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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
Search for more literature for 4.1.1.1

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
a

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