Enpp6 Reference Search Result - Rat Genome Database

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RGD ID	Title	Citation	Abstract	PubMed	Pub Date
11354152	Expression, purification, crystallization and preliminary X-ray crystallographic analysis of Enpp6.	Morita J, etal., Acta Crystallogr F Struct Biol Commun. 2014 Jun;70(Pt 6):794-9. doi: 10.1107/S2053230X14008929. Epub 2014 May 24.	Enpp (ectonucleotide phosphodiesterase/pyrophosphatase) 6 is a membrane-bound glycoprotein that hydrolyzes choline-containing compounds such as lysophosphatidylcholine and glycerophosphorylcholine, and presumably participates in choline metabolism. The catalytic domain of mouse Enpp6 ... (more) ght:700;'>Enpp6 was expressed in HEK293T cells, purified using the TARGET tag/P20.1-Sepharose system and crystallized. An X-ray diffraction data set was collected to 1.8 A resolution. The crystal belonged to space group P1, with unit-cell parameters a=63.7, b=68.8, c=69.7 A, alpha=60.6, beta=87.0, gamma=68.1 degrees . Assuming the presence of two protein molecules per asymmetric unit, the solvent content was estimated to be 49.5%.	24915096	2014-07-01
11354340	Structure and biological function of ENPP6, a choline-specific glycerophosphodiester-phosphodiesterase.	Morita J, etal., Sci Rep. 2016 Feb 18;6:20995. doi: 10.1038/srep20995.	Choline is an essential nutrient for all living cells and is produced extracellularly by sequential degradation of phosphatidylcholine (PC). However, little is known about how choline is produced extracellularly. Here, we report that ENPP6, a choline-specific ph ... (more) osphodiesterase, hydrolyzes glycerophosphocholine (GPC), a degradation product of PC, as a physiological substrate and participates in choline metabolism. ENPP6 is highly expressed in liver sinusoidal endothelial cells and developing oligodendrocytes, which actively incorporate choline and synthesize PC. ENPP6-deficient mice exhibited fatty liver and hypomyelination, well known choline-deficient phenotypes. The choline moiety of GPC was incorporated into PC in an ENPP6-dependent manner both in vivo and in vitro. The crystal structure of ENPP6 in complex with phosphocholine revealed that the choline moiety of the phosphocholine is recognized by a choline-binding pocket formed by conserved aromatic and acidic residues. The present study provides the molecular basis for ENPP6-mediated choline metabolism at atomic, cellular and tissue levels.	26888014	1000-07-01