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Literature summary for 2.2.1.6 extracted from

  • Holtzclaw, W.D.; Chapman, L.F
    Degradative acetolactate synthase of Bacillus subtilis: purification and properties (1975), J. Bacteriol., 121, 917-922.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
acetate stimulates Bacillus subtilis

Inhibitors

Inhibitors Comment Organism Structure
phosphate inhibits activity of enzyme assayed in acetate buffer Bacillus subtilis
SO42- competitive when assayed in phosphate buffer, mixed type, when assayed in acetate buffer Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
13
-
pyruvate
-
Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
250000
-
gel filtration Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pyruvate Bacillus subtilis
-
?
-
?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Bacillus subtilis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
8.28
-
-
Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate
-
Bacillus subtilis 2-acetolactate + CO2
-
?
pyruvate
-
Bacillus subtilis ?
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.8
-
acetate buffer Bacillus subtilis
7
-
phosphate buffer Bacillus subtilis

pH Range

pH Minimum pH Maximum Comment Organism
6 8 pH 6.0: about 55% of maximal activity, pH 8.0: about 50% of maximal activity Bacillus subtilis