1.4.1.21: aspartate dehydrogenase
This is an abbreviated version!
For detailed information about aspartate dehydrogenase, go to the full flat file.
Word Map on EC 1.4.1.21
-
1.4.1.21
-
analysis
-
synthesis
-
oxaloacetate
-
dehydrogenases
-
thermotoga
-
maritima
-
dehydrogenation
-
fulgidus
-
palustris
-
archaeoglobus
-
rhodopseudomonas
-
eutropha
-
ammonia-lyase
-
d-aspartate
-
electrocardiogram
- 1.4.1.21
- analysis
- synthesis
- oxaloacetate
- dehydrogenases
-
thermotoga
- maritima
-
dehydrogenation
- fulgidus
- palustris
-
archaeoglobus
-
rhodopseudomonas
- eutropha
-
ammonia-lyase
- d-aspartate
-
electrocardiogram
Reaction
Synonyms
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
ECTree
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Substrates Products
Substrates Products on EC 1.4.1.21 - aspartate dehydrogenase
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REACTION DIAGRAM
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
-
-
?
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
-
-
-
-
?
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
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
-
-
-
-
?
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
-
-
r
oxaloacetate + NH3 + NADPH + H+
L-aspartate + H2O + NADP+
-
-
-
-
r
L-aspartate + NAD+ + H2O
-
strictly specific for oxaloacetate and NADH, not NADPH
-
?
oxaloacetate + NH4+ + NADH
L-aspartate + NAD+ + H2O
-
biosynthesis of aspartate
-
?
oxaloacetate + NH4+ + NADH
L-aspartate + NAD+ + H2O
-
strictly specific for oxaloacetate and NADH, not NADPH
-
?
oxaloacetate + NH4+ + NADH
L-aspartate + NAD+ + H2O
-
biosynthesis of aspartate
-
?
?
-
-
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
?
-
-
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 catalyzes in vitro the reductive amination of oxaloacetate to L-aspartate by an order faster than the deamination reaction
-
-
?
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
?
-
-
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
-
-
?