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Literature summary extracted from

  • Semeraro, R.J.; Wixom, R.L.
    Studies in valine biosynthesis. X. The acetolactate synthase from Rhodopseudomonas spheroides (1977), Microbios, 20, 7-14.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.2.1.6 Val competitive Cereibacter sphaeroides

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.2.1.6 4.5
-
 pyruvate
-
 Cereibacter sphaeroides

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.2.1.6 Mg2+ required Cereibacter sphaeroides
2.2.1.6 Mg2+ Km: 1.01 mM Cereibacter sphaeroides

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.2.1.6 pyruvate Cereibacter sphaeroides first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.2.1.6 Cereibacter sphaeroides
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.2.1.6 pyruvate
-
 Cereibacter sphaeroides 2-acetolactate + CO2
-
 ?
2.2.1.6 pyruvate first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile Cereibacter sphaeroides ?
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.2.1.6 7.2 7.4
-
 Cereibacter sphaeroides

Cofactor

EC Number Cofactor Comment Organism Structure
2.2.1.6 FAD required Cereibacter sphaeroides
2.2.1.6 thiamine diphosphate
-
 Cereibacter sphaeroides