Regular ArticleSynthesis and Characterization of Short-Chain Diacylphosphatidic Acids
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Role of tryptophan residues in interfacial binding of phosphatidylinositol-specific phospholipase C
2002, Journal of Biological ChemistryCitation Excerpt :The decrease in fluorescence was the least for W242A and the double mutant. Upon micelle formation of diC6PA (the CMC depends on the ionic strength and pH of the medium and is likely to be 5–7 mm under these buffer conditions (22)), all proteins except W242A and the double mutant showed large increases in fluorescence consistent with micelle binding as well as active site binding of the PA molecule. This could suggest that Trp-242 not only senses micelle binding but contributes to the decrease in fluorescence as lipids bind to the active site.
A 20-kDa domain is required for phosphatidic acid-induced allosteric activation of phospholipase D from Streptomyces chromofuscus
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