PDC2 | Pyruvate decarboxylase 2
AS10 691 | Clonality: Polyclonal | Host: Rabbit | Reactivity: A. thaliana, O. sativa, Z. mobilis
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65 | 65 kDa (Arabidopsis thaliana)
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Pyruvate decarboxylase (PDC) is a homotetrameric enzyme (E.C.22.214.171.124) 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 126.96.36.199), that catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA.
Gil-Monreal et al. (2019). ERF-VII transcription factors induce ethanol fermentation in response to amino acid biosynthesis-inhibiting herbicides. J Exp Bot. 2019 Aug 6. pii: erz355. doi: 10.1093/jxb/erz355.
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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