The hydrolysis rates of different diphosphates, compared with the one obser
ved with natural phosphatidylcholine, are used to identify the molecular ba
sis for phospholipase D (PLD) catalysis. Experimental data strongly support
the idea that PLD is a rather generic phosphodiesterase with very wide sub
strate specificity and a net preference for Lipophilic substrates. The pres
ence of choline in the polar head is not required for activity although it
improves hydrolysis efficiency. Choline esters are found to be substrates f
or PLD hydrolysis, but only with long chain fatty acids. (C) 2001 Elsevier
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