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 ACCESSION NO.
LITERATURE
L-aspartate + H2O + NAD(P)+ = oxaloacetate + NH3 + NAD(P)H + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
redox reaction
-
-
reduction
-
-
PATHWAY
KEGG Link
MetaCyc Link
Metabolic pathways
-
Nicotinate and nicotinamide metabolism
-
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 ACCESSION NO.
COMMENTARY
LITERATURE
L-aspartate dehydrogenase
-
-
-
-
L-aspartate dehydrogenase
-
-
L-aspartate dehydrogenase
-
-
L-aspartate dehydrogenase
Q46VA0
-
L-aspartate dehydrogenase
Cupriavidus necator JMP134
-, Q46VA0
-
-
L-aspartate dehydrogenase
-
-
L-aspartate dehydrogenase
Klebsiella pneumoniae IFO 13541, Klebsiella pneumoniae MGH 78578
-
-
-
L-aspartate dehydrogenase
Q9HYA4
-
L-aspartate dehydrogenase
-
-
L-aspartate dehydrogenase
Q9X1X6
-
L-aspDH
Q46VA0
-
L-aspDH
Cupriavidus necator JMP134
-, Q46VA0
-
-
L-aspDH
Klebsiella pneumoniae IFO 13541, Klebsiella pneumoniae MGH 78578
-
-
-
L-aspDH
Q9HYA4
-
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
SEQUENCE CODE
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 ACCESSION NO.
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
Q9HYA4
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
Q9HYA4
involvement of L-AspDH in NAD biosynthesis, overview
physiological function
-
involvement of L-AspDH in NAD biosynthesis, overview
physiological function
-, Q46VA0
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
Q9HYA4
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 ACCESSION NO.
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 + 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
Q9HYA4
-
-
-
r
L-aspartate + H2O + NAD+
oxaloacetate + NH3 + NADH + H+
show the reaction diagram
-, Q46VA0
-
-
-
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
Q46VA0
-
-
-
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
Q9HYA4
-
-
-
r
L-aspartate + H2O + NADP+
oxaloacetate + NH3 + NADPH + H+
show the reaction diagram
-, Q46VA0
-
-
-
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
Q46VA0
-
-
-
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
Q9X1X6, -
-
-
-
-
L-aspartate + NAD(P)+
oxaloacetate + NH4+ + NAD(P)H
show the reaction diagram
Q9X1X6, -
-
-
-
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
-, O28440
-
-
-
?
L-aspartate + NAD+
oxaloacetate + NH4+ + NADH
show the reaction diagram
-
-
-
-
?
oxaloacetate + NAD(P)H + NH4+
L-aspartate + NAD(P)+
show the reaction diagram
Q9X1X6, -
-
-
-
-
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
Q9HYA4
-
-
-
r
oxaloacetate + NH3 + NADH + H+
L-aspartate + H2O + NAD+
show the reaction diagram
-, Q46VA0
-
-
-
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
Q46VA0
-
-
-
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
Q9HYA4
-
-
-
r
oxaloacetate + NH3 + NADPH + H+
L-aspartate + H2O + NADP+
show the reaction diagram
-, Q46VA0
-
-
-
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
?
-
-, Q46VA0
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
?
-
Q9HYA4
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
Q46VA0
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 ACCESSION NO.
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
?
-
-, Q46VA0
the wild-type strain synthesizes 3-hydroxy-polybutyrate from fructose or L-Asp, while the enzyme knockout mutant strain does not
-
-
-
additional information
?
-
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 ACCESSION NO.
