Abstract
The hydrolysis rates of different diphosphates, compared with the one observed with natural phosphatidylcholine, are used to identify the molecular basis for phospholipase D (PLD) catalysis. Experimental data strongly support the idea that PLD is a rather generic phosphodiesterase with very wide substrate specificity and a net preference for lipophilic substrates. The presence of choline in the polar head is not required for activity although it improves hydrolysis efficiency. Choline esters are found to be substrates for PLD hydrolysis, but only with long chain fatty acids.
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