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Literature summary extracted from

  • Hitchcock, M.J.M.; Hodgson, B.
    Lysine- and lysine-plus-threonine-inhibitable aspartokinases in Bacillus brevis (1976), Biochim. Biophys. Acta, 445, 350-363.
    View publication on PubMed

General Stability

EC Number General Stability Organism
2.7.2.4 aspartokinase II unstable in absence of L-lysine, both isoenzymes stablized by sulfhydryl reducing agents Brevibacillus brevis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.2.4 L-lysine concerted feedback inhibition with L-threonine Brevibacillus brevis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.2.4 95000
-
 aspartokinase II Brevibacillus brevis
2.7.2.4 110000
-
 aspartokinase I Brevibacillus brevis

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 Brevibacillus brevis first step common to the biosynthesis of L-lysine, L-threonine, isoleucine and methionine ADP + 4-phospho-L-aspartate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.7.2.4 Brevibacillus brevis
-
 ATCC 10068
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.2.4 partially, 2 isoenzymes Brevibacillus brevis

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 additional information
-
 0.483 units/mg Brevibacillus brevis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.2.4 ATP + L-aspartate
-
 Brevibacillus brevis ADP + 4-phospho-L-aspartate
-
 r
2.7.2.4 ATP + L-aspartate first step common to the biosynthesis of L-lysine, L-threonine, isoleucine and methionine Brevibacillus brevis ADP + 4-phospho-L-aspartate
-
 r