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2-oxoglutarate + NH3 + NAD(P)H + H+
L-glutamate + H2O + NAD(P)+
L-alanine + H2O + NAD(P)+
pyruvate + NH3 + NAD(P)H + H+
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
L-aspartate + H2O + NAD+
oxaloacetate + NH3 + NADH + H+
L-aspartate + H2O + NADP+
oxaloacetate + NH3 + NADPH + H+
L-aspartate + NAD(P)+
oxaloacetate + NH4+ + NAD(P)H
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-aspartate + NAD+
oxaloacetate + NH4+ + NADH
L-aspartate + NADP+ + H2O
oxaloacetate + NH4+ + NADPH
-
-
-
?
L-glutamate + H2O + NAD(P)+
2-oxoglutarate + NH3 + NAD(P)H + H+
oxaloacetate + NAD(P)H + NH4+
L-aspartate + NAD(P)+
-
-
-
?
oxaloacetate + NH3 + NAD(P)H + H+
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NADH + H+
L-aspartate + H2O + NAD+
oxaloacetate + NH3 + NADPH + H+
L-aspartate + H2O + NADP+
oxaloacetate + NH4+ + NADH
L-aspartate + NAD+ + H2O
pyruvate + NH3 + NAD(P)H + H+
L-alanine + H2O + NAD(P)+
additional information
?
-
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)+
-
-
-
-
?
L-alanine + H2O + NAD(P)+
pyruvate + NH3 + NAD(P)H + H+
-
-
-
?
L-alanine + H2O + NAD(P)+
pyruvate + NH3 + NAD(P)H + H+
-
-
-
-
?
L-alanine + H2O + NAD(P)+
pyruvate + 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+
-
-
-
?
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+
-
-
-
-
?
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+
-
-
-
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 + 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 + 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+
-
-
-
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-aspartate + H2O + NADP+
oxaloacetate + NH3 + NADPH + H+
-
-
-
-
r
L-aspartate + NAD(P)+
oxaloacetate + NH4+ + NAD(P)H
-
-
-
?, r
L-aspartate + NAD(P)+
oxaloacetate + NH4+ + NAD(P)H
-
-
-
-
r
L-aspartate + NAD+
oxaloacetate + NH4+ + NADH
-
-
-
-
?
L-aspartate + NAD+
oxaloacetate + NH4+ + NADH
-
-
-
?
L-aspartate + NAD+
oxaloacetate + NH4+ + NADH
-
-
-
?
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+
-
-
-
-
?
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+
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+
-
-
-
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+
-
-
-
-
?
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 + NADH + H+
L-aspartate + H2O + NAD+
-
-
-
-
r
oxaloacetate + NH3 + NADH + H+
L-aspartate + H2O + NAD+
-
-
-
-
r
oxaloacetate + NH3 + NADPH + H+
L-aspartate + H2O + NADP+
-
-
-
-
r
oxaloacetate + NH3 + NADPH + H+
L-aspartate + H2O + NADP+
-
-
-
-
r
oxaloacetate + NH3 + NADPH + H+
L-aspartate + H2O + NADP+
-
-
-
-
r
oxaloacetate + NH3 + NADPH + H+
L-aspartate + H2O + NADP+
-
-
-
r
oxaloacetate + NH3 + NADPH + H+
L-aspartate + H2O + NADP+
-
-
-
-
r
oxaloacetate + NH3 + NADPH + H+
L-aspartate + H2O + NADP+
-
-
-
-
?
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
oxaloacetate + NH3 + NADPH + H+
L-aspartate + H2O + NADP+
-
-
-
-
r
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
-
?
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
-
?
pyruvate + NH3 + NAD(P)H + H+
L-alanine + H2O + NAD(P)+
-
-
-
?
pyruvate + NH3 + NAD(P)H + H+
L-alanine + H2O + NAD(P)+
-
-
-
-
?
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
?
-
-
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
-
-
?
