A new protein phosphatase inhibitor, 19-epi-okadaic acid, was isolated from the marine dinoflagellate Prorocentrum belizeanum. Its structure and conformation in solution has been determined, and important differences were found when compared with the lead compound okadaic acid. The new metabolite showed nanomolar activities, and its selectivity for PP2A versus PP1 surpasses that shown by okadaic acid 10-fold, making it one of the most selective inhibitors of this class.
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Cruz et al. (2007) studied this question.
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