Literature summary for 4.1.1.1 extracted from
Chang, A.K.; Nixon, P.F.; Duggleby, R.G.
Aspartate-27 and glutamate-473 are involved in catalysis by Zymomonas mobilis pyruvate decarboxylase (1999), Biochem. J., 339, 255-260.
No PubMed abstract available
Cloned(Commentary)
Cloned (Comment) |
Organism |
expression of PDC mutants D27E, D27N, E473D and E473Q in Escherichia coli |
Zymomonas mobilis |
Protein Variants
Protein Variants |
Comment |
Organism |
D27E |
0.072% of wild-type specific activity, small decrease in affinity for cofactors thiamine diphosphate and Mg2+, kinetic properties, mutation slows the decarboxylation step |
Zymomonas mobilis |
D27N |
0.049% of wild-type specific activity, small decrease in affinity for cofactors thiamine diphosphate and Mg2+, kinetic properties, mutation slows the decarboxylation step |
Zymomonas mobilis |
E473D |
0.173% of wild-type specific activity, small decrease in affinity for cofactors thiamine diphosphate and Mg2+, kinetic properties, mutation slows the decarboxylation step |
Zymomonas mobilis |
E473Q |
0.025% of wild-type specific activity, more tightly bound cofactors thiamine diphosphate and Mg2+, kinetic properties, mutation slows the decarboxylation step |
Zymomonas mobilis |
E50D |
2.9% of wild-type activity |
Zymomonas mobilis |
E50Q |
0.46% of wild-type activity |
Zymomonas mobilis |
KM Value [mM]
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Comment |
Organism |
Structure |
additional information |
- |
additional information |
kinetic data |
Zymomonas mobilis |
|
0.18 |
0.2 |
pyruvate |
30°C, E473D mutant PDC |
Zymomonas mobilis |
|
0.25 |
- |
pyruvate |
30°C, D27E mutant PDC |
Zymomonas mobilis |
|
0.43 |
0.48 |
pyruvate |
30°C, D27N mutant PDC |
Zymomonas mobilis |
|
0.66 |
0.68 |
pyruvate |
30°C, wild-type PDC |
Zymomonas mobilis |
|
1.04 |
1.17 |
pyruvate |
30°C, E473Q mutant PDC |
Zymomonas mobilis |
|
Metals/Ions
Metals/Ions |
Comment |
Organism |
Structure |
Mg2+ |
cofactor, mode of active site binding, contains 1 mol Mg2+ per subunit |
Zymomonas mobilis |
|
Molecular Weight [Da]
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
60000 |
- |
4 * 60000, wild-type PDC and mutants D27E, D27N, E473D and E473Q, SDS-PAGE |
Zymomonas mobilis |
240000 |
- |
wild-type and E473Q mutant 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 |
catalyzes the penultimate step in ethanol fermentation |
acetaldehyde + CO2 |
- |
? |
|
Organism
Organism |
UniProt |
Comment |
Textmining |
Zymomonas mobilis |
- |
- |
- |
Purification (Commentary)
Purification (Comment) |
Organism |
PDC mutants D27E, D27N, E473D and E473Q |
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. |
pyruvate |
active site structure, catalytic mechanism |
Zymomonas mobilis |
acetaldehyde + CO2 |
- |
? |
|
pyruvate |
catalyzes the penultimate step in ethanol fermentation |
Zymomonas mobilis |
acetaldehyde + CO2 |
- |
? |
|
Subunits
Subunits |
Comment |
Organism |
tetramer |
4 * 60000, wild-type PDC and mutants D27E, D27N, E473D and E473Q, 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 |
Cofactor
Cofactor |
Comment |
Organism |
Structure |
thiamine diphosphate |
mode of active site binding, contains 1 mol thiamine diphosphate per subunit |
Zymomonas mobilis |
|