Protein Variants | Comment | Organism |
---|---|---|
C221E/C222A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
D28A | site-directed mutagenesis of the active site residue, the mutant shows reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
D28N | site-directed mutagenesis of the active site residue, the mutant shows reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
E477Q | site-directed mutagenesis of the active site residue, the mutant shows reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
E51A | site-directed mutagenesis of the active site residue, the mutant shows reduced activity compared to the wild-type enzyme,and the mutant is no longer capable of forming a hydrogen bond with cofactor thiamine diphosphate | Saccharomyces cerevisiae |
E51D | site-directed mutagenesis of the active site residue, the mutant is still capable of forming a hydrogen bond with cofactor thiamine diphosphate, albeit weaker, and shows reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
E51N | site-directed mutagenesis of the active site residue, the mutant is still capable of forming a hydrogen bond with cofactor thiamine diphosphate, albeit weaker, and shows reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
E51Q | site-directed mutagenesis of the active site residue, the mutant is still capable of forming a hydrogen bond with cofactor thiamine diphosphate, albeit weaker, and shows reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
E91D | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | transient state, pre-steady-state, and steady-state complex formations of substrate/intermediate and thiamine diphosphate cofactor and of kinetics of wild-type and mutant enzymes, overview | Saccharomyces cerevisiae | |
0.72 | - |
pyruvate | per subunit, pH 6.0, 30°C, mutant E51A | Saccharomyces cerevisiae | |
1.1 | - |
pyruvate | per subunit, pH 6.0, 30°C, wild-type enzyme | Saccharomyces cerevisiae | |
1.47 | - |
pyruvate | per subunit, pH 6.0, 30°C, mutant C221E/C222A | Saccharomyces cerevisiae | |
1.66 | - |
pyruvate | per subunit, pH 6.0, 30°C, mutant D28A | Saccharomyces cerevisiae | |
1.79 | - |
pyruvate | per subunit, pH 6.0, 30°C, mutant E91D | Saccharomyces cerevisiae | |
3.02 | - |
pyruvate | per subunit, pH 6.0, 30°C, mutant E477Q | Saccharomyces cerevisiae | |
14.9 | - |
pyruvate | per subunit, pH 6.0, 30°C, mutant E51Q | Saccharomyces cerevisiae | |
23.1 | - |
pyruvate | per subunit, pH 6.0, 30°C, mutant E51D | Saccharomyces cerevisiae | |
31.5 | - |
pyruvate | per subunit, pH 6.0, 30°C, mutant E51N | Saccharomyces cerevisiae |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | 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 | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
a 2-oxo carboxylate = an aldehyde + CO2 | mechanism of catalytic cycle of yeast pyruvate decarboxylase, overview. Pyruvate and analogues induce active site asymmetry in the wild-type yeast enzyme and mutant variants. The rare 1',4'-iminopyrimidine thiamine diphosphate tautomer participates in formation of thiamine diphosphate-bound intermediates. Propionylphosphinate also binds at the regulatory site and its binding is reflected by catalytic events at the active site 20 A away. The yeast enzyme stabilizes an electrostatic model for the 4'-aminopyrimidinium ionization state, an important contribution of the protein to catalysis | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pyruvate | - |
Saccharomyces cerevisiae | acetaldehyde + CO2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer or tetramer | a tight dimer, known as the functional dimer, is the minimal catalytically active unit, two of these functional dimers assemble into a loose tetramer in the quaternary structure | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
yeast pyruvate decarboxylase | - |
Saccharomyces cerevisiae |
YPDC | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Saccharomyces cerevisiae |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0024 | - |
pyruvate | per subunit, pH 6.0, 30°C, mutant E51N | Saccharomyces cerevisiae | |
0.0043 | - |
pyruvate | per subunit, pH 6.0, 30°C, mutant E51A | Saccharomyces cerevisiae | |
0.035 | - |
pyruvate | per subunit, pH 6.0, 30°C, mutant E51Q | Saccharomyces cerevisiae | |
0.049 | - |
pyruvate | per subunit, pH 6.0, 30°C, mutant E51D | Saccharomyces cerevisiae | |
0.066 | - |
pyruvate | per subunit, pH 6.0, 30°C, mutant D28A | Saccharomyces cerevisiae | |
0.086 | - |
pyruvate | per subunit, pH 6.0, 30°C, mutant E477Q | Saccharomyces cerevisiae | |
11 | - |
pyruvate | per subunit, pH 6.0, 30°C, mutant E91D | Saccharomyces cerevisiae | |
18.2 | - |
pyruvate | per subunit, pH 6.0, 30°C, mutant C221E/C222A | Saccharomyces cerevisiae | |
60 | - |
pyruvate | per subunit, pH 6.0, 30°C, wild-type enzyme | Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
assay at | Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
thiamine diphosphate | bound in the V conformation in the active sites of the enzyme, side chains of residues Glu51, Glu477, Asp28, His114, and His 115 potentially participate in proton transfer steps | Saccharomyces cerevisiae |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme is a member of the superfamily of thiamine diphosphate-dependent enzymes | Saccharomyces cerevisiae |