EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.7.2.4 | DL-meso-diaminopimelic acid | ATCC6051, aspartokinase I | Bacillus subtilis | |
2.7.2.4 | L-lysine | - |
Bacillus subtilis | |
2.7.2.4 | additional information | threonine has no effect | Bacillus subtilis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.7.2.4 | 0.35 | - |
ATP | pH 7.0, 25°C | Bacillus subtilis | |
2.7.2.4 | 1 | - |
L-aspartate | pH 7.0, 25°C | Bacillus subtilis |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.7.2.4 | 17000 | - |
1 * 17000 + 1 * 43000, alpha and beta subunits, SDS-PAGE | Bacillus subtilis |
2.7.2.4 | 43000 | - |
1 * 17000 + 1 * 43000, alpha and beta subunits, SDS-PAGE | Bacillus subtilis |
2.7.2.4 | 115000 | - |
aspartokinase II, equilibrium sedimentation | Bacillus subtilis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.2.4 | ATP + L-aspartate | Bacillus subtilis | first specific step in the biosynthesis of L-lysine, L-threonine and L-methionine | ADP + 4-phospho-L-aspartate | - |
r | |
2.7.2.4 | ATP + L-aspartate | Bacillus subtilis VB217 | first specific step in the biosynthesis of L-lysine, L-threonine and L-methionine | ADP + 4-phospho-L-aspartate | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.7.2.4 | Bacillus subtilis | - |
VB217, ATCC6051 | - |
2.7.2.4 | Bacillus subtilis VB217 | - |
VB217, ATCC6051 | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.7.2.4 | VB217, aspartokinase II | Bacillus subtilis |
EC Number | Renatured (Comment) | Organism |
---|---|---|
2.7.2.4 | when renatured after treatment with 6.0 M guanidine hydrochloride 80 to 90% of the original activity regained, renaturation of isolated alpha subunits leads to a lower recovery of activity, 65%, which is increased by about 30% in presence of an equivalent amount of beta subunit | Bacillus subtilis |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
2.7.2.4 | 30 | - |
- |
Bacillus subtilis |
EC Number | Storage Stability | Organism |
---|---|---|
2.7.2.4 | 4°C, refolded enzyme, no loss of activity for 24 h | Bacillus subtilis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.2.4 | ATP + L-aspartate | - |
Bacillus subtilis | ADP + 4-phospho-L-aspartate | - |
r | |
2.7.2.4 | ATP + L-aspartate | first specific step in the biosynthesis of L-lysine, L-threonine and L-methionine | Bacillus subtilis | ADP + 4-phospho-L-aspartate | - |
r | |
2.7.2.4 | ATP + L-aspartate | - |
Bacillus subtilis VB217 | ADP + 4-phospho-L-aspartate | - |
r | |
2.7.2.4 | ATP + L-aspartate | first specific step in the biosynthesis of L-lysine, L-threonine and L-methionine | Bacillus subtilis VB217 | ADP + 4-phospho-L-aspartate | - |
r |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.7.2.4 | heterodimer | 1 * 17000 + 1 * 43000, alpha and beta subunits, SDS-PAGE | Bacillus subtilis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.7.2.4 | aspartokinase II | - |
Bacillus subtilis |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.7.2.4 | 0.1 | - |
L-lysine | pH 7.0, 25°C | Bacillus subtilis |