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Literature summary for 4.1.1.1 extracted from
- Folding and stability of different oligomeric states of thiamin diphosphate dependent homomeric pyruvate decarboxylase (2002), Biophys. Chem., 96, 259-271.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
- |
Saccharomyces cerevisiae |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Guanidinium chloride | 6 M, denaturates | Saccharomyces cerevisiae |  |
| Urea | 8 M, denaturates | Saccharomyces cerevisiae | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | essential for activity, coordinated in the active site at the diphosphate moiety of the coenzyme thiamine diphosphate, also able to coordinate to other specific functional groups than in the active site region, stabilizes the monomeric state of enzyme | Saccharomyces cerevisiae | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 60000 | - |
1 * 60000, alpha subunit, catalytically inactive form | Saccharomyces cerevisiae |
| 240000 | - |
native tetrameric PDC | Saccharomyces cerevisiae |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| pyruvate | Saccharomyces cerevisiae | enzyme within the glycolytic pathway in fermenting cells | acetaldehyde + CO2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
recombinant homomeric, alpha-only, PDC1 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant homomeric, alpha-only, PDC1 | Saccharomyces cerevisiae |
Renatured (Commentary)
| Renatured (Comment) | Organism |
|---|---|
| unfolding and folding kinetics after treatment with urea, reactivation study in terms of dependence on different conditions and additives, reactivation of homomeric PDC requires both refolding to monomers and their correct association to enzymatically active dimers or tetramers | 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 |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| pyruvate | - |
Saccharomyces cerevisiae | acetaldehyde + CO2 | - |
? | |
| pyruvate | enzyme within the glycolytic pathway in fermenting cells | Saccharomyces cerevisiae | acetaldehyde + CO2 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | catalytically active form | Saccharomyces cerevisiae |
| heterotetramer | native, catalytically active form, dimer of dimers | Saccharomyces cerevisiae |
| monomer | 1 * 60000, alpha subunit, catalytically inactive form | Saccharomyces cerevisiae |
| More | different oligomeric states, tetramers, dimers and monomers, of enzyme occur under defined conditions, unfolding kinetics, tetramers dissociate via a stable dimeric state into monomers | Saccharomyces cerevisiae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PDC1 | - |
Saccharomyces cerevisiae |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 10 | 95 | thermal denaturation study | Saccharomyces cerevisiae |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| thiamine diphosphate | coenzyme, bound in the interface between two subunits, binds pH-dependently | Saccharomyces cerevisiae | |
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