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 (Comment) | Organism |
---|---|
expression of W412F and W412A mutant PDC in Escherichia coli BL21(DE3) | Saccharomyces cerevisiae |
Crystallization (Comment) | Organism |
---|---|
- |
Saccharomyces cerevisiae |
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 | Organism |
---|---|
central role of the beta domain in stabilizing the overall structure | Saccharomyces cerevisiae |
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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
pyruvate | Saccharomyces cerevisiae | - |
acetaldehyde + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Purification (Comment) | Organism |
---|---|
W412F and W412A mutant PDC, expressed in Escherichia coli, W412A is purified as apoenzyme | Saccharomyces cerevisiae |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
a 2-oxo carboxylate = an aldehyde + CO2 | mechanism | Saccharomyces cerevisiae |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
- |
Saccharomyces cerevisiae |
Storage Stability | Organism |
---|---|
4°C, wild-type and W412F mutant PDC, several months, stable | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pyruvate | - |
Saccharomyces cerevisiae | acetaldehyde + CO2 | - |
? | |
pyruvate | mechanism | Saccharomyces cerevisiae | acetaldehyde + CO2 | - |
ir |
Subunits | Comment | Organism |
---|---|---|
tetramer | - |
Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
PDC | - |
Saccharomyces cerevisiae |
scpdc1 | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Saccharomyces cerevisiae |
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 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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
- |
Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
thiamine diphosphate | requirement, located at the active site at the interface of the alpha and gamma domains | Saccharomyces cerevisiae |