Protein Variants | Comment | Organism |
---|---|---|
F204A | site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme | Saccharomyces cerevisiae |
H181A | site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme | Saccharomyces cerevisiae |
H205A | site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme | Saccharomyces cerevisiae |
H219A | site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme | Saccharomyces cerevisiae |
K218A | site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme | Saccharomyces cerevisiae |
L177A | site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme | Saccharomyces cerevisiae |
L222A | site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme | Saccharomyces cerevisiae |
P206A | site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme | Saccharomyces cerevisiae |
R216A | site-directed mutagenesis, the mutant shows reduced stimulation by MgATP2- and decreased Ki with valine compared to the wild-type enzyme | Saccharomyces cerevisiae |
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 | Comment | Organism | Structure |
---|---|---|---|
valine | feedback inhibition, reversible by MgATP2- | Saccharomyces cerevisiae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics | Saccharomyces cerevisiae |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
MgATP2- | activates | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
pyruvate | Saccharomyces cerevisiae | the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine | 2-acetolactate + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
2 pyruvate = 2-acetolactate + CO2 | action model for the regulatory subunit | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pyruvate | - |
Saccharomyces cerevisiae | 2-acetolactate + CO2 | - |
? | |
pyruvate | the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine | Saccharomyces cerevisiae | 2-acetolactate + CO2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | heterotetrameric enzyme composed of a small, regulatory and a large, catalytic subunit | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
acetohydroxyacid synthase | - |
Saccharomyces cerevisiae |
AHAS | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Saccharomyces cerevisiae | |
thiamine diphosphate | - |
Saccharomyces cerevisiae |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.003 | - |
valine | pH 7.0, 30°C, mutant L222A | Saccharomyces cerevisiae | |
0.006 | - |
valine | pH 7.0, 30°C, mutant K218A | Saccharomyces cerevisiae | |
0.0156 | - |
valine | pH 7.0, 30°C, mutant S212A | Saccharomyces cerevisiae | |
0.0162 | - |
valine | pH 7.0, 30°C, mutant L177A | Saccharomyces cerevisiae | |
0.02 | - |
valine | pH 7.0, 30°C, mutant H205A | Saccharomyces cerevisiae | |
0.0245 | - |
valine | pH 7.0, 30°C, mutant R216A | Saccharomyces cerevisiae | |
0.026 | - |
valine | pH 7.0, 30°C, mutant F204A | Saccharomyces cerevisiae | |
0.039 | - |
valine | pH 7.0, 30°C, mutant P206A | Saccharomyces cerevisiae | |
0.058 | - |
valine | pH 7.0, 30°C, mutant H181A | Saccharomyces cerevisiae | |
0.177 | - |
valine | pH 7.0, 30°C, wild-type enzyme | Saccharomyces cerevisiae |