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Literature summary 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

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

General Stability

EC Number General Stability Organism
2.7.2.4 L-lysine, L-threonine or L-methionine protects the enzymic activity against heat inactivation Rhodocyclus tenuis
2.7.2.4 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

EC Number Inhibitors Comment Organism Structure
2.7.2.4 aspartate-beta-semialdehyde
-
 Bacillus licheniformis
2.7.2.4 aspartate-beta-semialdehyde
-
 Cereibacter sphaeroides
2.7.2.4 DL-meso-diaminopimelic acid aspartokinase I, noncompetitive inhibition Bacillus subtilis
2.7.2.4 DL-meso-diaminopimelic acid
-
 Geobacillus stearothermophilus
2.7.2.4 L-lysine
-
 Azotobacter sp.
2.7.2.4 L-lysine
-
 Bacillus cereus
2.7.2.4 L-lysine
-
 Bacillus licheniformis
2.7.2.4 L-lysine
-
 Bacillus subtilis
2.7.2.4 L-lysine concerted feedback inhibition with L-threonine [Brevibacterium] flavum
2.7.2.4 L-lysine
-
 Cereibacter sphaeroides
2.7.2.4 L-lysine concerted feedback inhibition with L-threonine Corynebacterium glutamicum
2.7.2.4 L-lysine
-
 Escherichia coli
2.7.2.4 L-lysine
-
 Geobacillus stearothermophilus
2.7.2.4 L-lysine
-
 Paenibacillus polymyxa
2.7.2.4 L-lysine
-
 Pseudomonas aeruginosa
2.7.2.4 L-lysine concerted feedback inhibition with L-threonine Pseudomonas fluorescens
2.7.2.4 L-lysine
-
 Pseudomonas putida
2.7.2.4 L-lysine
-
 Rhodobacter capsulatus
2.7.2.4 L-lysine
-
 Rhodocyclus tenuis
2.7.2.4 L-lysine
-
 Salmonella enterica subsp. enterica serovar Typhimurium
2.7.2.4 L-threonine aspartokinase II, competitive inhibition Bacillus subtilis
2.7.2.4 L-threonine
-
 Escherichia coli
2.7.2.4 L-threonine
-
 Geobacillus stearothermophilus
2.7.2.4 L-threonine
-
 Paenibacillus polymyxa
2.7.2.4 L-threonine
-
 Pseudomonas aeruginosa
2.7.2.4 L-threonine
-
 Pseudomonas fluorescens
2.7.2.4 L-threonine
-
 Pseudomonas putida
2.7.2.4 L-threonine
-
 Rhodocyclus tenuis
2.7.2.4 L-threonine
-
 Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.2.4 0.18
-
 ATP aspartokinase I Escherichia coli
2.7.2.4 0.9
-
 L-aspartate
-
 Rhodocyclus tenuis
2.7.2.4 1.5
-
 L-aspartate
-
 Paenibacillus polymyxa
2.7.2.4 1.5
-
 L-aspartate aspartokinase I Escherichia coli
2.7.2.4 1.9
-
 ATP aspartokinase II, 27°C Escherichia coli
2.7.2.4 2.1
-
 L-aspartate aspartokinase II, 27°C Escherichia coli
2.7.2.4 3
-
 ATP
-
 Rhodocyclus tenuis
2.7.2.4 3
-
 L-aspartate aspartokinase I Bacillus subtilis
2.7.2.4 4
-
 ATP aspartokinase I Escherichia coli
2.7.2.4 4.7
-
 L-aspartate aspartokinase III, 27°C Escherichia coli
2.7.2.4 4.8
-
 ATP
-
 Pseudomonas putida
2.7.2.4 4.8
-
 L-aspartate
-
 Pseudomonas putida
2.7.2.4 4.8
-
 ATP aspartokinase III, 27°C Escherichia coli
2.7.2.4 17
-
 L-aspartate aspartokinase II Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.2.4 Fe2+
-
 Saccharomyces cerevisiae
2.7.2.4 Fe2+
-
 Neurospora crassa
2.7.2.4 Fe2+
-
 Paenibacillus polymyxa
2.7.2.4 K+
-
 Bacillus subtilis
2.7.2.4 K+
-
 Geobacillus stearothermophilus
2.7.2.4 K+
-
 Pseudomonas fluorescens
2.7.2.4 K+ activity enhanced Paenibacillus polymyxa
2.7.2.4 Mg2+
-
 Saccharomyces cerevisiae
2.7.2.4 Mg2+
-
 Neurospora crassa
2.7.2.4 Mg2+
-
 Paenibacillus polymyxa
2.7.2.4 Mn2+
-
 Saccharomyces cerevisiae
2.7.2.4 Mn2+
-
 Neurospora crassa
2.7.2.4 Mn2+
-
 Pseudomonas fluorescens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.2.4 17000
-
 2 * 17000 + 2 * 47000, SDS-PAGE Paenibacillus polymyxa
2.7.2.4 43000
-
 4 * 43000, aspartokinase II, equilibrium sedimentation Escherichia coli
2.7.2.4 47000
-
 2 * 17000 + 2 * 47000, SDS-PAGE Paenibacillus polymyxa
2.7.2.4 60000
-
 ? * 60000, high-speed sedimentation equilibrium in 6.0 mM guanidinium chloride Escherichia coli
2.7.2.4 66000
-
 4 * 66000, ultracentrifugation Escherichia coli
2.7.2.4 80000
-
 4 * 80000, aspartokinase-homoserine dehydrogenase complex, sedimentation equlibrium performed on guanidinium chloride dissolved complex Escherichia coli
2.7.2.4 84000
-
 4 * 84000, SDS-PAGE Escherichia coli
2.7.2.4 88000
-
 4 * 88000, gel filtration in 6.0 mM guanidinium chloride Escherichia coli
2.7.2.4 100000
-
 gel filtration Rhodocyclus tenuis
2.7.2.4 110000
-
 gel filtration Geobacillus stearothermophilus
2.7.2.4 116000
-
 equilibrium ultracentrifugation Paenibacillus polymyxa
2.7.2.4 122000
-
 2 * 122000, ultracentrifugation in TES or HEPES buffer Escherichia coli
2.7.2.4 125000
-
 aspartokinase II Bacillus subtilis
2.7.2.4 126000
-
 gel filtration Pseudomonas putida
2.7.2.4 127000
-
 aspartokinase III, sedimentation equilibrium Escherichia coli
2.7.2.4 169000
-
 aspartokinase II, equilibrium sedimentation Escherichia coli
2.7.2.4 250000
-
 aspartokinase I Bacillus subtilis
2.7.2.4 358000
-
 light scattering studies Escherichia coli
2.7.2.4 360000
-
 equilibrium sedimentation Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.2.4 ATP + L-aspartate Salmonella enterica subsp. enterica serovar Typhimurium
-
 ADP + 4-phospho-L-aspartate
-
 r
2.7.2.4 ATP + L-aspartate Escherichia coli
-
 ADP + 4-phospho-L-aspartate
-
 r
2.7.2.4 ATP + L-aspartate Saccharomyces cerevisiae
-
 ADP + 4-phospho-L-aspartate
-
 r
2.7.2.4 ATP + L-aspartate Geobacillus stearothermophilus
-
 ADP + 4-phospho-L-aspartate
-
 r
2.7.2.4 ATP + L-aspartate Neurospora crassa
-
 ADP + 4-phospho-L-aspartate
-
 r
2.7.2.4 ATP + L-aspartate Pseudomonas fluorescens
-
 ADP + 4-phospho-L-aspartate
-
 r
2.7.2.4 ATP + L-aspartate Rhodobacter capsulatus
-
 ADP + 4-phospho-L-aspartate
-
 r
2.7.2.4 ATP + L-aspartate Paenibacillus polymyxa
-
 ADP + 4-phospho-L-aspartate
-
 r
2.7.2.4 ATP + L-aspartate Rhodospirillum rubrum
-
 ADP + 4-phospho-L-aspartate
-
 r
2.7.2.4 ATP + L-aspartate Rhodocyclus tenuis
-
 ADP + 4-phospho-L-aspartate
-
 r
2.7.2.4 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

