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Information on EC 1.4.1.21 - aspartate dehydrogenase
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EC Tree
1.4.1.21 aspartate dehydrogenaseIUBMB 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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Word Map
- 1.4.1.21
- analysis
- synthesis
- oxaloacetate
- dehydrogenases
-
thermotoga
- maritima
-
dehydrogenation
- fulgidus
- palustris
-
archaeoglobus
-
rhodopseudomonas
- eutropha
-
ammonia-lyase
- d-aspartate
-
electrocardiogram
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
+
+
=
+
+
+
Synonyms
aspartate dehydrogenase, l-aspdh, aspdh, l-aspartate dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AspDH
-
-
-
-
L-aspartate dehydrogenase
L-aspartate:NAD(P)+ oxidoreductase (deaminating)
-
-
-
-
L-aspDH
NAD-dependent aspartate dehydrogenase
NADH2-dependent aspartate dehydrogenase
NADP+-dependent aspartate dehydrogenase
nadX
-
-
-
-
L-aspartate dehydrogenase
-
-
-
-
NAD-dependent aspartate dehydrogenase
-
-
-
-
NADH2-dependent aspartate dehydrogenase
-
-
-
-
NADP+-dependent aspartate dehydrogenase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-iminosuccinate + H2O = oxaloacetate + NH3
(1b), spontaneous
-
-
-
L-aspartate + H2O + NAD(P)+ = oxaloacetate + NH3 + NAD(P)H + H+
overall reaction
-
-
-
L-aspartate + NAD(P)+ = 2-iminosuccinate + NAD(P)H + H+
(1a)
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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+.
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CAS REGISTRY NUMBER
COMMENTARY
37278-97-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-aspartate + NAD(P)+ + H2O
oxaloacetate + NH4+ + NAD(P)H
-
the enzyme shows pro-R (A-type) stereospecificity for hydrogen transfer from the C4 position of the nicotinamide moiety ofNADH
-
-
?
2-oxoglutarate + NH3 + NAD(P)H + H+
L-glutamate + H2O + NAD(P)+
-
-
-
?
2-oxoglutarate + NH3 + NAD(P)H + H+
L-glutamate + H2O + NAD(P)+
-
-
-
-
?
2-oxoglutarate + NH3 + NAD(P)H + H+
L-glutamate + H2O + NAD(P)+
Klebsiella pneumoniae 34618
-
-
-
-
?
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
-
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
-
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
-
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
-
-
-
?
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
-
-
-
-
?
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
-
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
-
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
-
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
-
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
-
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
-
-
-
-
r
L-aspartate + H2O + NAD+
oxaloacetate + NH3 + NADH + H+
-
-
-
-
r
L-aspartate + H2O + NAD+
oxaloacetate + NH3 + NADH + H+
-
-
-
r
L-aspartate + H2O + NAD+
oxaloacetate + NH3 + NADH + H+
-
-
-
-
r
L-aspartate + H2O + NAD+
oxaloacetate + NH3 + NADH + H+
-
-
-
-
r
L-aspartate + H2O + NAD+
oxaloacetate + NH3 + NADH + H+
-
-
-
r
L-aspartate + H2O + NAD+
oxaloacetate + NH3 + NADH + H+
-
the enzyme is capable of utilizing both NAD/H and NADP/H as coenzymes
-
-
r
L-aspartate + H2O + NADP+
oxaloacetate + NH3 + NADPH + H+
-
-
-
-
r
L-aspartate + H2O + NADP+
oxaloacetate + NH3 + NADPH + H+
-
-
-
r
L-aspartate + H2O + NADP+
oxaloacetate + NH3 + NADPH + H+
-
-
-
-
r
L-aspartate + H2O + NADP+
oxaloacetate + NH3 + NADPH + H+
-
-
-
-
r
L-aspartate + H2O + NADP+
oxaloacetate + NH3 + NADPH + H+
-
-
-
r
L-aspartate + H2O + NADP+
oxaloacetate + NH3 + NADPH + H+
-
the enzyme is capable of utilizing both NAD/H and NADP/H as coenzymes
-
-
r
L-aspartate + H2O + NADP+
oxaloacetate + NH3 + NADPH + H+
-
-
-
-
r
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H + H+
-
-
-
?
