GDE1 hydrolyzes GroPIns

Stable Identifier
Reaction [transition]
Homo sapiens
Locations in the PathwayBrowser
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

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
Catalyst Activity

glycerophosphoinositol glycerophosphodiesterase activity of GDE1 [plasma membrane]

Orthologous Events
Cite Us!