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Literature summary for 4.1.1.1 extracted from
- Pyruvate decarboxylase from Kluyveromyces lactis. An enzyme with an extraordinary substrate activation behaviour (2002), Eur. J. Biochem., 269, 3256-3263.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| Pyruvamide | artificial activator | Kluyveromyces lactis |  |
| pyruvate | concentration-dependent substrate activation, minimum at 1.5 mM, mechanism, kinetics | Kluyveromyces lactis | |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Pyruvamide | mixed type inhibitor | Kluyveromyces lactis | |
| pyruvate | weak substrate inhibition, above 100 mM | Kluyveromyces lactis | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetic studies | Kluyveromyces lactis | |
| 0.24 | - |
pyruvate | pH 6, 30°C | Kluyveromyces lactis | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytosol | - |
Kluyveromyces lactis | 5829 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | cofactor, requirement | Kluyveromyces lactis | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 61500 | - |
4 * 61500, mass spectrometry, SDS-PAGE, 4 * 61821, calculated from the amino acid sequence | Kluyveromyces lactis |
| 61821 | - |
4 * 61500, mass spectrometry, SDS-PAGE, 4 * 61821, calculated from the amino acid sequence | Kluyveromyces lactis |
| 200000 | - |
about, gel filtration | Kluyveromyces lactis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| pyruvate | Kluyveromyces lactis | key enzyme at the branching point of alcoholic fermentation and respiration, expression at high glucose and low oxygen concentration | acetaldehyde + CO2 | - |
? | |
| pyruvate | Kluyveromyces lactis JA-6 | key enzyme at the branching point of alcoholic fermentation and respiration, expression at high glucose and low oxygen concentration | acetaldehyde + CO2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Kluyveromyces lactis | - |
- |
- |
| Kluyveromyces lactis JA-6 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Kluyveromyces lactis |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| a 2-oxo carboxylate = an aldehyde + CO2 | catalytic mechanism | Kluyveromyces lactis |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
- |
Kluyveromyces lactis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| pyruvate | catalytic mechanism, contains catalytic and regulatory pyruvate binding site | Kluyveromyces lactis | acetaldehyde + CO2 | - |
? | |
| pyruvate | key enzyme at the branching point of alcoholic fermentation and respiration, expression at high glucose and low oxygen concentration | Kluyveromyces lactis | acetaldehyde + CO2 | - |
? | |
| pyruvate | catalytic mechanism, contains catalytic and regulatory pyruvate binding site | Kluyveromyces lactis JA-6 | acetaldehyde + CO2 | - |
? | |
| pyruvate | key enzyme at the branching point of alcoholic fermentation and respiration, expression at high glucose and low oxygen concentration | Kluyveromyces lactis JA-6 | acetaldehyde + CO2 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| tetramer | 4 * 61500, mass spectrometry, SDS-PAGE, 4 * 61821, calculated from the amino acid sequence | Kluyveromyces lactis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| KlPDC | - |
Kluyveromyces lactis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Kluyveromyces lactis |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 40 | - |
pyruvate | pH 6, 30°C, enzyme monomer | Kluyveromyces lactis | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6 | - |
assay at | Kluyveromyces lactis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| thiamine diphosphate | requirement | Kluyveromyces lactis | |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1200 | - |
pyruvate | pH 6, 30°C | Kluyveromyces lactis | |
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Release 2023.1 (January 2023)
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