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Glycerophosphodiester phosphodiesterase 1 (GDE1) is an approximately 43 kDa integral membrane glycoprotein characterized by a conserved GDE domain serving as its catalytic site. Localized mainly to internal cell membranes, GDE1 hydrolyzes glycerophosphodiesters such as glycerophosphoinositol and glycerophosphoserine, producing inositol and glycerol 3-phosphate. Its activity is regulated via G protein-coupled receptor (GPCR) signaling, interacting with regulator of G protein signaling (RGS) proteins, and is essential for membrane phospholipid metabolism, intracellular trafficking, and potentially neural signaling by recycling serine from glycerophosphoserine pools in the nervous system. Knockout models show dramatic alteration of related metabolites in the brain, suggesting critical roles in neurochemical homeostasis, but no direct disease associations, biomarkers for patient selection, or interacting drugs have been validated.
Enzyme inhibition or modulation (hypothetical for drugs: would inhibit or enhance GDE1's phosphodiesterase activity)
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