Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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)

EC Number Cloned (Comment) Organism
4.1.1.1 expression of PDC mutants D27E, D27N, E473D and E473Q in Escherichia coli Zymomonas mobilis

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.1 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
4.1.1.1 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
4.1.1.1 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
4.1.1.1 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
4.1.1.1 E50D 2.9% of wild-type activity Zymomonas mobilis
4.1.1.1 E50Q 0.46% of wild-type activity Zymomonas mobilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.1 additional information
-
 additional information kinetic data Zymomonas mobilis
4.1.1.1 0.18 0.2 pyruvate 30°C, E473D mutant PDC Zymomonas mobilis
4.1.1.1 0.25
-
 pyruvate 30°C, D27E mutant PDC Zymomonas mobilis
4.1.1.1 0.43 0.48 pyruvate 30°C, D27N mutant PDC Zymomonas mobilis
4.1.1.1 0.66 0.68 pyruvate 30°C, wild-type PDC Zymomonas mobilis
4.1.1.1 1.04 1.17 pyruvate 30°C, E473Q mutant PDC Zymomonas mobilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.1 Mg2+ cofactor, mode of active site binding, contains 1 mol Mg2+ per subunit Zymomonas mobilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.1 60000
-
 4 * 60000, wild-type PDC and mutants D27E, D27N, E473D and E473Q, SDS-PAGE Zymomonas mobilis
4.1.1.1 240000
-
 wild-type and E473Q mutant PDC, gel filtration Zymomonas mobilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.1 pyruvate Zymomonas mobilis catalyzes the penultimate step in ethanol fermentation acetaldehyde + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.1 Zymomonas mobilis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.1 PDC mutants D27E, D27N, E473D and E473Q Zymomonas mobilis

Reaction

EC Number Reaction Comment Organism Reaction ID
4.1.1.1 a 2-oxo carboxylate = an aldehyde + CO2 catalytic mechanism Zymomonas mobilis
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.1.1.1 additional information
-
-
 Zymomonas mobilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.1 pyruvate active site structure, catalytic mechanism Zymomonas mobilis acetaldehyde + CO2
-
 ?
4.1.1.1 pyruvate catalyzes the penultimate step in ethanol fermentation Zymomonas mobilis acetaldehyde + CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.1.1 tetramer 4 * 60000, wild-type PDC and mutants D27E, D27N, E473D and E473Q, SDS-PAGE Zymomonas mobilis

Synonyms

EC Number Synonyms Comment Organism
4.1.1.1 PDC
-
 Zymomonas mobilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.1.1 30
-
 assay at Zymomonas mobilis

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.1 thiamine diphosphate mode of active site binding, contains 1 mol thiamine diphosphate per subunit Zymomonas mobilis