Application | Comment | Organism |
---|---|---|
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 | Klebsiella pneumoniae |
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 | Cupriavidus necator |
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 | Archaeoglobus fulgidus |
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 | Thermotoga maritima |
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 | Pseudomonas aeruginosa |
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 | Klebsiella pneumoniae |
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 | Cupriavidus necator |
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 | Archaeoglobus fulgidus |
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 | Thermotoga maritima |
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 | Pseudomonas aeruginosa |
Cloned (Comment) | Organism |
---|---|
gene KPN_03362, DNA and amino acid sequence determination and analysis | Klebsiella pneumoniae |
gene nadX, phylogenetic analysis | Pseudomonas aeruginosa |
gene nadX, the gene forms an operon with the NAD biosynthesis genes nadA and nadC | Thermotoga maritima |
Protein Variants | Comment | Organism |
---|---|---|
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 | Pseudomonas aeruginosa |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.014 | - |
NADH | pH not specified in the publication, 37°C | Cupriavidus necator | |
0.045 | - |
NADH | pH 8.2, 37°C | Pseudomonas aeruginosa | |
0.061 | - |
NADH | pH not specified in the publication, 50°C | Archaeoglobus fulgidus | |
0.067 | - |
L-aspartate | pH and temperature not specified in the publication, with NAD+ | Thermotoga maritima | |
0.11 | - |
NAD+ | pH 10.2, 37°C | Cupriavidus necator | |
0.19 | - |
L-aspartate | pH 10.2, 37°C, with NAD+ | Cupriavidus necator | |
0.25 | - |
NAD+ | pH and temperature not specified in the publication | Thermotoga maritima | |
0.32 | - |
NADP+ | pH 10.2, 37°C | Cupriavidus necator | |
0.47 | - |
NAD+ | pH 9.8, 37°C | Pseudomonas aeruginosa | |
0.47 | - |
NADP+ | pH 9.8, 37°C | Pseudomonas aeruginosa | |
0.72 | - |
NADP+ | pH and temperature not specified in the publication | Thermotoga maritima | |
0.97 | - |
NAD+ | pH 11.6, 50°C | Archaeoglobus fulgidus | |
1.2 | - |
L-aspartate | pH and temperature not specified in the publication, with NADP+ | Thermotoga maritima | |
1.2 | - |
oxaloacetate | pH not specified in the publication, 37°C, with NADH | Cupriavidus necator | |
2.12 | - |
oxaloacetate | pH 8.2, 37°C, with NADH | Pseudomonas aeruginosa | |
2.3 | - |
L-aspartate | pH 11.6, 50°C, with NAD+ | Archaeoglobus fulgidus | |
2.32 | - |
oxaloacetate | pH not specified in the publication, 50°C, with NADH | Archaeoglobus fulgidus | |
4.3 | - |
L-aspartate | pH 10.2, 37°C, with NADP+ | Cupriavidus necator | |
4.74 | - |
L-aspartate | pH 9.8, 37°C, with NADP+ | Pseudomonas aeruginosa | |
4.87 | - |
L-aspartate | pH 9.8, 37°C, with NAD+ | Pseudomonas aeruginosa | |
7.43 | - |
NADP+ | pH 11.6, 50°C | Archaeoglobus fulgidus | |
10.1 | - |
NH3 | pH 8.2, 37°C, with NADH | Pseudomonas aeruginosa | |
14.9 | - |
NH3 | pH not specified in the publication, 50°C, with NADH | Archaeoglobus fulgidus | |
26.6 | - |
