NTE is a member of a novel protein family represented in organisms from bacteria to man; of its 1327 amino acids, 200 near the C-terminal are highly conserved, and the active site serine (S966) lies within this region [96]. Atkins and Glynn expressed an active site region corresponding to residues 727–1216 in E. coli and referred it as NEST (NTE-esterase domain) [97]. This made it possible to study substrate specificity, which showed preferential hydrolysis of lipids [98]. A more recent study showed that NTE in mammalian cells and its homologue in yeast degrade phosphatidylcholine to glycerophosphocholine, thereby substantiating a primary role in lipid homeostasis [99]. Quistad et al. provided evidence that NTE may be a lysophospholipase (LysoPLA), which hydrolyzes lysolecithin, a major membrane phospholipid which has demyelinating properties [100]; neuropathic compounds were found to inhibit NTE and NTE-LysoPLA to the same extent, both in vitro and in vivo [100] and [101].