EC Number Organism UniProt Comment Textmining
2.7.2.4 Azotobacter sp.
-
-
-
2.7.2.4 Bacillus cereus
-
-
-
2.7.2.4 Bacillus licheniformis
-
-
-
2.7.2.4 Bacillus subtilis
-
-
-
2.7.2.4 Cereibacter sphaeroides
-
-
-
2.7.2.4 Corynebacterium glutamicum
-
-
-
2.7.2.4 Escherichia coli
-
 K12
-
2.7.2.4 Geobacillus stearothermophilus
-
-
-
2.7.2.4 Neurospora crassa
-
-
-
2.7.2.4 no activity in Edwardsiella sp.
-
-
-
2.7.2.4 no activity in Providencia sp.
-
-
-
2.7.2.4 Paenibacillus polymyxa
-
-
-
2.7.2.4 Pseudomonas aeruginosa
-
-
-
2.7.2.4 Pseudomonas fluorescens
-
-
-
2.7.2.4 Pseudomonas putida
-
-
-
2.7.2.4 Rhodobacter capsulatus
-
-
-
2.7.2.4 Rhodocyclus tenuis
-
-
-
2.7.2.4 Rhodospirillum rubrum
-
-
-
2.7.2.4 Saccharomyces cerevisiae
-
 yeast
-
2.7.2.4 Salmonella enterica subsp. enterica serovar Typhimurium
-
-
-
2.7.2.4 [Brevibacterium] flavum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.2.4
-
 Cereibacter sphaeroides
2.7.2.4
-
 Paenibacillus polymyxa
2.7.2.4
-
 Rhodocyclus tenuis
2.7.2.4 aspartokinase III Escherichia coli
2.7.2.4 partially Geobacillus stearothermophilus