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
Q9HYA4
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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
K+
-
potassium ion in phosphate buffer may be inhibitory
L-Malate
-
competitive
NH4+
-
competitive
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
unaffected by EDTA, CaCl2, NiCl2, CoCl2, CuSO4 or ZnCl2
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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+
0.19
-
L-aspartate
Q46VA0
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+
4.3
-
L-aspartate
Q46VA0
pH 10.2, 37C, with NADP+
4.74
-
L-aspartate
-
pH 9.8, 37C, with NADP+
4.74
-
L-aspartate
Q9HYA4
pH 9.8, 37C, with NADP+
4.87
-
L-aspartate
-
pH 9.8, 37C, with NAD+
4.87
-
L-aspartate
Q9HYA4
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
0.11
-
NAD+
Q46VA0
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
0.47
-
NAD+
Q9HYA4
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
-, Q46VA0
pH 8.2, 37C
0.045
-
NADH
-
pH 8.2, 37C
0.045
-
NADH
Q9HYA4
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
0.32
-
NADP+
Q46VA0
pH 10.2, 37C
0.47
-
NADP+
-
pH 9.8, 37C
0.47
-
NADP+
Q9HYA4
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
10.1
-
NH3
Q9HYA4
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
-, Q46VA0
pH 8.2, 37C, with NADH
1.2
-
oxaloacetate
-
-
1.2
-
oxaloacetate
-
pH not specified in the publication, 37C, with NADH
1.2
-
oxaloacetate
-, Q46VA0
pH 8.2, 37C, with NADH
2.12
-
oxaloacetate
-
pH 8.2, 37C, with NADH
2.12
-
oxaloacetate
Q9HYA4
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]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.78
-
L-Asp
-
cofactor NAD+
4.9
-
L-Asp
-
cofactor NADP+
2.86
-
L-aspartate
-
pH 9.8, 28C, recombinant enzyme
4.9
-
L-aspartate
-
+/- 0.09, with NADP+
7.3
-
L-aspartate
-
pH 9.8, 28C, recombinant enzyme
42.7
-
L-aspartate
-
pH 9.8, 37C, with NADP+
59.7
-
L-aspartate
-
pH 9.8, 37C, with NAD+
0.78
-
L-aspartate with NAD
-
+/- 0.02, with NAD+
-
1.2
-
NAD+
-
; +/- 0.04, with L-aspartate
1.59
-
NAD+
-
pH 9.8, 28C, recombinant enzyme
3.3
-
NAD+
-
pH 9.8, 28C, recombinant enzyme
62.9
-
NAD+
-
pH 9.8, 37C
5.2
-
NADH
-
pH 9.0, 28C, recombinant enzyme
26.2
-
NADH
-
pH 9.0, 28C, recombinant enzyme
70.5
-
NADH
-
pH 8.2, 37C
2.33
-
NADP+
-
pH 9.8, 28C, recombinant enzyme
6.2
-
NADP+
-
pH 9.8, 28C, recombinant enzyme
7.2
-
NADP+
-
; +/- 0.17, with L-aspartate
46.1
-
NADP+
-
pH 9.8, 37C
19
-
NADPH
-
pH 9.0, 28C, recombinant enzyme
41
-
NADPH
-
pH 9.0, 28C, recombinant enzyme
80.2
-
NADPH
-
pH 8.2, 37C
10.3
-
NH3
-
pH 9.0, 28C, recombinant enzyme
24.7
-
NH3
-
pH 9.0, 28C, recombinant enzyme
62
-
NH3
-
pH 8.2, 37C, with NADH
77.6
-
NH3
-
pH 8.2, 37C, with NADPH
14.2
-
oxaloacetate
-
pH 9.0, 28C, recombinant enzyme
48
-
oxaloacetate
-
pH 9.0, 28C, recombinant enzyme
68.4
-
oxaloacetate
-
pH 8.2, 37C, with NADH
71.6
-
oxaloacetate
-
pH 8.2, 37C, with NADPH
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.21
-
L-aspartate
-
pH 9.8, 28C, recombinant enzyme
12113
0.28
-
L-aspartate
-
pH 9.8, 28C, recombinant enzyme
12113
9.01
-
L-aspartate
-
pH 9.8, 37C, with NADP+
12113
12.3
-
L-aspartate
-
pH 9.8, 37C, with NAD+
12113
0.23
-
NAD+
-
pH 9.8, 28C, recombinant enzyme
14330
0.33
-
NAD+
-
pH 9.8, 28C, recombinant enzyme
14330
133.8
-
NAD+
-
pH 9.8, 37C
14330
1.1
-
NADH
-
pH 9.0, 28C, recombinant enzyme
14331
100
-
NADH
-
pH 9.0, 28C, recombinant enzyme
14331
1567
-
NADH
-
pH 8.2, 37C
14331
23
-
NADP+
-
pH 9.8, 28C, recombinant enzyme
27497
53
-
NADP+
-
pH 9.8, 28C, recombinant enzyme
27497
98.1
-
NADP+
-
pH 9.8, 37C
27497
90
-
NADPH
-
pH 9.0, 28C, recombinant enzyme
27498
1300
-
NADPH
-
pH 9.0, 28C, recombinant enzyme
27498
1542
-
NADPH
-
pH 8.2, 37C
27498
0.91
-
NH3
-
pH 9.0, 28C, recombinant enzyme
14472
5.7
-
NH3
-
pH 9.0, 28C, recombinant enzyme
14472
6.11
-
NH3
-
pH 8.2, 37C, with NADPH
14472
6.14
-
NH3
-
pH 8.2, 37C, with NADH
14472
1.5
-
oxaloacetate
-
