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Insight Into Binding of Calyculin A to Protein Phosphatase 1: Isolation of Hemicalyculin a and Chemical Transformation of Calyculin A

Insight Into Binding of Calyculin A to Protein Phosphatase 1: Isolation of Hemicalyculin a and Chemical Transformation of Calyculin A

Toshiyuki Wakimoto, Shigeki Matsunaga, Akira Takai, Nobuhiro Fusetani

Chem Biol. 2002 Mar;9(3):309-19.

PMID: 11927256

Abstract:

Calyculin A isolated from the marine sponge Discodermia calyx is a potent inhibitor of protein phosphatases 1 and 2A. We attempted to elucidate its mode of binding to the enzymes by examining the activity of natural and chemically transformed derivatives. Ten natural derivatives including a new compound, hemicalyculin A, were provided. The structure of hemicalyculin A, which comprises the southern hemisphere of calyculin A, was firmly established by chemical methods. Six compounds were prepared by selective modifications of functional groups in calyculin A. The enzyme inhibitory activity of these compounds indicated that 17-phosphate, 13-hydroxyl, and the hydrophobic tetraene moieties were all necessary for binding to the enzymes. The derivatives lacking the peptide portion were less cytotoxic even when they possessed full enzyme inhibitory activity.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP101932712	Calyculin A from Discodermia calyx		101932-71-2	Price

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