GDE1 hydrolyzes GroPIns

Stable Identifier
R-HSA-6813740
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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GDE1 (glycerophosphodiester phosphodiesterase 1) catalyzes the hydrolysis of GroPIns (1-(sn-glycero-3-O-phosphonato)-1D-myo-inositol; glycerophosphoinositol) to G3P (glycerol-3-phosphate) and Ins (inositol). Experimental studies of the homologous rat enzyme have shown it to be associated with cellular membranes, to have a strong preference for glycerophosphoinositol over glycerophosphocholine as a substrate, and to be stimulated by G protein agonists, suggesting a possible role for GDE1 in signaling by G protein-coupled receptors (Zheng et al. 2000, 2003). Modeling studies with the human protein have been interpreted to suggest localization specifically to the plasma membrane (Bachmann et al. 2006).

Literature References
PubMed ID Title Journal Year
16472945 Genomic organization, characterization, and molecular 3D model of GDE1, a novel mammalian glycerophosphoinositol phosphodiesterase

Bachmann, AS, Duennebier, FF, Mocz, G

Gene 2006
12576545 GDE1/MIR16 is a glycerophosphoinositol phosphodiesterase regulated by stimulation of G protein-coupled receptors

Zheng, B, Berrie, CP, Corda, D, Farquhar, MG

Proc. Natl. Acad. Sci. U.S.A. 2003
10760272 MIR16, a putative membrane glycerophosphodiester phosphodiesterase, interacts with RGS16

Zheng, B, Chen, D, Farquhar, MG

Proc. Natl. Acad. Sci. U.S.A. 2000
Participants
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Catalyst Activity
Catalyst Activity
Title
glycerophosphoinositol glycerophosphodiesterase activity of GDE1 [plasma membrane]
Physical Entity
Activity
Orthologous Events
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