The competitive inhibition of tissue transglutaminase by alpha-difluoromethylornithine.
The transglutaminase-mediated insertion of putrescine into casein was inhibited competitively by alpha-difluoromethylornithine (alpha-DFMO), an enzyme-activated irreversible inhibitor of ornithine decarboxylase. Preincubation of the amine acceptor (casein) or the enzyme itself with the inhibitor did not affect enzyme activity. Alpha-DFMO is a poorer substrate for transglutaminase (Km = 2.10 mM) than putrescine (Km = 0.17 mM). The inhibitory effect was also found with fibronectin as amine acceptor.
D000217:Acyltransferases / Q000037:antagonists & inhibitors*; D000818:Animals; D002364:Caseins / Q000378:metabolism; D000518:Eflornithine; D006168:Guinea Pigs; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D009952:Ornithine / Q000031:analogs & derivatives* / Q000378:metabolism / Q000494:pharmacology; D011700:Putrescine / Q000378:metabolism; D011503:Transglutaminases
D002364:Caseins; D009952:Ornithine; D000217:Acyltransferases; D011503:Transglutaminases; D011700:Putrescine; D000518:Eflornithine