Activating Compound | Comment | Organism | Structure |
---|---|---|---|
NH4+ | - |
Geobacillus stearothermophilus | |
NH4+ | - |
Paenibacillus polymyxa |
General Stability | Organism |
---|---|
L-lysine, L-threonine or L-methionine protects the enzymic activity against heat inactivation | Rhodocyclus tenuis |
nonpolar L-amino acids protect from inactivation by heat and detergent and reverse the inhibition caused by feedback inhibitors L-lysine and L-threonine | Paenibacillus polymyxa |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
aspartate-beta-semialdehyde | - |
Bacillus licheniformis | |
aspartate-beta-semialdehyde | - |
Cereibacter sphaeroides | |
DL-meso-diaminopimelic acid | aspartokinase I, noncompetitive inhibition | Bacillus subtilis | |
DL-meso-diaminopimelic acid | - |
Geobacillus stearothermophilus | |
L-lysine | - |
Azotobacter sp. | |
L-lysine | - |
Bacillus cereus | |
L-lysine | - |
Bacillus licheniformis | |
L-lysine | - |
Bacillus subtilis | |
L-lysine | concerted feedback inhibition with L-threonine | [Brevibacterium] flavum | |
L-lysine | - |
Cereibacter sphaeroides | |
L-lysine | concerted feedback inhibition with L-threonine | Corynebacterium glutamicum | |
L-lysine | - |
Escherichia coli | |
L-lysine | - |
Geobacillus stearothermophilus | |
L-lysine | - |
Paenibacillus polymyxa | |
L-lysine | - |
Pseudomonas aeruginosa | |
L-lysine | concerted feedback inhibition with L-threonine | Pseudomonas fluorescens | |
L-lysine | - |
Pseudomonas putida | |
L-lysine | - |
Rhodobacter capsulatus | |
L-lysine | - |
Rhodocyclus tenuis | |
L-lysine | - |
Salmonella enterica subsp. enterica serovar Typhimurium | |
L-threonine | aspartokinase II, competitive inhibition | Bacillus subtilis | |
L-threonine | - |
Escherichia coli | |
L-threonine | - |
Geobacillus stearothermophilus | |
L-threonine | - |
Paenibacillus polymyxa | |
L-threonine | - |
Pseudomonas aeruginosa | |
L-threonine | - |
Pseudomonas fluorescens | |
L-threonine | - |
Pseudomonas putida | |
L-threonine | - |
Rhodocyclus tenuis | |
L-threonine | - |
Saccharomyces cerevisiae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.18 | - |
ATP | aspartokinase I | Escherichia coli | |
0.9 | - |
L-aspartate | - |
Rhodocyclus tenuis | |
1.5 | - |
L-aspartate | - |
Paenibacillus polymyxa | |
1.5 | - |
L-aspartate | aspartokinase I | Escherichia coli | |
1.9 | - |
ATP | aspartokinase II, 27°C | Escherichia coli | |
2.1 | - |
L-aspartate | aspartokinase II, 27°C | Escherichia coli | |
3 | - |
ATP | - |
Rhodocyclus tenuis | |
3 | - |
L-aspartate | aspartokinase I | Bacillus subtilis | |
4 | - |
ATP | aspartokinase I | Escherichia coli | |
4.7 | - |
L-aspartate | aspartokinase III, 27°C | Escherichia coli | |
4.8 | - |
ATP | - |
Pseudomonas putida | |
4.8 | - |
L-aspartate | - |
Pseudomonas putida | |
4.8 | - |
ATP | aspartokinase III, 27°C | Escherichia coli | |
17 | - |
L-aspartate | aspartokinase II | Bacillus subtilis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | - |
Saccharomyces cerevisiae | |
Fe2+ | - |
Neurospora crassa | |
Fe2+ | - |
Paenibacillus polymyxa | |
K+ | - |
Bacillus subtilis | |
K+ | - |
Geobacillus stearothermophilus | |
K+ | - |
Pseudomonas fluorescens | |
K+ | activity enhanced | Paenibacillus polymyxa | |
Mg2+ | - |
Saccharomyces cerevisiae | |
Mg2+ | - |
Neurospora crassa | |
Mg2+ | - |
Paenibacillus polymyxa | |
Mn2+ | - |
Saccharomyces cerevisiae | |
Mn2+ | - |
Neurospora crassa | |
Mn2+ | - |
Pseudomonas fluorescens |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
17000 | - |
2 * 17000 + 2 * 47000, SDS-PAGE | Paenibacillus polymyxa |
43000 | - |
4 * 43000, aspartokinase II, equilibrium sedimentation | Escherichia coli |
