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A lysophospholipase D activity (ENPP2, Q13822, also known as ectonucleotide pyrophosphatase/phosphodiesterase 2, phosphodiesterase I, nucleotide pyrophosphatase 2, autotaxin) has been described, which not only catalyses the production of lysophosphatidic acid (LPA) from lysophosphatidylcholine, but also cleaves ATP (see Goding et al., 2003 [1]). Additionally, an N-acylethanolamine-specific phospholipase D (NAPEPLD, Q6IQ20) has been characterized, which appears to have a role in the generation of endocannabinoids/endovanilloids, including anandamide [8]. This enzyme activity appears to be enhanced by polyamines in the physiological range [4] and fails to transphosphatidylate with alcohols [10].
Three further, less well-characterised isoforms are PLD3 (PLD3, Q8IV08, other names Choline phosphatase 3, HindIII K4L homolog, Hu-K4), PLD4 (PLD4, Q96BZ4, other names Choline phosphatase 4, Phosphatidylcholine-hydrolyzing phospholipase, D4C14orf175 UNQ2488/PRO5775) and PLD5 (PLD5, Q8N7P1). PLD3 has been reported to be involved in myogenesis [9]. PLD4 is described not to have phospholipase D catalytic activity [17], but has been associated with inflammatory disorders [7,15-16]. Sequence analysis suggests that PLD5 is catalytically inactive.