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Information on EC 1.4.1.21 - aspartate dehydrogenase and Organism(s) Pseudomonas aeruginosa and UniProt Accession Q9HYA4
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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 taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
aspartate dehydrogenase, l-aspdh, aspdh, l-aspartate dehydrogenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AspDH
-
-
-
-
L-aspartate dehydrogenase
-
-
-
-
L-aspartate:NAD(P)+ oxidoreductase (deaminating)
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-
-
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NAD-dependent aspartate dehydrogenase
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-
-
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NADH2-dependent aspartate dehydrogenase
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-
-
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NADP+-dependent aspartate dehydrogenase
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-
-
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nadX
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-
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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+.
CAS REGISTRY NUMBER
COMMENTARY
37278-97-0
-
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 + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + H+
-
-
-
r
L-aspartate + H2O + NAD+
oxaloacetate + NH3 + NADH + H+
-
-
-
r
L-aspartate + H2O + NADP+
oxaloacetate + NH3 + NADPH + H+
-
-
-
r
oxaloacetate + NH3 + NADH + H+
L-aspartate + H2O + NAD+
-
-
-
r
oxaloacetate + NH3 + NADPH + H+
L-aspartate + H2O + NADP+
-
-
-
r
L-aspartate + H2O + NAD(P)+
oxaloacetate + NH3 + NAD(P)H + 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+
-
the enzyme is capable of utilizing both NAD/H and NADP/H as coenzymes
-
-
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+
-
the enzyme is capable of utilizing both NAD/H and NADP/H as coenzymes
-
-
r
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
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-
?
additional information
?
-
-
the enzyme exhibits a very high specific activity for L-aspartate and oxaloacetate
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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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
the enzyme is capable of utilizing both NAD/H and NADP/H as coenzymes
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Michaelis-Menten kinetics
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
L-AspDH members and other putative homologs share surprisingly low homology, below 10%, with the other amino acid dehydrogenases
physiological function
involvement of L-AspDH in NAD biosynthesis, overview
evolution
-
L-aspartate dehydrogenase is a rare member of amino acid dehydrogenase superfamily
additional information
three-dimensional structure comparisons, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
three-dimensional structure comparisons, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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
-
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
-
20 min, Tm of purified enzyme in presence of 0.4 M NaCl or 30% glycerol
additional information
improving the thermostability of mesophilic AspDHs by the addition of 0.4 M NaCl or 30% glycerol
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21 (DE3) to homogeneity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ORF PA3505, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli strain BL21 (DE3)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Appl. Microbiol. Biotechnol.
90
1953-1962
2011
Pseudomonas aeruginosa
Li, Y.; Ogola, H.J.; Sawa, Y.
L-aspartate dehydrogenase: features and applications
Appl. Microbiol. Biotechnol.
93
503-516
2012
Archaeoglobus fulgidus, Cupriavidus necator, Cupriavidus necator JMP 134-1, Klebsiella pneumoniae, Klebsiella pneumoniae IFO 13541, Klebsiella pneumoniae MGH 78578, Pseudomonas aeruginosa (Q9HYA4), Thermotoga maritima
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