47000 | - |
2 * 17000 + 2 * 47000, SDS-PAGE | Paenibacillus polymyxa |
60000 | - |
? * 60000, high-speed sedimentation equilibrium in 6.0 mM guanidinium chloride | Escherichia coli |
66000 | - |
4 * 66000, ultracentrifugation | Escherichia coli |
80000 | - |
4 * 80000, aspartokinase-homoserine dehydrogenase complex, sedimentation equlibrium performed on guanidinium chloride dissolved complex | Escherichia coli |
84000 | - |
4 * 84000, SDS-PAGE | Escherichia coli |
88000 | - |
4 * 88000, gel filtration in 6.0 mM guanidinium chloride | Escherichia coli |
100000 | - |
gel filtration | Rhodocyclus tenuis |
110000 | - |
gel filtration | Geobacillus stearothermophilus |
116000 | - |
equilibrium ultracentrifugation | Paenibacillus polymyxa |
122000 | - |
2 * 122000, ultracentrifugation in TES or HEPES buffer | Escherichia coli |
125000 | - |
aspartokinase II | Bacillus subtilis |
126000 | - |
gel filtration | Pseudomonas putida |
127000 | - |
aspartokinase III, sedimentation equilibrium | Escherichia coli |
169000 | - |
aspartokinase II, equilibrium sedimentation | Escherichia coli |
250000 | - |
aspartokinase I | Bacillus subtilis |
358000 | - |
light scattering studies | Escherichia coli |
360000 | - |
equilibrium sedimentation | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-aspartate | Salmonella enterica subsp. enterica serovar Typhimurium | - |
ADP + 4-phospho-L-aspartate | - |
r | |
ATP + L-aspartate | Escherichia coli | - |
ADP + 4-phospho-L-aspartate | - |
r | |
ATP + L-aspartate | Saccharomyces cerevisiae | - |
ADP + 4-phospho-L-aspartate | - |
r | |
ATP + L-aspartate | Geobacillus stearothermophilus | - |
ADP + 4-phospho-L-aspartate | - |
r | |
ATP + L-aspartate | Neurospora crassa | - |
ADP + 4-phospho-L-aspartate | - |
r | |
ATP + L-aspartate | Pseudomonas fluorescens | - |
ADP + 4-phospho-L-aspartate | - |
r | |
ATP + L-aspartate | Rhodobacter capsulatus | - |
ADP + 4-phospho-L-aspartate | - |
r | |
ATP + L-aspartate | Paenibacillus polymyxa | - |
ADP + 4-phospho-L-aspartate | - |
r | |
ATP + L-aspartate | Rhodospirillum rubrum | - |
ADP + 4-phospho-L-aspartate | - |
r | |
ATP + L-aspartate | Rhodocyclus tenuis | - |
ADP + 4-phospho-L-aspartate | - |
r | |
ATP + L-aspartate | Bacillus subtilis | physiological role of aspartokinase II is to supply precursors for the amino acid pool | ADP + 4-phospho-L-aspartate | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Azotobacter sp. | - |
- |
- |
Bacillus cereus | - |
- |
- |
Bacillus licheniformis | - |
- |
- |
Bacillus subtilis | - |
- |
- |
Cereibacter sphaeroides | - |
- |
- |
Corynebacterium glutamicum | - |
- |
- |
Escherichia coli | - |
K12 | - |
Geobacillus stearothermophilus | - |
- |
- |
Neurospora crassa | - |
- |
- |
no activity in Edwardsiella sp. | - |
- |
- |
no activity in Providencia sp. | - |
- |
- |
Paenibacillus polymyxa | - |
- |
- |
Pseudomonas aeruginosa | - |
- |
- |
Pseudomonas fluorescens | - |
- |
- |
Pseudomonas putida | - |
- |
- |
Rhodobacter capsulatus | - |
- |
- |
Rhodocyclus tenuis | - |
- |
- |
Rhodospirillum rubrum | - |
- |
- |
Saccharomyces cerevisiae | - |
yeast | - |
Salmonella enterica subsp. enterica serovar Typhimurium | - |
- |
- |
[Brevibacterium] flavum | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Cereibacter sphaeroides |
- |
Paenibacillus polymyxa |
- |
Rhodocyclus tenuis |
aspartokinase III | Escherichia coli |
partially | Geobacillus stearothermophilus |
Storage Stability | Organism |
---|---|
-10°C, can be stored over a period of 6 months with a 40% loss of activity, longer storage does not lead to further inactivation | Paenibacillus polymyxa |
