Activating Compound | Comment | Organism | Structure |
---|---|---|---|
Pyruvamide | a substrate activator surrogate, activates, a flexible loop spanning residues 290 to 304 on the beta-domain of the enzyme, not seen in the absence of pyruvamide, occurs in presence of the activator, residues on the loop affect the enzyme activity, conformational equilibrium between the open and closed conformations of the enzyme identified in the pyruvamide-activated structure | Saccharomyces cerevisiae |
Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Saccharomyces cerevisiae |
Protein Variants | Comment | Organism |
---|---|---|
D291A | site-directed mutagenesis, the mutant shows altered kinetics with highly reduced kcat compared to the wild-type enzyme | Saccharomyces cerevisiae |
D291N | site-directed mutagenesis, the mutant shows altered kinetics with highly reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
L111A | site-directed mutagenesis, the mutant shows 47% of the wild-type kcat | Saccharomyces cerevisiae |
L111Q | site-directed mutagenesis, the mutant shows 73% of the wild-type kcat | Saccharomyces cerevisiae |
L111V | site-directed mutagenesis, the mutant shows 21% of the wild-type kcat | Saccharomyces cerevisiae |
additional information | construction of mutant pdc-803 with a S296DELTAF297DELTA deletion, the mutant shows highly reduced activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
N293A | site-directed mutagenesis, the mutant shows altered kinetics with highly reduced kcat compared to the wild-type enzyme | Saccharomyces cerevisiae |
S298A | site-directed mutagenesis, the mutant shows altered kinetics with highly reduced kcat compared to the wild-type enzyme | Saccharomyces cerevisiae |
S300A | site-directed mutagenesis, the mutant shows altered kinetics with slightly reduced kcat compared to the wild-type enzyme | Saccharomyces cerevisiae |
T294A | site-directed mutagenesis, the mutant shows altered kinetics with highly reduced kcat compared to the wild-type enzyme | Saccharomyces cerevisiae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | pre-steady-state and steady-state kinetics of recombinant wild-type and mutant enzymes, overview | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3) | Saccharomyces cerevisiae |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
a 2-oxo carboxylate = an aldehyde + CO2 | reaction mechanism, overview | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | in the pyruvamide-activated enzyme form, the flexible loop located on the beta-domain can transfer information to the active center thiamine diphosphate located at the interface of the alpha and gamma domains, overview | Saccharomyces cerevisiae | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | conformational equilibrium between the open and closed conformations of the enzyme identified in the pyruvamide-activated structure | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
pyruvamide-activated yeast pyruvate decarboxylase | - |
Saccharomyces cerevisiae |
YPDC | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
31 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.6 | - |
wild-type enzyme | Saccharomyces cerevisiae |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
5.1 | 7.5 | - |
Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
thiamine diphosphate | bound to the active site located at the interface of the alpha and gamma domains | Saccharomyces cerevisiae |