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Literature summary for 4.1.1.1 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
Search for more literature for 4.1.1.1

Inhibitors

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

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Reaction

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
fluoropyruvate
-
 Saccharomyces cerevisiae ?
-
 ?
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 ?
-
 ?
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
-
 ?
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

Synonyms Comment Organism
SCPDC
-
 Saccharomyces cerevisiae

Turnover Number [1/s]

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

Cofactor

Cofactor Comment Organism Structure
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