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Literature summary for 2.7.2.4 extracted from

  • Moir, D.; Paulus, H.
    Properties and subunit structure of aspartokinase II from Bacillus subtilis VB217 (1977), J. Biol. Chem., 252, 4648-4654.
    View publication on PubMed
Search for more literature for 2.7.2.4

Inhibitors

Inhibitors Comment Organism Structure
DL-meso-diaminopimelic acid ATCC6051, aspartokinase I Bacillus subtilis
L-lysine
-
 Bacillus subtilis
additional information threonine has no effect Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.35
-
 ATP pH 7.0, 25°C Bacillus subtilis
1
-
 L-aspartate pH 7.0, 25°C Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
17000
-
 1 * 17000 + 1 * 43000, alpha and beta subunits, SDS-PAGE Bacillus subtilis
43000
-
 1 * 17000 + 1 * 43000, alpha and beta subunits, SDS-PAGE Bacillus subtilis
115000
-
 aspartokinase II, equilibrium sedimentation Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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
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

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
 VB217, ATCC6051
-
Bacillus subtilis VB217
-
 VB217, ATCC6051
-

Purification (Commentary)

Purification (Comment) Organism
VB217, aspartokinase II Bacillus subtilis

Renatured (Commentary)

Renatured (Comment) Organism
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

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
30
-
-
 Bacillus subtilis

Storage Stability

Storage Stability Organism
4°C, refolded enzyme, no loss of activity for 24 h Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-aspartate
-
 Bacillus subtilis ADP + 4-phospho-L-aspartate
-
 r
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
ATP + L-aspartate
-
 Bacillus subtilis VB217 ADP + 4-phospho-L-aspartate
-
 r
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

Subunits

Subunits Comment Organism
heterodimer 1 * 17000 + 1 * 43000, alpha and beta subunits, SDS-PAGE Bacillus subtilis

Synonyms

Synonyms Comment Organism
aspartokinase II
-
 Bacillus subtilis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.1
-
 L-lysine pH 7.0, 25°C Bacillus subtilis