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Literature summary 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

Inhibitors

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

KM Value [mM]

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

Molecular Weight [Da]

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

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 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

Organism

EC Number Organism UniProt Comment Textmining
2.7.2.4 Bacillus subtilis
-
VB217, ATCC6051
-
2.7.2.4 Bacillus subtilis VB217
-
VB217, ATCC6051
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.2.4 VB217, aspartokinase II Bacillus subtilis

Renatured (Commentary)

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.2.4 30
-
-
Bacillus subtilis

Storage Stability

EC Number Storage Stability Organism
2.7.2.4 4°C, refolded enzyme, no loss of activity for 24 h Bacillus subtilis

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
2.7.2.4 aspartokinase II
-
Bacillus subtilis

Ki Value [mM]

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