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Literature summary for 4.1.1.1 extracted from
- Catalytic acid-base groups in yeast pyruvate decarboxylase. 2. Insights into the specific roles of D28 and E477 from the rates and stereospecificity of formation of carboligase side products (2001), Biochemistry, 40, 7369-7381.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| overexpression of wild-type and mutant YPDC in Escherichia coli BL21 | Saccharomyces cerevisiae |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D28A | lower catalytic efficiency in acetaldehyde formation, study of the effect of the active site mutation on the carboligase reaction | Saccharomyces cerevisiae |
| D28N | lower catalytic efficiency in acetaldehyde formation, study of the effect of the active site mutation on the carboligase reaction, higher acetoin formation than by wild-type YPDC | Saccharomyces cerevisiae |
| E477Q | lower catalytic efficiency in acetaldehyde formation, study of the effect of the active site mutation on the carboligase reaction, higher acetoin formation than by wild-type YPDC | Saccharomyces cerevisiae |
| H114F | active site mutant | Saccharomyces cerevisiae |
| H115F | active site mutant | Saccharomyces cerevisiae |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| pyruvate | substrate inhibition at high concentrations | Saccharomyces cerevisiae |  |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetic parameters for carboligase reactions of wild-type and mutant YPDC | Saccharomyces cerevisiae |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | cofactor | Saccharomyces cerevisiae | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| pyruvate | Saccharomyces cerevisiae | penultimate step of alcohol fermentation | acetaldehyde + CO2 | - |
ir | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| a 2-oxo carboxylate = an aldehyde + CO2 | catalytic mechanism, catalyzes the carboligation of 2 aldehydes as side reaction, mechanism | Saccharomyces cerevisiae |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
carboligase reaction, wild-type and mutant YPDC, at different pH values | Saccharomyces cerevisiae |
| 0.02 | 0.03 | pH 6, 20°C, D28A mutant YPDC | Saccharomyces cerevisiae |
| 0.04 | 0.07 | pH 6, 20°C, D28N mutant YPDC | Saccharomyces cerevisiae |
| 0.1 | 0.15 | pH 6, 20°C, E477Q mutant YPDC | Saccharomyces cerevisiae |
| 40 | 45 | pH 6, 20°C, wild-type YPDC | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | catalyzes also carboligase reactions in which the central enamine intermediate reacts with acetaldehyde or pyruvate, instead of the usual proton electrophile, resulting in the formation of acetoin and acetolactate, respectively, typically 1% of the total reaction, stereochemistry of products | Saccharomyces cerevisiae | ? | - |
? | |
| pyruvate | catalytic mechanism, acetaldehyde is produced by protonation of the key C2alpha-carbanion/enamine intermediate | Saccharomyces cerevisiae | acetaldehyde + CO2 | - |
ir | |
| pyruvate | penultimate step of alcohol fermentation | Saccharomyces cerevisiae | acetaldehyde + CO2 | - |
ir | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homotetramer | - |
Saccharomyces cerevisiae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| YPDC | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Saccharomyces cerevisiae |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetic parameters for carboligase reactions of wild-type and mutant YPDC | Saccharomyces cerevisiae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6 | - |
assay at | Saccharomyces cerevisiae |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
wild-type YPDC forms more acetaldehyde at higher pH, followed by a decrease above pH 7 | Saccharomyces cerevisiae |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| thiamine diphosphate | - |
Saccharomyces cerevisiae | |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.45 | - |
pyruvate | pH 6, D28N mutant YPDC | Saccharomyces cerevisiae | |
| 3.04 | - |
pyruvate | pH 6, D28A mutant YPDC | Saccharomyces cerevisiae | |
| 136 | - |
pyruvate | pH 6, E477Q mutant YPDC | Saccharomyces cerevisiae | |
| 433 | - |
pyruvate | pH 6, wild-type YPDC | Saccharomyces cerevisiae | |
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