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Literature summary for 4.1.1.1 extracted from

  • Sergienko, E.A.; Jordan, F.
    New model for activation of yeast pyruvate decarboxylase by substrate consistent with the alternating sites mechanism: demonstration of the existence of two active forms of the enzyme (2002), Biochemistry, 41, 3952-3967.
    View publication on PubMed
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Activating Compound

Activating Compound Comment Organism Structure
Pyruvamide activates, pyruvate and pyruvamide have different activation pathways with distinct binding sites Saccharomyces cerevisiae
pyruvate allosteric substrate activation, alternating sites mechanism, random binding of pyruvate in the regulatory and active site, regulatory pyruvate is first bound to C-221 on the beta domain, binding generates a signal which is transmitted to the thiamine diphosphate cofactor, signal pathway, study of the pH-dependence of activation, two-step phenomenological model of activation, kinetics, pyruvate and pyruvamide have different activation pathways with distinct binding sites Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
E477Q active site mutant, kinetics, activation study of mutant enzyme Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
pyruvate
-
 Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic model, Km values for different conformations of wild-type enzyme at different pH values between pH 4.5 and 6.5 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
YPDC variants Saccharomyces cerevisiae

Reaction

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme catalyzes a carboligase reaction as side reaction forming acetoin and acetolactate Saccharomyces cerevisiae ?
-
 ?
pyruvate
-
 Saccharomyces cerevisiae acetaldehyde + CO2
-
 ?
pyruvate detailed mechanism, catalytic cycle, alternating sites mechanism based on tight communication between active sites of the functional dimer, with the ionizable residues D28, E477 and H115 likely to be important in creating this communication, enzyme exists in three conformations, one inactive and two active forms, enzyme structure Saccharomyces cerevisiae acetaldehyde + CO2
-
 ir

Subunits

Subunits Comment Organism
homotetramer dimer of dimers, minimal catalytic unit is a functional dimer Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
YPDC
-
 Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information kinetic model, kcat values for different conformations of wild-type enzyme at different pH values between pH 4.5 and 6.5 Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate requirement, cofactor is located between the alpha and the gamma domains Saccharomyces cerevisiae