Kinetic mechanism of formininotransferase from porcine liver.
Formiminotransferase (EC 2.1.2.5) and cyclodeaminase (EC 4.3.1.4) constitute an enzyme complex that catalyses two sequential metabolic reactions. The activity of native formiminotransferase can be measured without interference from cyclodeaminase, and its kinetic mechanism has been investigated. Although initial velocity plots yield families of parallel lines suggesting that the transferase utilizes a ping-pong mechanism, product inhibition and alternate substrate studies with tetrahydropteroic acid clearly show the mechanism to be sequential. Of the possible mechanisms compatible with these observations, several could be ruled out through the effects of various dead-end inhibitors. The data indicate that the transferase mechanism is rapid equilibrium random with formation of a dead-end complex enzyme-tetrahydrofolate-glutamate.
D000642:Ammonia-Lyases / Q000378:metabolism; D000818:Animals; D001667:Binding, Competitive; D005492:