Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | unaffected by EDTA, CaCl2, NiCl2, CoCl2, CuSO4 or ZnCl2 | Archaeoglobus fulgidus |
Application | Comment | Organism |
---|---|---|
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 | Archaeoglobus fulgidus |
Cloned (Comment) | Organism |
---|---|
ligated into the expression vector pET11a, expression in Escherichia coli strain BL21(DE3) | Archaeoglobus fulgidus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.014 | - |
NADH | - |
Archaeoglobus fulgidus | |
0.11 | - |
NAD+ | - |
Archaeoglobus fulgidus | |
0.19 | - |
L-aspartate | with NAD+ as the electron acceptor | Archaeoglobus fulgidus | |
0.32 | - |
NADP+ | - |
Archaeoglobus fulgidus | |
1.2 | - |
oxaloacetate | - |
Archaeoglobus fulgidus | |
4.3 | - |
L-aspartate | with NADP+ as the electron acceptor | Archaeoglobus fulgidus | |
167 | - |
NH4+ | - |
Archaeoglobus fulgidus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
26000 | - |
2 * 26000, SDS-PAGE, 2 * 26208, sequence analysis | Archaeoglobus fulgidus |
26208 | - |
2 * 26000, SDS-PAGE, 2 * 26208, sequence analysis | Archaeoglobus fulgidus |
48000 | - |
gel filtration | Archaeoglobus fulgidus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Archaeoglobus fulgidus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
to homogeneity by heat treatment and affinity chromatography | Archaeoglobus fulgidus |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
4.6 | - |
purified enzyme, at 50 °C | Archaeoglobus fulgidus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-aspartate + NAD(P)+ + H2O | the enzyme shows pro-R (A-type) stereospecificity for hydrogen transfer from the C4 position of the nicotinamide moiety ofNADH | Archaeoglobus fulgidus | oxaloacetate + NH4+ + NAD(P)H | - |
? | |
L-aspartate + NAD+ | - |
Archaeoglobus fulgidus | oxaloacetate + NH4+ + NADH | - |
? | |
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 | Archaeoglobus fulgidus | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodimer | 2 * 26000, SDS-PAGE, 2 * 26208, sequence analysis | Archaeoglobus fulgidus |
Synonyms | Comment | Organism |
---|---|---|
L-aspartate dehydrogenase | - |
Archaeoglobus fulgidus |
L-aspDH | - |
Archaeoglobus fulgidus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
80 | - |
- |
Archaeoglobus fulgidus |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | 100 | - |
Archaeoglobus fulgidus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
80 | - |
stable for 1 h | Archaeoglobus fulgidus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
11.6 | - |
- |
Archaeoglobus fulgidus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD(P)+ | - |
Archaeoglobus fulgidus |