GDE1 (glycerophosphodiester phosphodiesterase 1) is a membrane-associated enzyme that primarily hydrolyzes glycerophosphodiesters to produce glycerol phosphate and alcohols 1. The enzyme preferentially hydrolyzes glycerophosphoinositol and demonstrates specificity for this substrate over glycerophosphocholine 1. Structurally, GDE1 contains a TIM barrel core similar to bacterial glycerophosphodiester phosphodiesterases, with critical catalytic residues Glu97, Asp99, and His112 2. GDE1 plays a significant role in N-acylethanolamine (NAE) biosynthesis through NAPE-PLD-independent pathways, contributing to the production of bioactive lipid mediators including anandamide 3. The enzyme's expression is dysregulated in several pathological conditions: decreased expression occurs in paclitaxel-resistant ovarian cancers, contributing to altered choline metabolism 4, while increased expression is observed in preeclamptic placentas 5. GDE1 also participates in endocannabinoidome signaling, as demonstrated by its downregulation following treatment with compounds that increase endocannabinoid levels 6. Additionally, GDE1 has been identified as a component of Treg-related gene signatures in colorectal cancer prognosis models 7.