L-aspartate | pH 11.6, 50°C, with NADP+ | Archaeoglobus fulgidus | |
167 | - |
NH3 | pH not specified in the publication, 37°C, with NADH | Cupriavidus necator |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
26000 | - |
2 * 26000 | Archaeoglobus fulgidus |
27000 | - |
2 * 27000 | Thermotoga maritima |
27000 | - |
2 * 27000, about, sequence calculation | Klebsiella pneumoniae |
28000 | - |
2 * 28000 | Cupriavidus necator |
28000 | - |
2 * 28000 | Pseudomonas aeruginosa |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-aspartate + H2O + NAD(P)+ | Klebsiella pneumoniae | - |
oxaloacetate + NH3 + NAD(P)H + H+ | - |
r | |
L-aspartate + H2O + NAD(P)+ | Cupriavidus necator | - |
oxaloacetate + NH3 + NAD(P)H + H+ | - |
r | |
L-aspartate + H2O + NAD(P)+ | Archaeoglobus fulgidus | - |
oxaloacetate + NH3 + NAD(P)H + H+ | - |
r | |
L-aspartate + H2O + NAD(P)+ | Thermotoga maritima | - |
oxaloacetate + NH3 + NAD(P)H + H+ | - |
r | |
L-aspartate + H2O + NAD(P)+ | Pseudomonas aeruginosa | - |
oxaloacetate + NH3 + NAD(P)H + H+ | - |
r | |
L-aspartate + H2O + NAD(P)+ | Klebsiella pneumoniae MGH 78578 | - |
oxaloacetate + NH3 + NAD(P)H + H+ | - |
r | |
L-aspartate + H2O + NAD(P)+ | Cupriavidus necator JMP 134-1 | - |
oxaloacetate + NH3 + NAD(P)H + H+ | - |
r | |
L-aspartate + H2O + NAD(P)+ | Klebsiella pneumoniae IFO 13541 | - |
oxaloacetate + NH3 + NAD(P)H + H+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Archaeoglobus fulgidus | - |
- |
- |
Cupriavidus necator | - |
- |
- |
Cupriavidus necator JMP 134-1 | - |
- |
- |
Klebsiella pneumoniae | - |
- |
- |
Klebsiella pneumoniae | - |
subsp. pneumoniae, gene KPN_03362 | - |
Klebsiella pneumoniae IFO 13541 | - |
- |
- |
Klebsiella pneumoniae MGH 78578 | - |
subsp. pneumoniae, gene KPN_03362 | - |
Pseudomonas aeruginosa | Q9HYA4 | gene nadX | - |
Thermotoga maritima | - |
gene nadX | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.045 | - |
30°C, pH not specified in the publication | Klebsiella pneumoniae |
4.6 | - |
50°C, pH 11.6 | Archaeoglobus fulgidus |
127 | - |
pH 9.8, 37°C | Pseudomonas aeruginosa |
137 | - |
37°C, pH 10.2 | Cupriavidus necator |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-aspartate + H2O + NAD(P)+ | - |
Klebsiella pneumoniae | oxaloacetate + NH3 + NAD(P)H + H+ | - |
r | |
L-aspartate + H2O + NAD(P)+ | - |
Cupriavidus necator | oxaloacetate + NH3 + NAD(P)H + H+ | - |
r | |
L-aspartate + H2O + NAD(P)+ | - |
Archaeoglobus fulgidus | oxaloacetate + NH3 + NAD(P)H + H+ | - |
r | |
L-aspartate + H2O + NAD(P)+ | - |
Thermotoga maritima | oxaloacetate + NH3 + NAD(P)H + H+ | - |
r | |
L-aspartate + H2O + NAD(P)+ | - |
Pseudomonas aeruginosa | oxaloacetate + NH3 + NAD(P)H + H+ | - |
r | |
L-aspartate + H2O + NAD(P)+ | - |
Klebsiella pneumoniae MGH 78578 | oxaloacetate + NH3 + NAD(P)H + H+ | - |
r | |
L-aspartate + H2O + NAD(P)+ | - |
Cupriavidus necator JMP 134-1 | oxaloacetate + NH3 + NAD(P)H + H+ | - |
r | |
L-aspartate + H2O + NAD(P)+ | - |
Klebsiella pneumoniae IFO 13541 | oxaloacetate + NH3 + NAD(P)H + H+ | - |
r | |
L-aspartate + H2O + NAD+ | - |
Klebsiella pneumoniae | oxaloacetate + NH3 + NADH + H+ | - |
r | |
L-aspartate + H2O + NAD+ | - |
Cupriavidus necator | oxaloacetate + NH3 + NADH + H+ | - |
r | |
