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Literature summary for 2.7.2.4 extracted from

  • Truffa-Bachi, P.
    Microbial aspartokinases (1973), The Enzymes, 3rd Ed. (Boyer, P. D. , ed. ), 8, 509-553.
No PubMed abstract available

Activating Compound

Activating Compound Comment Organism Structure
NH4+
-
Geobacillus stearothermophilus
NH4+
-
Paenibacillus polymyxa

General Stability

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

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 [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

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 [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/ Products (Substrates)

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

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 (Commentary)

Purification (Comment) Organism
-
Cereibacter sphaeroides
-
Paenibacillus polymyxa
-
Rhodocyclus tenuis
aspartokinase III Escherichia coli
partially Geobacillus stearothermophilus

Storage Stability

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 and Products (Substrate)

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

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 [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
-
Geobacillus stearothermophilus

Turnover Number [1/s]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
Geobacillus stearothermophilus

pH Range

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