Storage Stability

EC Number Storage Stability Organism
2.7.2.4 -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
2.7.2.4 -15°C, aspartokinase II, stable in buffer containing 20% glycerol, remaining 100% active and homogenous for several months Escherichia coli
2.7.2.4 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.2.4 ATP + L-aspartate
-
 Salmonella enterica subsp. enterica serovar Typhimurium ADP + 4-phospho-L-aspartate
-
 r
2.7.2.4 ATP + L-aspartate
-
 Bacillus subtilis ADP + 4-phospho-L-aspartate
-
 r
2.7.2.4 ATP + L-aspartate
-
 Escherichia coli ADP + 4-phospho-L-aspartate
-
 r
2.7.2.4 ATP + L-aspartate
-
 Saccharomyces cerevisiae ADP + 4-phospho-L-aspartate
-
 r
2.7.2.4 ATP + L-aspartate
-
 Geobacillus stearothermophilus ADP + 4-phospho-L-aspartate
-
 r
2.7.2.4 ATP + L-aspartate
-
 Neurospora crassa ADP + 4-phospho-L-aspartate
-
 r
2.7.2.4 ATP + L-aspartate
-
 Pseudomonas fluorescens ADP + 4-phospho-L-aspartate
-
 r
2.7.2.4 ATP + L-aspartate
-
 Pseudomonas putida ADP + 4-phospho-L-aspartate
-
 ?
2.7.2.4 ATP + L-aspartate
-
 Rhodobacter capsulatus ADP + 4-phospho-L-aspartate
-
 r
2.7.2.4 ATP + L-aspartate
-
 Paenibacillus polymyxa ADP + 4-phospho-L-aspartate
-
 r
2.7.2.4 ATP + L-aspartate
-
 Rhodospirillum rubrum ADP + 4-phospho-L-aspartate
-
 r
2.7.2.4 ATP + L-aspartate
-
 Rhodocyclus tenuis ADP + 4-phospho-L-aspartate
-
 r
2.7.2.4 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
2.7.2.4 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
2.7.2.4 additional information
-
 Escherichia coli ?
-
 ?
2.7.2.4 additional information
-
 Saccharomyces cerevisiae ?
-
 ?
2.7.2.4 additional information
-
 Pseudomonas fluorescens ?
-
 ?
2.7.2.4 additional information
-
 Paenibacillus polymyxa ?
-
 ?
2.7.2.4 additional information no other natural aminoacids or D-aspartate are substrates of this reaction Neurospora crassa ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.2.4 dimer 2 * 122000, ultracentrifugation in TES or HEPES buffer Escherichia coli
2.7.2.4 heterodimer
-
 Bacillus subtilis
2.7.2.4 oligomer ? * 60000, high-speed sedimentation equilibrium in 6.0 mM guanidinium chloride Escherichia coli
2.7.2.4 tetramer 4 * 84000, SDS-PAGE Escherichia coli
2.7.2.4 tetramer 4 * 80000-120000, sedimentation in sucrose gradient in absence of threonine Escherichia coli
2.7.2.4 tetramer 2 * 17000 + 2 * 47000, SDS-PAGE Paenibacillus polymyxa
2.7.2.4 tetramer 4 * 43000, aspartokinase II, equilibrium sedimentation Escherichia coli
2.7.2.4 tetramer 4 * 80000, aspartokinase-homoserine dehydrogenase complex, sedimentation equlibrium performed on guanidinium chloride dissolved complex Escherichia coli
2.7.2.4 tetramer 4 * 88000, gel filtration in 6.0 mM guanidinium chloride Escherichia coli
2.7.2.4 tetramer 4 * 66000, ultracentrifugation Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.2.4 55
-
-
 Geobacillus stearothermophilus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.2.4 14.2
-
 L-aspartate aspartokinase II Escherichia coli
2.7.2.4 39.2
-
 L-aspartate aspartokinase III Escherichia coli
2.7.2.4 56.7
-
 L-aspartate aspartokinase I Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.2.4 8
-
-
 Geobacillus stearothermophilus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.7.2.4 6 9.5 aspartokinase I, pH range for 50% activity Bacillus subtilis
2.7.2.4 6.5 8.2 aspartokinase II, pH range for 50% activity Bacillus subtilis