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Literature summary for 2.2.1.6 extracted from

  • Poulsen, C.; Stougaard, P.
    Purification and properties of Saccharomyces cerevisiae acetolactate synthase from recombinant Escherichia coli (1989), Eur. J. Biochem., 185, 433-439.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.93
-
pyruvate
-
Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Saccharomyces cerevisiae
Mg2+ Km: 0.28 mM Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
75000
-
2 * 75000, SDS-PAGE Saccharomyces cerevisiae
150000
-
-
Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Saccharomyces cerevisiae

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
dimer 2 * 75000, SDS-PAGE Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
-
Saccharomyces cerevisiae

pH Range

pH Minimum pH Maximum Comment Organism
6 7.5 pH 6.0: about 25% of maximal activity, pH 7.5: about 65% of maximal activity Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
FAD required Saccharomyces cerevisiae
FAD Km: 0.0003 mM Saccharomyces cerevisiae
thiamine diphosphate required as cofactor Saccharomyces cerevisiae
thiamine diphosphate Km: 0.11 mM Saccharomyces cerevisiae