-15°C, aspartokinase II, stable in buffer containing 20% glycerol, remaining 100% active and homogenous for several months | Escherichia coli |
25°C, aspartokinase I, stable at room temperature either in presence of 1.0 mM L-threonine or of 0.15 M KCl | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-aspartate | - |
Salmonella enterica subsp. enterica serovar Typhimurium | ADP + 4-phospho-L-aspartate | - |
r | |
ATP + L-aspartate | - |
Bacillus subtilis | ADP + 4-phospho-L-aspartate | - |
r | |
ATP + L-aspartate | - |
Escherichia coli | ADP + 4-phospho-L-aspartate | - |
r | |
ATP + L-aspartate | - |
Saccharomyces cerevisiae | ADP + 4-phospho-L-aspartate | - |
r | |
ATP + L-aspartate | - |
Geobacillus stearothermophilus | ADP + 4-phospho-L-aspartate | - |
r | |
ATP + L-aspartate | - |
Neurospora crassa | ADP + 4-phospho-L-aspartate | - |
r | |
ATP + L-aspartate | - |
Pseudomonas fluorescens | ADP + 4-phospho-L-aspartate | - |
r | |
ATP + L-aspartate | - |
Pseudomonas putida | ADP + 4-phospho-L-aspartate | - |
? | |
ATP + L-aspartate | - |
Rhodobacter capsulatus | ADP + 4-phospho-L-aspartate | - |
r | |
ATP + L-aspartate | - |
Paenibacillus polymyxa | ADP + 4-phospho-L-aspartate | - |
r | |
ATP + L-aspartate | - |
Rhodospirillum rubrum | ADP + 4-phospho-L-aspartate | - |
r | |
ATP + L-aspartate | - |
Rhodocyclus tenuis | ADP + 4-phospho-L-aspartate | - |
r | |
ATP + L-aspartate | maximum velocity of the reverse reaction is only one-twelfth that of the forward reaction, but has the advantage of using commercial substrates | Escherichia coli | ADP + 4-phospho-L-aspartate | - |
r | |
ATP + L-aspartate | physiological role of aspartokinase II is to supply precursors for the amino acid pool | Bacillus subtilis | ADP + 4-phospho-L-aspartate | - |
r | |
additional information | - |
Escherichia coli | ? | - |
? | |
additional information | - |
Saccharomyces cerevisiae | ? | - |
? | |
additional information | - |
Pseudomonas fluorescens | ? | - |
? | |
additional information | - |
Paenibacillus polymyxa | ? | - |
? | |
additional information | no other natural aminoacids or D-aspartate are substrates of this reaction | Neurospora crassa | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 122000, ultracentrifugation in TES or HEPES buffer | Escherichia coli |
heterodimer | - |
Bacillus subtilis |
oligomer | ? * 60000, high-speed sedimentation equilibrium in 6.0 mM guanidinium chloride | Escherichia coli |
tetramer | 4 * 84000, SDS-PAGE | Escherichia coli |
tetramer | 4 * 80000-120000, sedimentation in sucrose gradient in absence of threonine | Escherichia coli |
tetramer | 2 * 17000 + 2 * 47000, SDS-PAGE | Paenibacillus polymyxa |
tetramer | 4 * 43000, aspartokinase II, equilibrium sedimentation | Escherichia coli |
tetramer | 4 * 80000, aspartokinase-homoserine dehydrogenase complex, sedimentation equlibrium performed on guanidinium chloride dissolved complex | Escherichia coli |
tetramer | 4 * 88000, gel filtration in 6.0 mM guanidinium chloride | Escherichia coli |
tetramer | 4 * 66000, ultracentrifugation | Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
55 | - |
- |
Geobacillus stearothermophilus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
14.2 | - |
L-aspartate | aspartokinase II | Escherichia coli | |
39.2 | - |
L-aspartate | aspartokinase III | Escherichia coli | |
56.7 | - |
L-aspartate | aspartokinase I | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
- |
Geobacillus stearothermophilus |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6 | 9.5 | aspartokinase I, pH range for 50% activity | Bacillus subtilis |
6.5 | 8.2 | aspartokinase II, pH range for 50% activity | Bacillus subtilis |