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Literature summary for 2.7.2.4 extracted from

  • Kobashi, N.; Nishiyama, M.; Yamane, H.
    Characterization of aspartate kinase III of Bacillus subtilis (2001), Biosci. Biotechnol. Biochem., 65, 1391-1394.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene yclM introduced into aspartate kinase deficient Escherichia coli cells Bacillus subtilis

Inhibitors

Inhibitors Comment Organism Structure
L-lysine
-
Bacillus subtilis
L-threonine
-
Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
21
-
L-aspartate pH 7.0, 30°C Bacillus subtilis
23.5
-
ATP pH 7.0, 30°C Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
recombinant protein, expressed in E. coli, gel filtration 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 step of a branched biosynthetic pathway for L-lysine, L-threonine, L-isoleucine and L-methionine, regulated by the end products through feedback inhibition, the 3 aspartate kinases I, II and II are regulated by different end products ADP + 4-phospho-L-aspartate
-
r

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant protein, expressed in Escherichia coli Gif106M1 Bacillus subtilis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.62
-
-
Bacillus subtilis

Storage Stability

Storage Stability Organism
4°C, all activity is lost in 1 day 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 step of a branched biosynthetic pathway for L-lysine, L-threonine, L-isoleucine and L-methionine, regulated by the end products through feedback inhibition, the 3 aspartate kinases I, II and II are regulated by different end products Bacillus subtilis ADP + 4-phospho-L-aspartate
-
r

Subunits

Subunits Comment Organism
monomer 1 * 50000, SDS-PAGE Bacillus subtilis

Synonyms

Synonyms Comment Organism
aspartate kinase III
-
Bacillus subtilis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.333
-
aspartate pH 7.0, 30°C Bacillus subtilis

pH Stability

pH Stability pH Stability Maximum Comment Organism
7.5
-
very unstable in 10 mM tris-HCl buffer, stabilized by addition of 500 mM ammoinium sulfate Bacillus subtilis