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Literature summary for 4.1.1.1 extracted from

  • Sergienko, E.A.; Jordan, F.
    Catalytic acid-base groups in yeast pyruvate decarboxylase. 3. A steady-state kinetic model consistent with the behavior of both wild-type and variant enzymes at all relevant pH values (2001), Biochemistry, 40, 7382-7403.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
Pyruvamide activation mechanism, binds only at the regulatory site, but with lower affinity than does pyruvate Saccharomyces cerevisiae
pyruvate allosteric substrate activation, activation mechanism Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
C221A mutant lacking the binding site for the regulatory pyruvate molecule with 25% of wild-type activity at pH 6 Saccharomyces cerevisiae
C221D mutant with nearly wild-type activity, hyperbolic kinetics Saccharomyces cerevisiae
C221E mutant with nearly wild-type activity, hyperbolic kinetics Saccharomyces cerevisiae
C221S mutant lacking the binding site for the regulatory pyruvate molecule with 25% of wild-type activity at pH 6 Saccharomyces cerevisiae
D28A active site mutant, kinetic properties, effect of the mutation on the activation/inhibition properties of pyruvate Saccharomyces cerevisiae
D28N active site mutant, kinetic properties, effect of the mutation on the activation/inhibition properties of pyruvate Saccharomyces cerevisiae
E477Q active site mutant, kinetic properties, effect of the mutation on the activation/inhibition properties of pyruvate Saccharomyces cerevisiae
E51D mutant with 50% of wild-type acetaldehyde producing activity Saccharomyces cerevisiae
H114F active site mutant Saccharomyces cerevisiae
H115F active site mutant Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
pyruvate modest substrate inhibition at high concentrations Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic model, kinetic data Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ cofactor, requirement Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pyruvate Saccharomyces cerevisiae
-
acetaldehyde + CO2
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharomyces cerevisiae

Reaction

Reaction Comment Organism Reaction ID
a 2-oxo carboxylate = an aldehyde + CO2 mechanism, catalyzes carboligation as side reaction Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme catalyzes also a carboligation as side reaction producing acetoin and acetolactate, mechanism, not: pyruvamide Saccharomyces cerevisiae ?
-
?
pyruvate
-
Saccharomyces cerevisiae acetaldehyde + CO2
-
?
pyruvate detailed mechanism with roles for the active center acid-base groups D28, E477, H114 and H115, catalytic cycle, mechanistic model of the reaction, alternating sites model Saccharomyces cerevisiae acetaldehyde + CO2
-
ir

Subunits

Subunits Comment Organism
homotetramer dimer of dimers, the minimal catalytic unit is the dimer with its active sites are not acting independently of one another, alternating sites model Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
YPDC
-
Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.8 6 wild-type YPDC Saccharomyces cerevisiae

pH Range

pH Minimum pH Maximum Comment Organism
5.5 7.2 nearly identical Vmax values in the pH range, wild-type YPDC Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate requirement, bound at the interface created by 2 subunits that form a tight dimer, mode of binding Saccharomyces cerevisiae

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
additional information
-
Saccharomyces cerevisiae
3.75
-
pyruvate D28A mutant YPDC Saccharomyces cerevisiae
112.2
-
pyruvate pH 6, E477Q mutant YPDC Saccharomyces cerevisiae