pH 9.0, 28C, recombinant enzyme
14857
2.3
-
oxaloacetate
-
pH 9.0, 28C, recombinant enzyme
14857
22.8
-
oxaloacetate
-
pH 8.2, 37C, with NADPH
14857
32.3
-
oxaloacetate
-
pH 8.2, 37C, with NADH
14857
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4.02
-
L-Malate
-
+/- 0.48
32.5
-
NH4+
-
+/- 4.9
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
127
-
Q9HYA4
pH 9.8, 37C
137
-
-
37C, pH 10.2
137
-
Q46VA0
37C, pH 10.2
147
-
-
purified enzyme, substrate oxaloacetate, pH 8.2, 37C
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
8.2
-
-, Q46VA0
amination
9.8
-
-
L-aspartate oxidation; L-Asp oxidation
9.8
-
-
deamination
9.8
-
Q9HYA4
deamination
10.2
-
-
deamination
10.2
-
Q46VA0
deamination
11.6
-
-
deamination
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8
10.5
-
L-aspartate oxidation; L-Asp oxidation
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
37
-
-
assay at
50
-
-, Q46VA0
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
60
-, Q46VA0
activity range, profile overview
PDB
SCOP
CATH
ORGANISM
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
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
48000
-
-
gel filtration
60000
-
-
gel filtration
124000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
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
Q9HYA4
2 * 28000
homodimer
-
2 * 27000
homodimer
-, Q46VA0
2 * 28000, SDS-PAGE
homodimer
Cupriavidus necator JMP134
-
2 * 28000; 2 * 28000, SDS-PAGE
-
tetramer
-, O28440
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
Q9HYA4
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 ACCESSION NO.
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
-, O28440
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
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
11.5
-
stable
5.8
6.6
Q9HYA4
stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
-
up to 20C, 10 min, Tris-HCl buffer, pH 7.5, stable
35
-
-, Q46VA0
20 min, fully stable up to
48
-
-
20 min, Tm of purified enzyme
48
-
Q9HYA4
20 min, Tm of purified enzyme
49
-
-
20 min, Tm of purified enzyme
49
-
Q46VA0
20 min, Tm of purified enzyme
50
-
-
10 min, Tris-HCl buffer, pH 7.5, 70% loss of activity
55
-
-, Q46VA0
20 min, inactivation
60
-
-
10 min, Tris-HCl buffer, pH 7.5, 100% loss of activity
60
-
-
20 min, Tm of purified enzyme in presence of 0.4 M NaCl or 30% glycerol
80
-
-
stable for 1 h
80
-
-
above, Tm of purified enzyme
100
-
-
boiling inactivates
100
-
-, O28440
the half life at 100C is 10 min
100
-
-
the half life at 100C is 10.7 min
100
-
-
half-life is 10 min
100
-
-
half-life is 10.7 min
additional information
-
-
thermostability of AfuAspDH is mainly ascribed to the intersubunit ion and aromatic pair interactions in the enzyme
additional information
-
Q9HYA4
improving the thermostability of mesophilic AspDHs by the addition of 0.4 M NaCl or 30% glycerol
additional information
-
-
thermostability of TmaAspDH is mainly ascribed to the intersubunit ion and aromatic pair interactions in the enzyme
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
enzyme activity in Tris-HCl buffer is about 7fold higher than in potassium phosphate buffer
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, 5% glycerol, 0.5 M NaCl, pH 7.5, no loss in activity after several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
LITERATURE
expressed in Escherichia coli
-, O28440
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
-, Q46VA0
gene KPN_03362, DNA and amino acid sequence determination and analysis
-
gene nadX, phylogenetic analysis
Q9HYA4
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 ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-, Q46VA0
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
Q9HYA4
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 ACCESSION NO.
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
Q9HYA4
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
Q9HYA4
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