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Literature summary for 2.2.1.6 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

Inhibitors Comment Organism Structure
Val competitive Cereibacter sphaeroides

KM Value [mM]

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Cereibacter sphaeroides
-
-
-

Substrates and Products (Substrate)

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2 7.4
-
Cereibacter sphaeroides

Cofactor

Cofactor Comment Organism Structure
FAD required Cereibacter sphaeroides
thiamine diphosphate
-
Cereibacter sphaeroides