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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Histidine modifying agents abolish pyruvate dehydrogenase kinase activity.

Pyruvate dehydrogenase kinase ( PDK) specifically phosphorylates the E1alpha subunit of the pyruvate dehydrogenase complex (PDC). Sequence analysis of cloned PDKs led to the proposal that they are mechanistically related to prokaryotic 2-component His-kinases. The reaction mechanism of protein His-kinases involves autophosphorylation of a specific His residue followed by phosphotransfer to an Asp residue. Treatment of recombinant Arabidopsis thaliana PDK with the His-directed reagents diethyl pyrocarbonate (DEPC) and dichloro-(2,2':6', 2"-terpyridine)-platinum(II) dihydrate led to a marked inhibition of autophosphorylation. In addition, DEPC treatment abolished the ability of PDK to trans-phosphorylate and inactivate PDC. These results validate the prediction that PDKs require His residues for activity.[1]

References

  1. Histidine modifying agents abolish pyruvate dehydrogenase kinase activity. Mooney, B.P., David, N.R., Thelen, J.J., Miernyk, J.A., Randall, D.D. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
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