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Literature summary for 4.1.1.1 extracted from
- Effects of deletions at the carboxyl terminus of Zymomonas mobilis pyruvate decarboxylase on the kinetic properties and substrate specificity (2000), Biochemistry, 39, 9430-9437.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of wild-type PDC and C-terminal deletion mutants in Escherichia coli | Zymomonas mobilis |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystal structure | Zymomonas mobilis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | engineering of 15 variants of PDC with several deletions at the C-terminus, properties of the mutants, kinetic data | Zymomonas mobilis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | values for several C-terminal deletion mutants, kinetic model of the catalytic cycle | Zymomonas mobilis | |
| 0.68 | - |
pyruvate | 30°C, wild-type PDC | Zymomonas mobilis |  |
| 2.86 | - |
2-Ketobutyrate | 30°C, wild-type PDC | Zymomonas mobilis | |
| 12.9 | - |
2-ketovalerate | 30°C, wild-type PDC | Zymomonas mobilis | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | cofactor, activates | Zymomonas mobilis | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 60800 | - |
4 * 60800, wild-type PDC, SDS-PAGE | Zymomonas mobilis |
| 200000 | - |
about, wild-type PDC, gel filtration | Zymomonas mobilis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| pyruvate | Zymomonas mobilis | - |
acetaldehyde + CO2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Zymomonas mobilis | P06672 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| 5 C-terminal deletion mutants | Zymomonas mobilis |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| a 2-oxo carboxylate = an aldehyde + CO2 | catalytic mechanism | Zymomonas mobilis |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
- |
Zymomonas mobilis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2-ketobutyrate | lower activity than with pyruvate | Zymomonas mobilis | ? | - |
? | |
| 2-ketovalerate | lower activity than with pyruvate | Zymomonas mobilis | ? | - |
? | |
| pyruvate | - |
Zymomonas mobilis | acetaldehyde + CO2 | - |
? | |
| pyruvate | C-terminal region occludes the active site, enzyme structure, catalytic cycle, active site closure is required for decarboxylation | Zymomonas mobilis | acetaldehyde + CO2 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homotetramer | 4 * 60800, wild-type PDC, SDS-PAGE | Zymomonas mobilis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PDC | - |
Zymomonas mobilis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Zymomonas mobilis |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | values for several C-terminal deletion mutants | Zymomonas mobilis | |
| 9 | - |
2-Ketobutyrate | 30°C, wild-type PDC | Zymomonas mobilis | |
| 13.7 | - |
2-ketovalerate | 30°C, wild-type PDC | Zymomonas mobilis | |
| 61.4 | - |
2-Ketobutyrate | 30°C, wild-type PDC | Zymomonas mobilis | |
| 113 | - |
pyruvate | 30°C, wild-type PDC | Zymomonas mobilis | |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| thiamine diphosphate | cofactor activation | Zymomonas mobilis | |
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