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Literature summary extracted from

  • Killenberg-Jabs, M.; Kern, G.; Hubner, G.; Golbik, R.
    Folding and stability of different oligomeric states of thiamin diphosphate dependent homomeric pyruvate decarboxylase (2002), Biophys. Chem., 96, 259-271.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.1
-
Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.1 Guanidinium chloride 6 M, denaturates Saccharomyces cerevisiae
4.1.1.1 Urea 8 M, denaturates Saccharomyces cerevisiae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.1 Mg2+ essential for activity, coordinated in the active site at the diphosphate moiety of the coenzyme thiamine diphosphate, also able to coordinate to other specific functional groups than in the active site region, stabilizes the monomeric state of enzyme Saccharomyces cerevisiae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.1 60000
-
1 * 60000, alpha subunit, catalytically inactive form Saccharomyces cerevisiae
4.1.1.1 240000
-
native tetrameric PDC Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.1 Saccharomyces cerevisiae
-
recombinant homomeric, alpha-only, PDC1
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.1 recombinant homomeric, alpha-only, PDC1 Saccharomyces cerevisiae

Renatured (Commentary)

EC Number Renatured (Comment) Organism
4.1.1.1 unfolding and folding kinetics after treatment with urea, reactivation study in terms of dependence on different conditions and additives, reactivation of homomeric PDC requires both refolding to monomers and their correct association to enzymatically active dimers or tetramers Saccharomyces cerevisiae

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
-
-
Saccharomyces cerevisiae

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
4.1.1.1 dimer catalytically active form Saccharomyces cerevisiae
4.1.1.1 heterotetramer native, catalytically active form, dimer of dimers Saccharomyces cerevisiae
4.1.1.1 monomer 1 * 60000, alpha subunit, catalytically inactive form Saccharomyces cerevisiae
4.1.1.1 More different oligomeric states, tetramers, dimers and monomers, of enzyme occur under defined conditions, unfolding kinetics, tetramers dissociate via a stable dimeric state into monomers Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
4.1.1.1 PDC1
-
Saccharomyces cerevisiae

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.1.1.1 10 95 thermal denaturation study Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.1 thiamine diphosphate coenzyme, bound in the interface between two subunits, binds pH-dependently Saccharomyces cerevisiae