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Literature summary for 4.1.1.1 extracted from
- Effects of substitution of tryptophan 412 in the substrate activation pathway of yeast pyruvate decarboxylase (1999), Biochemistry, 38, 10004-10012.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| pyruvate | substrate activation pathway from C221 to H92 to E91 to W412 to G413 to thiamine diphosphate, role of W412 | Saccharomyces cerevisiae |  |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of W412F and W412A mutant PDC in Escherichia coli BL21(DE3) | Saccharomyces cerevisiae |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
- |
Saccharomyces cerevisiae |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| W412A | mutant with 10fold reduced specific activity, reduced turnover number and catalytic efficiency, very much reduced substrate activation, reduced affinity for thiamine diphosphate, reduced stability | Saccharomyces cerevisiae |
| W412F | mutant with 4fold reduced specific activity, reduced turnover number and catalytic efficiency | Saccharomyces cerevisiae |
General Stability
| General Stability | Organism |
|---|---|
| central role of the beta domain in stabilizing the overall structure | Saccharomyces cerevisiae |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetic data, pH-dependence of steady-state kinetic parameters of wild-type, W412F and W412A mutant PDC | Saccharomyces cerevisiae |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| pyruvate | Saccharomyces cerevisiae | - |
acetaldehyde + CO2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| W412F and W412A mutant PDC, expressed in Escherichia coli, W412A is purified as apoenzyme | Saccharomyces cerevisiae |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| a 2-oxo carboxylate = an aldehyde + CO2 | mechanism | 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 |
Storage Stability
| Storage Stability | Organism |
|---|---|
| 4°C, wild-type and W412F mutant PDC, several months, stable | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| pyruvate | - |
Saccharomyces cerevisiae | acetaldehyde + CO2 | - |
? | |
| pyruvate | mechanism | Saccharomyces cerevisiae | acetaldehyde + CO2 | - |
ir | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| tetramer | - |
Saccharomyces cerevisiae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PDC | - |
Saccharomyces cerevisiae |
| scpdc1 | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Saccharomyces cerevisiae |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
Tm, W412A mutant PDC | Saccharomyces cerevisiae |
| 51.5 | - |
Tm, W412F mutant PDC | Saccharomyces cerevisiae |
| 59.5 | - |
Tm, wild-type PDC | Saccharomyces cerevisiae |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kcat values at different pH values from pH 4.5 to 7.5 of wild-type, W412F and W412A mutant PDC | Saccharomyces cerevisiae | |
| 0.03 | 0.55 | pyruvate | pH 6, 25°C, W412A mutant PDC | Saccharomyces cerevisiae | |
| 2.1 | - |
pyruvate | pH 6, 25°C, wild-type PDC | Saccharomyces cerevisiae | |
| 6.55 | - |
pyruvate | pH 6, 25°C, W412A mutant PDC | Saccharomyces cerevisiae | |
| 17.8 | - |
pyruvate | pH 6, 25°C, W412F mutant PDC | Saccharomyces cerevisiae | |
| 73.1 | - |
pyruvate | pH 6, 25°C, wild-type PDC | Saccharomyces cerevisiae | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6 | - |
- |
Saccharomyces cerevisiae |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| thiamine diphosphate | requirement, located at the active site at the interface of the alpha and gamma domains | Saccharomyces cerevisiae | |
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