Properties of a CDP-diglyceride hydrolase from guinea pig brain.
Enzymatic hydrolysis of the pyrophosphate bond of CDP-diglyceride (CDP-DG), previously shown to occur in bacteria, is demonstrable in mammalian tissues. Activity was enriched in a lysosomal fraction obtained from guinea pig cerebral cortex and was purified 92-fold relative to the homogenate by a combination of XM-300 ultrafiltration and DEAE-cellulose column chromatography. When incubated with CDP-dipalmitin, the purified enzyme produced stoichiometric amounts of CMP and phosphatidate. dCDP-DG served as a substrate, while ADP-DG was an inhibitor, as were 5'-AMP and 5'-dAMP. CDP-DG hydrolysis was not affected by the presence of excess amounts of CDP-choline, CDP-glycerol, sodium pyrophosphate, or cyclic 3',5'-AMP.
D000818:Animals; D001921:Brain / Q000201:enzymology*; D003567:Cytidine Diphosphate Diglycerides / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism; D006168:Guinea Pigs; D066298:In Vitro Techniques; D008297:Male; D011755:Pyrophosphatases / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D013347:Subcellular Fractions / Q000201:enzymology; D013379:Substrate Specificity
D003567:Cytidine Diphosphate Diglycerides; D011755:Pyrophosphatases; C019855:CDPdiacylglycerol pyrophosphatase