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Literature summary 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)

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.2.4 L-lysine
-
 Bacillus subtilis
2.7.2.4 L-threonine
-
 Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.2.4 21
-
 L-aspartate pH 7.0, 30°C Bacillus subtilis
2.7.2.4 23.5
-
 ATP pH 7.0, 30°C Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.2.4 50000
-
 recombinant protein, expressed in E. coli, gel filtration 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 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

EC Number Organism UniProt Comment Textmining
2.7.2.4 Bacillus subtilis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.2.4 recombinant protein, expressed in Escherichia coli Gif106M1 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 0.62
-
-
 Bacillus subtilis

Storage Stability

EC Number Storage Stability Organism
2.7.2.4 4°C, all activity is lost in 1 day 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 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

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

Synonyms

EC Number Synonyms Comment Organism
2.7.2.4 aspartate kinase III
-
 Bacillus subtilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.2.4 0.333
-
 aspartate pH 7.0, 30°C Bacillus subtilis

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
2.7.2.4 7.5
-
 very unstable in 10 mM tris-HCl buffer, stabilized by addition of 500 mM ammoinium sulfate Bacillus subtilis