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Literature summary for 2.2.1.6 extracted from
- Mutations in the regulatory subunit of yeast acetohydroxyacid synthase affect its activation by MgATP (2006), Biochem. J., 395, 331-336.
Protein Variants
| 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
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| valine | feedback inhibition, reversible by MgATP2- | Saccharomyces cerevisiae |  |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetics | Saccharomyces cerevisiae |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| MgATP2- | activates | Saccharomyces cerevisiae | |
Natural Substrates/ Products (Substrates)
| 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
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| 2 pyruvate = 2-acetolactate + CO2 | action model for the regulatory subunit | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| 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
| Subunits | Comment | Organism |
|---|---|---|
| More | heterotetrameric enzyme composed of a small, regulatory and a large, catalytic subunit | Saccharomyces cerevisiae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| acetohydroxyacid synthase | - |
Saccharomyces cerevisiae |
| AHAS | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Saccharomyces cerevisiae |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | - |
Saccharomyces cerevisiae | |
| thiamine diphosphate | - |
Saccharomyces cerevisiae | |
Ki Value [mM]
| 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 | |
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