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Literature summary extracted from

  • Lee, Y.T.; Duggleby, R.G.
    Mutations in the regulatory subunit of yeast acetohydroxyacid synthase affect its activation by MgATP (2006), Biochem. J., 395, 331-336.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
2.2.1.6 F204A site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme Saccharomyces cerevisiae
2.2.1.6 H181A site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme Saccharomyces cerevisiae
2.2.1.6 H205A site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme Saccharomyces cerevisiae
2.2.1.6 H219A site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme Saccharomyces cerevisiae
2.2.1.6 K218A site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme Saccharomyces cerevisiae
2.2.1.6 L177A site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme Saccharomyces cerevisiae
2.2.1.6 L222A site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme Saccharomyces cerevisiae
2.2.1.6 P206A site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme Saccharomyces cerevisiae
2.2.1.6 R216A site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme Saccharomyces cerevisiae
2.2.1.6 S212A site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.2.1.6 valine feedback inhibition, reversible by MgATP2- Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.2.1.6 additional information
-
 additional information kinetics Saccharomyces cerevisiae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.2.1.6 MgATP2- activates Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.2.1.6 pyruvate Saccharomyces cerevisiae the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine 2-acetolactate + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.2.1.6 Saccharomyces cerevisiae
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.2.1.6 2 pyruvate = 2-acetolactate + CO2 action model for the regulatory subunit Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.2.1.6 pyruvate
-
 Saccharomyces cerevisiae 2-acetolactate + CO2
-
 ?
2.2.1.6 pyruvate the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine Saccharomyces cerevisiae 2-acetolactate + CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
2.2.1.6 More heterotetrameric enzyme composed of a small, regulatory and a large, catalytic subunit Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
2.2.1.6 acetohydroxyacid synthase
-
 Saccharomyces cerevisiae
2.2.1.6 AHAS
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.2.1.6 30
-
 assay at Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.2.1.6 7
-
 assay at Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
2.2.1.6 FAD
-
 Saccharomyces cerevisiae
2.2.1.6 thiamine diphosphate
-
 Saccharomyces cerevisiae

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.2.1.6 0.003
-
 valine pH 7.0, 30°C, mutant L222A Saccharomyces cerevisiae
2.2.1.6 0.006
-
 valine pH 7.0, 30°C, mutant K218A Saccharomyces cerevisiae
2.2.1.6 0.0156
-
 valine pH 7.0, 30°C, mutant S212A Saccharomyces cerevisiae
2.2.1.6 0.0162
-
 valine pH 7.0, 30°C, mutant L177A Saccharomyces cerevisiae
2.2.1.6 0.02
-
 valine pH 7.0, 30°C, mutant H205A Saccharomyces cerevisiae
2.2.1.6 0.0245
-
 valine pH 7.0, 30°C, mutant R216A Saccharomyces cerevisiae
2.2.1.6 0.026
-
 valine pH 7.0, 30°C, mutant F204A Saccharomyces cerevisiae
2.2.1.6 0.039
-
 valine pH 7.0, 30°C, mutant P206A Saccharomyces cerevisiae
2.2.1.6 0.058
-
 valine pH 7.0, 30°C, mutant H181A Saccharomyces cerevisiae
2.2.1.6 0.177
-
 valine pH 7.0, 30°C, wild-type enzyme Saccharomyces cerevisiae