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Literature summary for 4.1.1.1 extracted from

  • de Assis, L.J.; Zingali, R.B.; Masuda, C.A.; Rodrigues, S.P.; Montero-Lomeli, M.
    Pyruvate decarboxylase activity is regulated by the Ser/Thr protein phosphatase Sit4p in the yeast Saccharomyces cerevisiae (2013), FEMS Yeast Res., 13, 518-528.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
additional information dephosphorylation of Pdc1p by alkaline phosphatase inhibits the enzyme activity by 50% Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3 6 pyruvate pH 6.0, 37°C Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-
Saccharomyces cerevisiae BY4741
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein Pdc1p is subject to reversible phosphorylation at Ser223 that is dependent on glucose availability, dephosphorylation of Pdc1p by alkaline phosphatase inhibits the enzyme activity by 50%. Phosphorylation of Pdc1p is dependent on the growth phase, being hyperphosphorylated in the logarithmic phase, dependent on the presence of Ser/Thr protein phosphatase SIT4p. The Ser/Thr protein phosphatase SIT4 reduces Pdc1p activity by altering the apparent affinity for the cofactor thiamine pyrophosphate Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
Pdc1p
-
Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
assay at Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate required, the Ser/Thr protein phosphatase SIT4 reduces Pdc1p activity by altering the apparent affinity for the cofactor thiamine pyrophosphate Saccharomyces cerevisiae

General Information

General Information Comment Organism
malfunction deletion of the Ser/Thr protein phosphatase SIT4 phosphatase decreases the pyruvate decarboxylase activity Saccharomyces cerevisiae
metabolism pyruvate decarboxylase activity is regulated by the Ser/Thr protein phosphatase Sit4p in the yeast Saccharomyces cerevisiae, mechanism of regulation of pyruvate decarboxylase activity, overview Saccharomyces cerevisiae
physiological function the enzyme is essential for directing the glucose flux to ethanol production. The activity of Pdc1p is regulated by phosphorylation of serine residues during growth Saccharomyces cerevisiae