EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
1.4.1.21 | additional information | unaffected by EDTA, CaCl2, NiCl2, CoCl2, CuSO4 or ZnCl2 | Archaeoglobus fulgidus |
EC Number | Application | Comment | Organism |
---|---|---|---|
1.4.1.21 | 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 |
EC Number | Cloned (Comment) | Organism |
---|---|---|
1.4.1.21 | ligated into the expression vector pET11a, expression in Escherichia coli strain BL21(DE3) | Archaeoglobus fulgidus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.4.1.21 | 0.014 | - |
NADH | - |
Archaeoglobus fulgidus | |
1.4.1.21 | 0.11 | - |
NAD+ | - |
Archaeoglobus fulgidus | |
1.4.1.21 | 0.19 | - |
L-aspartate | with NAD+ as the electron acceptor | Archaeoglobus fulgidus | |
1.4.1.21 | 0.32 | - |
NADP+ | - |
Archaeoglobus fulgidus | |
1.4.1.21 | 1.2 | - |
oxaloacetate | - |
Archaeoglobus fulgidus | |
1.4.1.21 | 4.3 | - |
L-aspartate | with NADP+ as the electron acceptor | Archaeoglobus fulgidus | |
1.4.1.21 | 167 | - |
NH4+ | - |
Archaeoglobus fulgidus |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.4.1.21 | 26000 | - |
2 * 26000, SDS-PAGE, 2 * 26208, sequence analysis | Archaeoglobus fulgidus |
1.4.1.21 | 26208 | - |
2 * 26000, SDS-PAGE, 2 * 26208, sequence analysis | Archaeoglobus fulgidus |
1.4.1.21 | 48000 | - |
gel filtration | Archaeoglobus fulgidus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.4.1.21 | Archaeoglobus fulgidus | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.4.1.21 | to homogeneity by heat treatment and affinity chromatography | Archaeoglobus fulgidus |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.4.1.21 | 4.6 | - |
purified enzyme, at 50 °C | Archaeoglobus fulgidus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.4.1.21 | 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 | - |
? | |
1.4.1.21 | L-aspartate + NAD+ | - |
Archaeoglobus fulgidus | oxaloacetate + NH4+ + NADH | - |
? | |
1.4.1.21 | 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 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.4.1.21 | homodimer | 2 * 26000, SDS-PAGE, 2 * 26208, sequence analysis | Archaeoglobus fulgidus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.4.1.21 | L-aspartate dehydrogenase | - |
Archaeoglobus fulgidus |
1.4.1.21 | L-aspDH | - |
Archaeoglobus fulgidus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.4.1.21 | 80 | - |
- |
Archaeoglobus fulgidus |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.4.1.21 | 37 | 100 | - |
Archaeoglobus fulgidus |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.4.1.21 | 80 | - |
stable for 1 h | Archaeoglobus fulgidus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.4.1.21 | 11.6 | - |
- |
Archaeoglobus fulgidus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.4.1.21 | NAD(P)+ | - |
Archaeoglobus fulgidus |