on October 8, 2018
Pyruvate (PYR) dehydrogenase complex (PDC) is an enzymatic system that plays a crucial role in cellular metabolism as it controls the entry of carbon into the Krebs cycle. Recent experimental investigations highlighted its important role in cancer metabolism and indicated it as a potential target for the development of new anticancer therapies.
In the study entitled ‘How phosphorylation influences E1 subunit pyruvate dehydrogenase: A computational study’, published in Scientific Reports, a team of scientists led by Andrea Cavalli clarified by computational techniques how this enzyme is regulated by phosphorylation of specific serine residues.
The results of this work improve the knowledge of the PDC functional mechanism and suggest new strategies of pharmacological intervention in both cancer and rare metabolic diseases.
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| Structure of the E1 subunit of the pyruvate dehydrogenase complex (PDC). The atoms of the phosphorylated serine residues are depicted as balls |
Article
How phosphorylation influences E1 subunit pyruvate dehydrogenase: A computational study
J. Sgrignani, J. Chen, A. Alimonti, A. Cavalli
in Sci Rep (2018) vol. 8 pp14683