L-aspartate + H2O + NAD+ | - |
Archaeoglobus fulgidus | oxaloacetate + NH3 + NADH + H+ | - |
r | |
L-aspartate + H2O + NAD+ | - |
Thermotoga maritima | oxaloacetate + NH3 + NADH + H+ | - |
r | |
L-aspartate + H2O + NAD+ | - |
Pseudomonas aeruginosa | oxaloacetate + NH3 + NADH + H+ | - |
r | |
L-aspartate + H2O + NAD+ | - |
Klebsiella pneumoniae MGH 78578 | oxaloacetate + NH3 + NADH + H+ | - |
r | |
L-aspartate + H2O + NAD+ | - |
Cupriavidus necator JMP 134-1 | oxaloacetate + NH3 + NADH + H+ | - |
r | |
L-aspartate + H2O + NAD+ | - |
Klebsiella pneumoniae IFO 13541 | oxaloacetate + NH3 + NADH + H+ | - |
r | |
L-aspartate + H2O + NADP+ | - |
Klebsiella pneumoniae | oxaloacetate + NH3 + NADPH + H+ | - |
r | |
L-aspartate + H2O + NADP+ | - |
Cupriavidus necator | oxaloacetate + NH3 + NADPH + H+ | - |
r | |
L-aspartate + H2O + NADP+ | - |
Archaeoglobus fulgidus | oxaloacetate + NH3 + NADPH + H+ | - |
r | |
L-aspartate + H2O + NADP+ | - |
Thermotoga maritima | oxaloacetate + NH3 + NADPH + H+ | - |
r | |
L-aspartate + H2O + NADP+ | - |
Pseudomonas aeruginosa | oxaloacetate + NH3 + NADPH + H+ | - |
r | |
L-aspartate + H2O + NADP+ | - |
Klebsiella pneumoniae MGH 78578 | oxaloacetate + NH3 + NADPH + H+ | - |
r | |
L-aspartate + H2O + NADP+ | - |
Cupriavidus necator JMP 134-1 | oxaloacetate + NH3 + NADPH + H+ | - |
r | |
L-aspartate + H2O + NADP+ | - |
Klebsiella pneumoniae IFO 13541 | oxaloacetate + NH3 + NADPH + H+ | - |
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 | Klebsiella pneumoniae | ? | - |
? | |
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 | Cupriavidus necator | ? | - |
? | |
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 | Archaeoglobus fulgidus | ? | - |
? | |
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 | Thermotoga maritima | ? | - |
? | |
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 | Pseudomonas aeruginosa | ? | - |
? | |
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 | Klebsiella pneumoniae MGH 78578 | ? | - |
? | |
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 | Cupriavidus necator JMP 134-1 | ? | - |
? | |
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 | Klebsiella pneumoniae IFO 13541 | ? | - |
? | |
oxaloacetate + NH3 + NADH + H+ | - |
Klebsiella pneumoniae | L-aspartate + H2O + NAD+ | - |
r | |
oxaloacetate + NH3 + NADH + H+ | - |
Cupriavidus necator | L-aspartate + H2O + NAD+ | - |
r | |
oxaloacetate + NH3 + NADH + H+ | - |
Archaeoglobus fulgidus | L-aspartate + H2O + NAD+ | - |
r | |
oxaloacetate + NH3 + NADH + H+ | - |
Thermotoga maritima | L-aspartate + H2O + NAD+ | - |
r | |
oxaloacetate + NH3 + NADH + H+ | - |
Pseudomonas aeruginosa | L-aspartate + H2O + NAD+ | - |
r | |
oxaloacetate + NH3 + NADH + H+ | - |
Klebsiella pneumoniae MGH 78578 | L-aspartate + H2O + NAD+ | - |
r | |
oxaloacetate + NH3 + NADH + H+ | - |
Cupriavidus necator JMP 134-1 | L-aspartate + H2O + NAD+ | - |
r | |
oxaloacetate + NH3 + NADH + H+ | - |
Klebsiella pneumoniae IFO 13541 | L-aspartate + H2O + NAD+ | - |
r | |
oxaloacetate + NH3 + NADPH + H+ | - |
Klebsiella pneumoniae | L-aspartate + H2O + NADP+ | - |
r | |
oxaloacetate + NH3 + NADPH + H+ | - |
Cupriavidus necator | L-aspartate + H2O + NADP+ | - |
r | |
