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Literature summary extracted from

  • Hajipour, G.; Schowen, K.B.; Schowen, R.L.
    The linkage of catalysis and regulation in enzyme action: oxidative diversion in the hysteretically regulated yeast pyruvate decarboxylase (1999), Bioorg. Med. Chem., 7, 887-894.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.1 2,6-dichlorophenolindophenol 0.1 mM, weak inhibition Saccharomyces cerevisiae

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 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 occupies the branch point between the oxidative metabolism of carbohydrates through the tricarboxylic acid cycle/electron-transport chain and the fermentative metabolism, hysteretically regulated by pyruvate acetaldehyde + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.1 Saccharomyces cerevisiae
-
-
-

Reaction

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.1 fluoropyruvate
-
 Saccharomyces cerevisiae ?
-
 ?
4.1.1.1 additional information oxidative diversion of the decarboxylation of pyruvate by 2,6-dichlorophenolindophenol, which traps a carbanionic intermediate and diverts the product from acetaldehyde to acetate, kinetics Saccharomyces cerevisiae ?
-
 ?
4.1.1.1 pyruvate catalytic cycle, 3 domains: a diphosphate-binding domain, a pyrimidine-binding domain and a regulatory domain, model for enzyme regulation Saccharomyces cerevisiae acetaldehyde + CO2
-
 ?
4.1.1.1 pyruvate enzyme occupies the branch point between the oxidative metabolism of carbohydrates through the tricarboxylic acid cycle/electron-transport chain and the fermentative metabolism, hysteretically regulated by pyruvate Saccharomyces cerevisiae acetaldehyde + CO2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.1.1 SCPDC
-
 Saccharomyces cerevisiae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.1.1 additional information
-
 additional information
-
 Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.1 thiamine diphosphate thiamine diphosphate-dependent enzyme, a diphosphate-binding domain and a pyrimidine-binding domain serve to anchor the cofactor with its thiazolium C2-H bond directed toward the presumed pyruvate binding site, catalytic mechanism Saccharomyces cerevisiae