Reactome | GDE1 hydrolyzes GroPIns

GDE1 hydrolyzes GroPIns

Stable Identifier

R-HSA-6813740

Type

Reaction [transition]

Species

Homo sapiens

Compartment

plasma membrane, cytosol

ReviewStatus

5/5

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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
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
16472945	Genomic organization, characterization, and molecular 3D model of GDE1, a novel mammalian glycerophosphoinositol phosphodiesterase Bachmann, AS, Duennebier, FF, Mocz, G	Gene	2006
10760272	MIR16, a putative membrane glycerophosphodiester phosphodiesterase, interacts with RGS16 Zheng, B, Chen, D, Farquhar, MG	Proc. Natl. Acad. Sci. U.S.A.	2000