Title : Pyruvate decarboxylase activity is regulated by the Ser/Thr protein phosphatase Sit4p in the yeast Saccharomyces cerevisiae.

Pub. Date : 2013 Sep

PMID : 23692511






4 Functional Relationships(s)
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Protein Name
Organism
1 Immunoblot analyses using anti-phosphoserine antibodies against the affinity-purified Pdc1p showed that Pdc1p is a phosphoenzyme. Phosphoserine indolepyruvate decarboxylase 1 Saccharomyces cerevisiae S288C
2 Immunoblot analyses using anti-phosphoserine antibodies against the affinity-purified Pdc1p showed that Pdc1p is a phosphoenzyme. Phosphoserine indolepyruvate decarboxylase 1 Saccharomyces cerevisiae S288C
3 These results suggest that the Pdc1p phosphorylation dependent on SIT4 occurs at residues that change the apparent affinity for TPP and pyruvate. Thiamine Pyrophosphate indolepyruvate decarboxylase 1 Saccharomyces cerevisiae S288C
4 These results suggest that the Pdc1p phosphorylation dependent on SIT4 occurs at residues that change the apparent affinity for TPP and pyruvate. Pyruvic Acid indolepyruvate decarboxylase 1 Saccharomyces cerevisiae S288C