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Literature summary for 4.1.1.1 extracted from
- Comparison of pyruvate decarboxylases from Saccharomyces cerevisiae and Komagataella pastoris (Pichia pastoris) (2013), Appl. Microbiol. Biotechnol., 97, 9439-9449.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli BL21(DE3)pLysS cells | Komagataella pastoris |
| expressed in Escherichia coli BL21(DE3)pLysS cells | Saccharomyces cerevisiae |
| subcloning in Escherichia coli strain DH5alpha, expression in Escherichia coli strain BL21(DE3)plysS | Komagataella pastoris |
| subcloning in Escherichia coli strain DH5alpha, expression of C-terminally His-tagged isozymes in Escherichia coli strain BL21(DE3)plysS | Saccharomyces cerevisiae |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | growth profile and ethanol production in isozyme knockout strains, overview | Saccharomyces cerevisiae |
General Stability
| General Stability | Organism |
|---|---|
| the highest enzyme activity is in glucose, followed by glycerol, while there is negligible activity on ethanol and methanol as growth medium | Komagataella pastoris |
| the highest enzyme activity is in glucose, followed by glycerol, while there is negligible activity on ethanol and methanol as growth medium | Saccharomyces cerevisiae |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Komagataella pastoris |  |
| Mg2+ | required | Saccharomyces cerevisiae | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 66000 | - |
x * 66000, SDS-PAGE | Komagataella pastoris |
| 66000 | - |
x * 66000, SDS-PAGE | Saccharomyces cerevisiae |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Saccharomyces cerevisiae | apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed | ? | - |
? | |
| additional information | Saccharomyces cerevisiae BY4741 | apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed | ? | - |
? | |
| pyruvate | Saccharomyces cerevisiae | - |
acetaldehyde + CO2 | - |
? | |
| pyruvate | Komagataella pastoris | - |
acetaldehyde + CO2 | - |
? | |
| pyruvate | Saccharomyces cerevisiae BY4741 | - |
acetaldehyde + CO2 | - |
? | |
| pyruvate | Komagataella pastoris GS115 | - |
acetaldehyde + CO2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Komagataella pastoris | - |
- |
- |
| Komagataella pastoris | C4R3T2 | i.e. Komagataella pastoris, has a single isozyme | - |
| Komagataella pastoris GS115 | C4R3T2 | i.e. Komagataella pastoris, has a single isozyme | - |
| Saccharomyces cerevisiae | P06169 | - |
- |
| Saccharomyces cerevisiae | P06169 | isozyme PDC1; pyruvate decarboxylase isozyme 1 | - |
| Saccharomyces cerevisiae | P16467 | - |
- |
| Saccharomyces cerevisiae | P16467 | isozyme PDC5; pyruvate decarboxylase isozyme 2, PDC5 | - |
| Saccharomyces cerevisiae | P26263 | - |
- |
| Saccharomyces cerevisiae | P26263 | isozyme PDC6; pyruvate decarboxylase isozyme 3, PDC6 | - |
| Saccharomyces cerevisiae BY4741 | P06169 | isozyme PDC1; pyruvate decarboxylase isozyme 1 | - |
| Saccharomyces cerevisiae BY4741 | P16467 | isozyme PDC5; pyruvate decarboxylase isozyme 2, PDC5 | - |
| Saccharomyces cerevisiae BY4741 | P26263 | isozyme PDC6; pyruvate decarboxylase isozyme 3, PDC6 | - |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| additional information | growth profile and ethanol production in isozyme knockout strains, overview | Saccharomyces cerevisiae | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
comparison of decarboxylation activities of the PDC isozymes, PDC5 shows the highest activity, overview | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed | Saccharomyces cerevisiae | ? | - |
? | |
| additional information | apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed | Saccharomyces cerevisiae BY4741 | ? | - |
? | |
| pyruvate | - |
Komagataella pastoris | acetaldehyde + CO2 | - |
? | |
| pyruvate | - |
Saccharomyces cerevisiae | acetaldehyde + CO2 | - |
? | |
| pyruvate | - |
Saccharomyces cerevisiae BY4741 | acetaldehyde + CO2 | - |
? | |
| pyruvate | - |
Komagataella pastoris GS115 | acetaldehyde + CO2 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 66000, SDS-PAGE | Komagataella pastoris |
| ? | x * 66000, SDS-PAGE | Saccharomyces cerevisiae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PDC | - |
Komagataella pastoris |
| PDC | - |
Saccharomyces cerevisiae |
| PDC1 | - |
Komagataella pastoris |
| PDC1 | isoform | Saccharomyces cerevisiae |
| Pdc5 | isoform | Saccharomyces cerevisiae |
| Pdc6 | isoform | Saccharomyces cerevisiae |
| scpdc1 | - |
Saccharomyces cerevisiae |
| ScPDC5 | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Saccharomyces cerevisiae |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 8.6 | - |
pyruvate | at pH 7.0 and 25°C | Komagataella pastoris | |
| 65 | - |
pyruvate | isoform PDC6, at pH 7.0 and 25°C | Saccharomyces cerevisiae | |
| 145 | - |
pyruvate | isoform PDC1, at pH 7.0 and 25°C | Saccharomyces cerevisiae | |
| 207 | - |
pyruvate | isoform PDC5, at pH 7.0 and 25°C | Saccharomyces cerevisiae | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.8 | - |
assay at | Saccharomyces cerevisiae |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| thiamine diphosphate | - |
Komagataella pastoris | |
| thiamine diphosphate | - |
Saccharomyces cerevisiae | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | roles of the three isozymes at different phases of Saccharomyces cerevisiae fermentation and with relevance for ethanol and carboligation reactions, overview | Saccharomyces cerevisiae |
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Release 2023.1 (January 2023)
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