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Literature summary extracted from

  • Li, Y.; Ishida, M.; Ashida, H.; Ishikawa, T.; Shibata, H.; Sawa, Y.
    A non-NadB type L-aspartate dehydrogenase from Ralstonia eutropha strain JMP134: molecular characterization and physiological functions (2011), Biosci. Biotechnol. Biochem., 75, 1524-1532.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.4.1.21 AspDH gene cluster, gene AspDH expression in Escherichia coli strain BL21(DE3), quantitative real-time PCR expression analysis Cupriavidus necator

Protein Variants

EC Number Protein Variants Comment Organism
1.4.1.21 additional information construction of an AspDH knockout strain, growth phenotype, compared to the wild-type Cupriavidus necator

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.1.21 0.014
-
 NADH pH 8.2, 37°C Cupriavidus necator
1.4.1.21 0.11
-
 NAD+ pH 10.2, 37°C Cupriavidus necator
1.4.1.21 0.19
-
 L-aspartate pH 10.2, 37°C, with NAD+ Cupriavidus necator
1.4.1.21 0.32
-
 NADP+ pH 10.2, 37°C Cupriavidus necator
1.4.1.21 1.2
-
 oxaloacetate pH 8.2, 37°C, with NADH Cupriavidus necator
1.4.1.21 4.3
-
 L-aspartate pH 10.2, 37°C, with NADP+ Cupriavidus necator
1.4.1.21 167
-
 NH3 pH 8.2, 37°C, with NADH Cupriavidus necator

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.4.1.21 28000
-
 2 * 28000, SDS-PAGE Cupriavidus necator

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.4.1.21 L-aspartate + H2O + NAD(P)+ Cupriavidus necator
-
 oxaloacetate + NH3 + NAD(P)H + H+
-
 r
1.4.1.21 L-aspartate + H2O + NAD(P)+ Cupriavidus necator JMP 134-1
-
 oxaloacetate + NH3 + NAD(P)H + H+
-
 r
1.4.1.21 additional information Cupriavidus necator the wild-type strain synthesizes 3-hydroxy-polybutyrate from fructose or L-Asp, while the enzyme knockout mutant strain does not ?
-
 ?
1.4.1.21 additional information Cupriavidus necator JMP 134-1 the wild-type strain synthesizes 3-hydroxy-polybutyrate from fructose or L-Asp, while the enzyme knockout mutant strain does not ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.21 Cupriavidus necator Q46VA0 gene B3576
-
1.4.1.21 Cupriavidus necator JMP 134-1 Q46VA0 gene B3576
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.4.1.21 137
-
 37°C, pH 10.2 Cupriavidus necator

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.1.21 L-aspartate + H2O + NAD(P)+
-
 Cupriavidus necator oxaloacetate + NH3 + NAD(P)H + H+
-
 r
1.4.1.21 L-aspartate + H2O + NAD(P)+
-
 Cupriavidus necator JMP 134-1 oxaloacetate + NH3 + NAD(P)H + H+
-
 r
1.4.1.21 L-aspartate + H2O + NAD+
-
 Cupriavidus necator oxaloacetate + NH3 + NADH + H+
-
 r
1.4.1.21 L-aspartate + H2O + NAD+
-
 Cupriavidus necator JMP 134-1 oxaloacetate + NH3 + NADH + H+
-
 r
1.4.1.21 L-aspartate + H2O + NADP+
-
 Cupriavidus necator oxaloacetate + NH3 + NADPH + H+
-
 r
1.4.1.21 L-aspartate + H2O + NADP+
-
 Cupriavidus necator JMP 134-1 oxaloacetate + NH3 + NADPH + H+
-
 r
1.4.1.21 additional information the wild-type strain synthesizes 3-hydroxy-polybutyrate from fructose or L-Asp, while the enzyme knockout mutant strain does not Cupriavidus necator ?
-
 ?
1.4.1.21 additional information the wild-type strain synthesizes 3-hydroxy-polybutyrate from fructose or L-Asp, while the enzyme knockout mutant strain does not Cupriavidus necator JMP 134-1 ?
-
 ?
1.4.1.21 oxaloacetate + NH3 + NADH + H+
-
 Cupriavidus necator L-aspartate + H2O + NAD+
-
 r
1.4.1.21 oxaloacetate + NH3 + NADH + H+
-
 Cupriavidus necator JMP 134-1 L-aspartate + H2O + NAD+
-
 r
1.4.1.21 oxaloacetate + NH3 + NADPH + H+
-
 Cupriavidus necator L-aspartate + H2O + NADP+
-
 r

Subunits

EC Number Subunits Comment Organism
1.4.1.21 homodimer 2 * 28000, SDS-PAGE Cupriavidus necator

Synonyms

EC Number Synonyms Comment Organism
1.4.1.21 L-aspartate dehydrogenase
-
 Cupriavidus necator
1.4.1.21 L-aspDH
-
 Cupriavidus necator

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.4.1.21 50
-
-
 Cupriavidus necator

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.4.1.21 30 60 activity range, profile overview Cupriavidus necator

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.4.1.21 35
-
 20 min, fully stable up to Cupriavidus necator
1.4.1.21 49
-
 20 min, Tm of purified enzyme Cupriavidus necator
1.4.1.21 55
-
 20 min, inactivation Cupriavidus necator

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.1.21 8.2
-
 amination Cupriavidus necator
1.4.1.21 10.2
-
 deamination Cupriavidus necator

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.4.1.21 5.8 7.2 stable Cupriavidus necator

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.1.21 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+ Cupriavidus necator
1.4.1.21 NAD+
-
 Cupriavidus necator
1.4.1.21 NADH
-
 Cupriavidus necator
1.4.1.21 NADP+
-
 Cupriavidus necator
1.4.1.21 NADPH
-
 Cupriavidus necator

General Information

EC Number General Information Comment Organism
1.4.1.21 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 Cupriavidus necator