, with NAD+
-
1.2
NAD+
Thermotoga maritima
-
; +/- 0.04, with L-aspartate
1.59
NAD+
Rhodopseudomonas palustris
-
pH 9.8, 28C, recombinant enzyme
3.3
NAD+
Bradyrhizobium japonicum
-
pH 9.8, 28C, recombinant enzyme
62.9
NAD+
Pseudomonas aeruginosa
-
pH 9.8, 37C
5.2
NADH
Rhodopseudomonas palustris
-
pH 9.0, 28C, recombinant enzyme
26.2
NADH
Bradyrhizobium japonicum
-
pH 9.0, 28C, recombinant enzyme
70.5
NADH
Pseudomonas aeruginosa
-
pH 8.2, 37C
2.33
NADP+
Rhodopseudomonas palustris
-
pH 9.8, 28C, recombinant enzyme
6.2
NADP+
Bradyrhizobium japonicum
-
pH 9.8, 28C, recombinant enzyme
7.2
NADP+
Thermotoga maritima
-
; +/- 0.17, with L-aspartate
46.1
NADP+
Pseudomonas aeruginosa
-
pH 9.8, 37C
19
NADPH
Rhodopseudomonas palustris
-
pH 9.0, 28C, recombinant enzyme
41
NADPH
Bradyrhizobium japonicum
-
pH 9.0, 28C, recombinant enzyme
80.2
NADPH
Pseudomonas aeruginosa
-
pH 8.2, 37C
10.3
NH3
Rhodopseudomonas palustris
-
pH 9.0, 28C, recombinant enzyme
24.7
NH3
Bradyrhizobium japonicum
-
pH 9.0, 28C, recombinant enzyme
62
NH3
Pseudomonas aeruginosa
-
pH 8.2, 37C, with NADH
77.6
NH3
Pseudomonas aeruginosa
-
pH 8.2, 37C, with NADPH
14.2
oxaloacetate
Rhodopseudomonas palustris
-
pH 9.0, 28C, recombinant enzyme
48
oxaloacetate
Bradyrhizobium japonicum
-
pH 9.0, 28C, recombinant enzyme
68.4
oxaloacetate
Pseudomonas aeruginosa
-
pH 8.2, 37C, with NADH
71.6
oxaloacetate
Pseudomonas aeruginosa
-
pH 8.2, 37C, with NADPH
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.21
L-aspartate
Rhodopseudomonas palustris
-
pH 9.8, 28C, recombinant enzyme
97
0.28
L-aspartate
Bradyrhizobium japonicum
-
pH 9.8, 28C, recombinant enzyme
97
9.01
L-aspartate
Pseudomonas aeruginosa
-
pH 9.8, 37C, with NADP+
97
12.3
L-aspartate
Pseudomonas aeruginosa
-
pH 9.8, 37C, with NAD+
97
0.23
NAD+
Rhodopseudomonas palustris
-
pH 9.8, 28C, recombinant enzyme
7
0.33
NAD+
Bradyrhizobium japonicum
-
pH 9.8, 28C, recombinant enzyme
7
133.8
NAD+
Pseudomonas aeruginosa
-
pH 9.8, 37C
7
1.1
NADH
Rhodopseudomonas palustris
-
pH 9.0, 28C, recombinant enzyme
8
100
NADH
Bradyrhizobium japonicum
-
pH 9.0, 28C, recombinant enzyme
8
1567
NADH
Pseudomonas aeruginosa
-
pH 8.2, 37C
8
23
NADP+
Rhodopseudomonas palustris
-
pH 9.8, 28C, recombinant enzyme
10
53
NADP+
Bradyrhizobium japonicum
-
pH 9.8, 28C, recombinant enzyme
10
98.1
NADP+
Pseudomonas aeruginosa
-
pH 9.8, 37C
10
90
NADPH
Rhodopseudomonas palustris
-
pH 9.0, 28C, recombinant enzyme
5
1300
NADPH
Bradyrhizobium japonicum
-
pH 9.0, 28C, recombinant enzyme
5
1542
NADPH
Pseudomonas aeruginosa
-
pH 8.2, 37C
5
0.91
NH3
Rhodopseudomonas palustris
-
pH 9.0, 28C, recombinant enzyme
27
5.7
NH3
Bradyrhizobium japonicum
-
pH 9.0, 28C, recombinant enzyme
27
6.11
NH3
Pseudomonas aeruginosa
-
pH 8.2, 37C, with NADPH
27
6.14
NH3
Pseudomonas aeruginosa
-
pH 8.2, 37C, with NADH
27
1.5
oxaloacetate
Rhodopseudomonas palustris
-
pH 9.0, 28C, recombinant enzyme
57
2.3
oxaloacetate
Bradyrhizobium japonicum
-
pH 9.0, 28C, recombinant enzyme
57
22.8
oxaloacetate
Pseudomonas aeruginosa
-
pH 8.2, 37C, with NADPH
57
32.3
oxaloacetate
Pseudomonas aeruginosa
-
pH 8.2, 37C, with NADH
57
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.02
L-Malate
-
+/- 0.48
32.5
NH4+
-
+/- 4.9
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.045
-
pH 7, 30C, crude extract
0.045
-
30C, pH not specified in the publication
0.75
-
bacteroid extract of Lupinus luteus nodules
1.63
-
+/- 0.15, L-aspartate with NAD+
3.1
-
purified recombinant enzyme, with L-aspartate and NADP+, pH 9.8, 28C
3.36
-
+/- 0.25, NAD+ with L-aspartate
4.2
-
purified recombinant enzyme, with L-aspartate and NADP+, pH 9.8, 28C