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H + H+
-
-
-
-
?
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H + H+
Klebsiella pneumoniae 34618
-
-
-
-
?
oxaloacetate + NH3 + NAD(P)H + H+
L-aspartate + H2O + NAD(P)+
-
-
-
?
oxaloacetate + NH3 + NAD(P)H + H+
L-aspartate + H2O + NAD(P)+
-
-
-
-
?
oxaloacetate + NH3 + NADH + H+
L-aspartate + H2O + NAD+
-
-
-
-
r
oxaloacetate + NH3 + NADH + H+
L-aspartate + H2O + NAD+
-
-
-
r
oxaloacetate + NH3 + NADH + H+
L-aspartate + H2O + NAD+
-
-
-
-
r
oxaloacetate + NH3 + NADH + H+
L-aspartate + H2O + NAD+
-
-
-
-
r
oxaloacetate + NH3 + NADH + H+
L-aspartate + H2O + NAD+
-
-
-
r
oxaloacetate + NH3 + NADH + H+
L-aspartate + H2O + NAD+
-
the enzyme is capable of utilizing both NAD/H and NADP/H as coenzymes
-
-
r
oxaloacetate + NH3 + NADPH + H+
L-aspartate + H2O + NADP+
-
-
-
r
oxaloacetate + NH3 + NADPH + H+
L-aspartate + H2O + NADP+
-
the enzyme is capable of utilizing both NAD/H and NADP/H as coenzymes
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-
r
oxaloacetate + NH3 + NADPH + H+
L-aspartate + H2O + NADP+
-
-
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r
oxaloacetate + NH4+ + NADH
L-aspartate + NAD+ + H2O
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strictly specific for oxaloacetate and NADH, not NADPH
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?
oxaloacetate + NH4+ + NADH
L-aspartate + NAD+ + H2O
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biosynthesis of aspartate
-
?
oxaloacetate + NH4+ + NADH
L-aspartate + NAD+ + H2O
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strictly specific for oxaloacetate and NADH, not NADPH
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?
oxaloacetate + NH4+ + NADH
L-aspartate + NAD+ + H2O
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biosynthesis of aspartate
-
?
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
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-
?
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
?
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the enzyme catalyzes in vitro the reductive amination of oxaloacetate to L-aspartate by an order faster than the deamination reaction
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-
?
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
?
-
the wild-type strain synthesizes 3-hydroxy-polybutyrate from fructose or L-Asp, while the enzyme knockout mutant strain does not
-
-
?
additional information
?
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-
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
?
-
-
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
?
-
-
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
?
-
-
the enzyme exhibits a very high specific activity for L-aspartate and oxaloacetate
-
-
?
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
?
-
-
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
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
-
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
-
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
-
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
-
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
-
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
-
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
-
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
-
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
-
-
-
-
r
oxaloacetate + NH4+ + NADH
L-aspartate + NAD+ + H2O
-
biosynthesis of aspartate
-
?
oxaloacetate + NH4+ + NADH
L-aspartate + NAD+ + H2O
-
biosynthesis of aspartate
-
?
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
?
-
the wild-type strain synthesizes 3-hydroxy-polybutyrate from fructose or L-Asp, while the enzyme knockout mutant strain does not
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
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+
-
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+
-
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, the L-AspDH of Klebsiella pneumoniae shows a higher specificity for NADP+ but inactive with NAD+
-
additional information
-
the enzyme is capable of utilizing both NAD/H and NADP/H as coenzymes
-
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INHIBITOR
ORGANISM