PDC2 | Pyruvate decarboxylase 2
AS10 691 | Clonality: Polyclonal | Host: Rabbit | Reactivity: A. thaliana, O. sativa, Z. mobilis
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Product Information
KLH-conjugated peptide derived from available PDC sequences including Arabidopsis thaliana, UniProt: Q9FFT4-1, TAIR: AT5G54960
65 | 65 kDa (Arabidopsis thaliana)
Reactivity
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Application examples
Additional information
Background
Pyruvate decarboxylase (PDC) is a homotetrameric enzyme (E.C.4.1.1.1) that catalyses the decarboxylation of pyruvic acid to acetaldehyde carbon dioxide in the cytoplasm. It is also called 2-oxo-acid carboxylase, and pyruvic decarboxylase. In anaerobic conditions, this enzyme is part of the fermentation process that occurs in yeast, especially the Saccharomyces genus, to produce ethanol by fermentation. Pyruvate decarboxylase starts this process by converting pyruvate into acetaldehyde and carbon dioxide. Pyruvate decarboxylase depends on cofactors thiamine pyrophosphate (TPP) and magnesium. This enzyme should not be mistaken for the unrelated enzyme pyruvate dehydrogenase, an oxidoreductase (EC 1.2.4.1), that catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA.
Product citations
Giuntoli et al. (2014). A trihelix DNA binding protein counterbalances hypoxia-responsive transcriptional activation in Arabidopsis. PLoS Biol. 2014 Sep 16;12(9):e1001950. doi: 10.1371/journal.pbio.1001950. eCollection 2014.
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