4.6
-
purified enzyme, at 50 C
4.6
-
50C, pH 11.6
9.51
-
+/- 0.17, L-aspartate with NADP+
12.32
-
+/- 0.88, NADP+ with L-aspartate
127
-
purified enzyme, substrate L-aspartate, pH 8.2, 37C
137
-
37C, pH 10.2
137
37C, pH 10.2
147
-
purified enzyme, substrate oxaloacetate, pH 8.2, 37C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
-
in Tris-HCl buffer, oxidative deamination of L-aspartate
8
-
in potassium phosphate buffer, oxidative deamination of L-aspartate
8
-
oxaloacetate amination; oxaloacetate animation
8.2
-
amination
9.8
-
L-aspartate oxidation; L-Asp oxidation
10.2
-
deamination
11.6
-
deamination
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8 - 10.5
-
L-aspartate oxidation; L-Asp oxidation
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
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
LITERATURE
48000
-
gel filtration
672387
60000
-
gel filtration
724055
124000
-
gel filtration
652990
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
crystal structure; from crystal structure
dimer
-
x-ray crystallography
dimer
-
2 * 27920, sequence calculation, 2 * 28000, SDS-PAGE
homodimer
-
2 * 62000, SDS-PAGE
homodimer
-
2 * 26000, SDS-PAGE, 2 * 26208, sequence analysis
homodimer
-
2 * 26000
homodimer
-
2 * 28000
homodimer
-
2 * 27000, about, sequence calculation; three-dimensional structure comparisons, overview
homodimer
2 * 28000
homodimer
-
2 * 27000
homodimer
2 * 28000, SDS-PAGE
homodimer
Cupriavidus necator JMP134
-
2 * 28000; 2 * 28000, SDS-PAGE
-
tetramer
x-ray crystallography
homodimer
Klebsiella pneumoniae IFO 13541, Klebsiella pneumoniae MGH 78578
-
2 * 27000, about, sequence calculation; three-dimensional structure comparisons, overview
-
additional information
-
enzyme homology modeling, overview
additional information
-
three-dimensional structure comparisons, overview
additional information
three-dimensional structure comparisons, overview
additional information
-
three-dimensional structure comparisons, overview
additional information
Cupriavidus necator JMP134, Klebsiella pneumoniae IFO 13541, Klebsiella pneumoniae MGH 78578
-
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
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
LITERATURE
4.5 - 11.5
-
stable
724068
5.8 - 6.6
stable
724068
5.8 - 7.2
-
stable
724068, 724591
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
-
up to 20C, 10 min, Tris-HCl buffer, pH 7.5, stable
652990
35
20 min, fully stable up to
724591
48
-
20 min, Tm of purified enzyme
724055
48
20 min, Tm of purified enzyme
724068
49
-
20 min, Tm of purified enzyme
724068, 724591
49
20 min, Tm of purified enzyme
724591
50
-
10 min, Tris-HCl buffer, pH 7.5, 70% loss of activity
652990
55
20 min, inactivation
724591
60
-
10 min, Tris-HCl buffer, pH 7.5, 100% loss of activity
652990
60
-
20 min, Tm of purified enzyme in presence of 0.4 M NaCl or 30% glycerol
724055
80
-
stable for 1 h
672387
80
-
above, Tm of purified enzyme
724068
100
-
boiling inactivates
652990
100
the half life at 100C is 10 min
686668
100
-
the half life at 100C is 10.7 min
686668
100
-
half-life is 10 min
724068
100
-
half-life is 10.7 min
724068
additional information
-
thermostability of AfuAspDH is mainly ascribed to the intersubunit ion and aromatic pair interactions in the enzyme
724068
additional information
improving the thermostability of mesophilic AspDHs by the addition of 0.4 M NaCl or 30% glycerol
724068
additional information
-
thermostability of TmaAspDH is mainly ascribed to the intersubunit ion and aromatic pair interactions in the enzyme
724068
