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Literature summary for 4.1.1.1 extracted from

  • Killenberg-Jabs, M.; Jabs, A.; Lilie, H.; Golbik, R.; Hubner, G.
    Active oligomeric states of pyruvate decarboxylase and their functional characterization (2001), Eur. J. Biochem., 268, 1698-1704.
    View publication on PubMed
Search for more literature for 4.1.1.1

Activating Compound

Activating Compound Comment Organism Structure
pyruvate allosteric substrate activation, kinetics of dimeric and tetrameric enzyme Saccharomyces cerevisiae

Crystallization (Commentary)

Crystallization (Comment) Organism
X-ray crystallography structure Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ cofactor, tetramer binds 4 Mg2+ ions, tightly bound at pH 6, dissociates reversibly above pH 7 Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
60000
-
 1 * 60000, catalytically inactive enzyme state, SDS-PAGE Saccharomyces cerevisiae
60000
-
 2 * 60000, smallest enzymatically active unit, PDC consists of dimers and tetramers under physiological conditions, subunit interactions, SDS-PAGE Saccharomyces cerevisiae
60000
-
 4 * 60000, native, active enzyme state, dimer of dimers, PDC consists of dimers and tetramers under physiological conditions, subunit interactions, SDS-PAGE Saccharomyces cerevisiae
240000
-
 tetramer Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pyruvate Saccharomyces cerevisiae enzyme within the glycolytic pathway in fermenting cells acetaldehyde + CO2
-
 ?

Organic Solvent Stability

Organic Solvent Comment Organism
urea treatment with 0.5 M urea results in dimeric, with 2 M urea in monomeric enzyme state Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 no difference in specific activity of dimeric and tetrameric enzyme state Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate
-
 Saccharomyces cerevisiae acetaldehyde + CO2
-
 ?
pyruvate enzyme within the glycolytic pathway in fermenting cells Saccharomyces cerevisiae acetaldehyde + CO2
-
 ?

Subunits

Subunits Comment Organism
homodimer 2 * 60000, smallest enzymatically active unit, PDC consists of dimers and tetramers under physiological conditions, subunit interactions, SDS-PAGE Saccharomyces cerevisiae
homotetramer 4 * 60000, native, active enzyme state, dimer of dimers, PDC consists of dimers and tetramers under physiological conditions, subunit interactions, SDS-PAGE Saccharomyces cerevisiae
monomer 1 * 60000, catalytically inactive enzyme state, SDS-PAGE Saccharomyces cerevisiae
More treatment with 0.5 M urea results in dimeric, with 2 M urea in monomeric enzyme state Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
PDC
-
 Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.8
-
 dimer and tetramer Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate requirement, tetramer binds 4 molecules, at the interface between two monomers involving the alpha and gamma domains, tightly bound at pH 6, dissociates reversibly above pH 7 Saccharomyces cerevisiae