Specific inhibition of phosphatidate cytidylyltransferase from Bacillus subtilis membranes by cytidine monophosphate.
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.
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
D003597:Cytosine Nucleotides; D010743:Phospholipids; D009713:Nucleotidyltransferases; C022348:phosphatidate cytidylyltransferase; D003568:Cytidine Monophosphate