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Literature summary for 2.7.2.4 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
Search for more literature for 2.7.2.4

General Stability

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

Inhibitors

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Brevibacillus brevis
-
 ATCC 10068
-

Purification (Commentary)

Purification (Comment) Organism
partially, 2 isoenzymes Brevibacillus brevis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 0.483 units/mg Brevibacillus brevis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-aspartate
-
 Brevibacillus brevis ADP + 4-phospho-L-aspartate
-
 r
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