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

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Dnacin A1 and dnacin B1 are antitumor antibiotics that inhibit cdc25B phosphatase activity.

The p80cdc25 protein is a protein phosphatase directly involved in p34cdc2 protein kinase activation by dephosphorylation. The cdc25B gene is one of three human cdc25 homologs which can complement the temperature-sensitive cdc25 mutation of Schizosaccharomyces pombe, and is expressed a high levels in human cell lines, particularly in some cancer cells. A fusion protein of glutathione-S-transferase (GST) and the catalytic domain of cdc25B protein was constructed and found to retain phosphatase activity in the manner of a p80cdc25 phosphatase by using a chromogenic substrate, p-nitrophenylphosphate. Two benzoquinoid antitumor compounds, dnacin A1 and dnacin B1, inhibited phosphatase activity in a non-competitive manner.[1]

References

  1. Dnacin A1 and dnacin B1 are antitumor antibiotics that inhibit cdc25B phosphatase activity. Horiguchi, T., Nishi, K., Hakoda, S., Tanida, S., Nagata, A., Okayama, H. Biochem. Pharmacol. (1994) [Pubmed]
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