title: Specific inhibition of phosphatidate cytidylyltransferase from Bacillus subtilis membranes by cytidine monophosphate.
abstract: In Bacillus subtilis, the phosphatidate cytidylyltransferase was localized exclusively in the membrane fraction prepared by sucrose density gradient fractionation. A single enzyme could synthesize the two liponucleotides: CDPdiacylglycerol and dCDPdiacylglycerol. Kinetic experiments and isotopic exchange reactions suggested a ping-pong mechanism. Among the nucleosides monophosphate, CMP specifically reduced the synthesis of both liponucleotides. This inhibition was non-competitive and might be involved in regulation of phospholipid synthesis.
mesh_terms: D001412:Bacillus subtilis / Q000201:enzymology*; D055598:Chemical Phenomena; D002621:Chemistry; D003568:Cytidine Monophosphate / Q000494:pharmacology*; D003597:Cytosine Nucleotides / Q000494:pharmacology*; D007700:Kinetics; D009713:Nucleotidyltransferases / Q000037:antagonists & inhibitors*; D010743:Phospholipids / Q000096:biosynthesis; D013379:Substrate Specificity
chemical_list: D003597:Cytosine Nucleotides; D010743:Phospholipids; D009713:Nucleotidyltransferases; C022348:phosphatidate cytidylyltransferase; D003568:Cytidine Monophosphate