oxaloacetate + NH3 + NADPH + H+ | - |
Archaeoglobus fulgidus | L-aspartate + H2O + NADP+ | - |
r | |
oxaloacetate + NH3 + NADPH + H+ | - |
Thermotoga maritima | L-aspartate + H2O + NADP+ | - |
r | |
oxaloacetate + NH3 + NADPH + H+ | - |
Pseudomonas aeruginosa | L-aspartate + H2O + NADP+ | - |
r |
Subunits | Comment | Organism |
---|---|---|
homodimer | 2 * 28000 | Cupriavidus necator |
homodimer | 2 * 28000 | Pseudomonas aeruginosa |
homodimer | 2 * 26000 | Archaeoglobus fulgidus |
homodimer | 2 * 27000 | Thermotoga maritima |
homodimer | 2 * 27000, about, sequence calculation | Klebsiella pneumoniae |
homodimer | three-dimensional structure comparisons, overview | Klebsiella pneumoniae |
More | three-dimensional structure comparisons, overview | Klebsiella pneumoniae |
More | three-dimensional structure comparisons, overview | Cupriavidus necator |
More | three-dimensional structure comparisons, overview | Archaeoglobus fulgidus |
More | three-dimensional structure comparisons, overview | Thermotoga maritima |
More | three-dimensional structure comparisons, overview | Pseudomonas aeruginosa |
Synonyms | Comment | Organism |
---|---|---|
L-aspartate dehydrogenase | - |
Klebsiella pneumoniae |
L-aspartate dehydrogenase | - |
Cupriavidus necator |
L-aspartate dehydrogenase | - |
Archaeoglobus fulgidus |
L-aspartate dehydrogenase | - |
Thermotoga maritima |
L-aspartate dehydrogenase | - |
Pseudomonas aeruginosa |
L-aspDH | - |
Klebsiella pneumoniae |
L-aspDH | - |
Cupriavidus necator |
L-aspDH | - |
Archaeoglobus fulgidus |
L-aspDH | - |
Thermotoga maritima |
L-aspDH | - |
Pseudomonas aeruginosa |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | - |
- |
Cupriavidus necator |
50 | - |
- |
Pseudomonas aeruginosa |
70 | - |
above | Thermotoga maritima |
80 | - |
- |
Archaeoglobus fulgidus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
improving the thermostability of mesophilic AspDHs by the addition of 0.4 M NaCl or 30% glycerol | Pseudomonas aeruginosa |
additional information | - |
thermostability of AfuAspDH is mainly ascribed to the intersubunit ion and aromatic pair interactions in the enzyme | Archaeoglobus fulgidus |
additional information | - |
thermostability of TmaAspDH is mainly ascribed to the intersubunit ion and aromatic pair interactions in the enzyme | Thermotoga maritima |
48 | - |
20 min, Tm of purified enzyme | Pseudomonas aeruginosa |
49 | - |
20 min, Tm of purified enzyme | Cupriavidus necator |
80 | - |
above, Tm of purified enzyme | Archaeoglobus fulgidus |
80 | - |
above, Tm of purified enzyme | Thermotoga maritima |
100 | - |
half-life is 10 min | Archaeoglobus fulgidus |
100 | - |
half-life is 10.7 min | Thermotoga maritima |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
9.8 | - |
deamination | Pseudomonas aeruginosa |
10.2 | - |
deamination | Cupriavidus necator |
11.6 | - |
deamination | Archaeoglobus fulgidus |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
4.5 | 11.5 | stable | Archaeoglobus fulgidus |
5.8 | 6.6 | stable | Pseudomonas aeruginosa |
5.8 | 7.2 | stable | Cupriavidus necator |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | L-AspDH can utilize both NAD+ and NADP+ as a coenzyme, albeit at different efficiencies | Archaeoglobus fulgidus | |