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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
-
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
-
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
-
metabolism
-
proposed pathways of L-Asp metabolism, overview
metabolism
-
proposed pathways of L-Asp metabolism, overview
-
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
-
involvement of L-AspDH in NAD biosynthesis, overview
physiological function
involvement of L-AspDH in NAD biosynthesis, overview
physiological function
-
the amination activity of the enzyme may be important for the fixation of inorganic nitrogen
physiological function
-
the amination activity of the enzyme may be important for the fixation of inorganic nitrogen
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
-
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
-
involvement of L-AspDH in NAD biosynthesis, overview
-
additional information
-
three-dimensional structure comparisons, overview
additional information
-
three-dimensional structure comparisons, overview
additional information
-
three-dimensional structure comparisons, overview
additional information
-
three-dimensional structure comparisons, overview
additional information
three-dimensional structure comparisons, overview
additional information
-
three-dimensional structure comparisons, overview
-
additional information
-
three-dimensional structure comparisons, overview
-
additional information
-
three-dimensional structure comparisons, overview
-
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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
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
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
-
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
-
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
-
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
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
-
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
-
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
-
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
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
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
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
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
synthesis
-
individual overexpression of ASPDH, aspartate-semialdehyde dehydrogenase from Tistrella mobilis, dihydrodipicolinate reductase from Escherichia coli, and diaminopimelate dehydrogenase from Pseudothermotoga thermarum in Corynebacterium glutamicum LC298, a basic lysine producer, increases the production of lysine by 30.7%, 32.4%, 17.4%, and 36.8%, respectively. The highest increase of lysine production (30.7%) is observed for a triple-mutant strain (27.7 g/L, 0.35 g/g glucose) expressing ASPDH, aspartate-semialdehyde dehydrogenase from Tistrella mobilis, dihydrodipicolinate reductase from Escherichia coli. A quadruple-mutant strain expressing all of the four NADH-utilizing enzymes allows high lysine production (24.1 g/l, 0.30 g/g glucose) almost independent of the oxidative pentose phosphate pathway
synthesis
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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
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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
-
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
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Klebsiella pneumoniae
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The synthesis of aspartic acid in Rhizobium lupini bacteroids
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1981
Bradyrhizobium lupini, Bradyrhizobium lupini 359a
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Thermotoga maritima (Q9X1X6), Thermotoga maritima
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Archaeoglobus fulgidus
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Archaeoglobus fulgidus (O28440), Archaeoglobus fulgidus, Thermotoga maritima (Q9X1X6), Thermotoga maritima
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2013
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brenda
Li, Y.; Kawakami, N.; Ogola, H.J.; Ashida, H.; Ishikawa, T.; Shibata, H.; Sawa, Y.
A novel L-aspartate dehydrogenase from the mesophilic bacterium Pseudomonas aeruginosa PAO1: molecular characterization and application for L-aspartate production
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90
1953-1962
2011
Pseudomonas aeruginosa
brenda
Li, Y.; Ogola, H.J.; Sawa, Y.
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93
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2012
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brenda
Li, Y.; Ishida, M.; Ashida, H.; Ishikawa, T.; Shibata, H.; Sawa, Y.
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75
1524-1532
2011
Cupriavidus necator (Q46VA0), Cupriavidus necator JMP 134-1 (Q46VA0)
brenda
Ozyurt, C.; Evran, S.; Telefoncu, A.
Development of a novel fluorescent protein construct by genetically fusing green fluorescent protein to the N-terminal of aspartate dehydrogenase
Biotechnol. Appl. Biochem.
60
399-404
2013
Thermotoga maritima
brenda
Wu, W.; Zhang, Y.; Liu, D.; Chen, Z.
Efficient mining of natural NADH-utilizing dehydrogenases enables systematic cofactor engineering of lysine synthesis pathway of Corynebacterium glutamicum
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52
77-86
2019
Pseudomonas aeruginosa
brenda
Li, H.; Zhu, T.; Miao, L.; Zhang, D.; Li, Y.; Li, Q.; Li, Y.
Discovery of novel highly active and stable aspartate dehydrogenases
Sci. Rep.
7
7881
2017
Klebsiella pneumoniae, Delftia sp. Cs1-4 (F6ALN7), Klebsiella pneumoniae 34618
brenda