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme activity in Tris-HCl buffer is about 7fold higher than in potassium phosphate buffer
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, 5% glycerol, 0.5 M NaCl, pH 7.5, no loss in activity after several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to homogeneity by heat treatment and affinity chromatography
-
recombinant His-tagged enzyme 28fold from Escherichia coli by nickel affinity chromatography
-
about 500fold
-
recombinant enzyme from Escherichia coli strain BL21 (DE3) to homogeneity
-
recombinant His-tagged enzyme 5fold from Escherichia coli by nickel affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
ligated into the expression vector pET11a, expression in Escherichia coli strain BL21(DE3)
-
DNA and amino acid sequence determination and analysis, expression of His-tagged enzyme in Escherichia coli
-
AspDH gene cluster, gene AspDH expression in Escherichia coli strain BL21(DE3), quantitative real-time PCR expression analysis
gene KPN_03362, DNA and amino acid sequence determination and analysis
-
gene nadX, phylogenetic analysis
ORF PA3505, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli strain BL21 (DE3)
-
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
-
gene nadX, the gene forms an operon with the NAD biosynthesis genes nadA and nadC
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
construction of an AspDH knockout strain, growth phenotype, compared to the wild-type
additional information
Cupriavidus necator JMP134
-
construction of an AspDH knockout strain, growth phenotype, compared to the wild-type
-
additional information
-
establishing of a L-Asp production system consisting of PaeAspDH, Bacillus subtilis malate dehydrogenase and Escherichia coli fumarase, achieving a high level of L-Asp production from fumarate in fed-batch process with a molar conversion yield of 89.4% in LB medium supplemented with fumarate, and 100 mM NH4Cl, overview, or in the same production system with glucose M9 minimal medium containing 50 mM glucose and 80 mM urea as carbon and nitrogen source, respectively
additional information
L-Asp production system consisting of PaeAspDH, Bacillus subtilis malate dehydrogenase and Escherichia coli fumarase, achieving a high level of L-Asp production from fumarate in fed-batch process with a molar conversion yield of 89.4% in LB medium supplemented with fumarate, and 100 mM NH4Cl, overview, or in the same production system with glucose M9 minimal medium containing 50 mM glucose and 80 mM urea as carbon and nitrogen source, respectively
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
analysis
Cupriavidus necator JMP134
-
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
Cupriavidus necator JMP134
-
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
-
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
analysis
Klebsiella pneumoniae IFO 13541
-
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
Klebsiella pneumoniae IFO 13541
-
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
-
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
-
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
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
analysis
-
development of a genetically encoded fluorescent protein construct for monitoring of L-Asp in vitro, and employment of aspartate dehydrogenase scaffold as a biorecognition element
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
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
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