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

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Physiological correlation between glycyrrhizin, glycyrrhizin-binding lipoxygenase and casein kinase II.

By means of glycyrrhizin (GL)-affinity column chromatography, a GL-binding lipoxygenase (gbLOX) was selectively purified from the partially purified soybean LOX-1 fraction. Polypeptide analysis of the purified gbLOX by SDS-PAGE detected two distinct polypeptides ( p96 and p94), which were identical to LOX-3 as determined by their partial N-terminal amino acid sequences. Moreover, it was found that (i) phosphorylation of gpLOX by casein kinase II ( CK-II) is significantly stimulated by 3 microM GL, but inhibited by 30 microM GL or 10 microM oGA; and (ii) gbLOX activity is enhanced when the enzyme is phosphorylated by CK-II in the presence of 3 microM GL. These results suggest that (i) CK-II is a kinase responsible for the activation of gbLOX through its specific phosphorylation; and (ii) GL is one of the regulatory substances for specific phosphorylation of gbLOX (LOX-3) by CK-II in plant cells.[1]

References

  1. Physiological correlation between glycyrrhizin, glycyrrhizin-binding lipoxygenase and casein kinase II. Shimoyama, Y., Ohtaka, H., Nagata, N., Munakata, H., Hayashi, N., Ohtsuki, K. FEBS Lett. (1996) [Pubmed]
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