additional information | L-AspDH can utilize both NAD+ and NADP+ as a coenzyme, albeit at different efficiencies | Thermotoga maritima | |
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 | |
additional information | L-AspDH can utilize both NAD+ and NADP+ as a coenzyme, albeit at different efficiencies, similar Km values for NADP+ and NAD+ | Pseudomonas aeruginosa | |
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+ | Klebsiella pneumoniae | |
NAD+ | - |
Klebsiella pneumoniae | |
NAD+ | - |
Cupriavidus necator | |
NAD+ | - |
Archaeoglobus fulgidus | |
NAD+ | - |
Thermotoga maritima | |
NAD+ | - |
Pseudomonas aeruginosa | |
NADH | - |
Klebsiella pneumoniae | |
NADH | - |
Cupriavidus necator | |
NADH | - |
Archaeoglobus fulgidus | |
NADH | - |
Thermotoga maritima | |
NADH | - |
Pseudomonas aeruginosa | |
NADP+ | - |
Klebsiella pneumoniae | |
NADP+ | - |
Cupriavidus necator | |
NADP+ | - |
Archaeoglobus fulgidus | |
NADP+ | - |
Thermotoga maritima | |
NADP+ | - |
Pseudomonas aeruginosa | |
NADPH | - |
Klebsiella pneumoniae | |
NADPH | - |
Cupriavidus necator | |
NADPH | - |
Archaeoglobus fulgidus | |
NADPH | - |
Thermotoga maritima | |
NADPH | - |
Pseudomonas aeruginosa |
General Information | Comment | Organism |
---|---|---|
evolution | L-AspDH members and other putative homologs share surprisingly low homology, below 10%, with the other amino acid dehydrogenases | Klebsiella pneumoniae |
evolution | L-AspDH members and other putative homologs share surprisingly low homology, below 10%, with the other amino acid dehydrogenases | Cupriavidus necator |
evolution | L-AspDH members and other putative homologs share surprisingly low homology, below 10%, with the other amino acid dehydrogenases | Archaeoglobus fulgidus |
evolution | L-AspDH members and other putative homologs share surprisingly low homology, below 10%, with the other amino acid dehydrogenases | Thermotoga maritima |
evolution | L-AspDH members and other putative homologs share surprisingly low homology, below 10%, with the other amino acid dehydrogenases | Pseudomonas aeruginosa |
metabolism | proposed pathways of L-Asp metabolism, overview | Cupriavidus necator |
additional information | three-dimensional structure comparisons, overview | Klebsiella pneumoniae |
additional information | three-dimensional structure comparisons, overview | Cupriavidus necator |
additional information | three-dimensional structure comparisons, overview | Archaeoglobus fulgidus |
additional information | three-dimensional structure comparisons, overview | Thermotoga maritima |
additional information | three-dimensional structure comparisons, overview | Pseudomonas aeruginosa |
physiological function | involvement of L-AspDH in NAD biosynthesis, overview | Klebsiella pneumoniae |
physiological function | involvement of L-AspDH in NAD biosynthesis, overview | Cupriavidus necator |
physiological function | involvement of L-AspDH in NAD biosynthesis, overview | Archaeoglobus fulgidus |
physiological function | involvement of L-AspDH in NAD biosynthesis, overview | Thermotoga maritima |
physiological function | involvement of L-AspDH in NAD biosynthesis, overview | Pseudomonas aeruginosa |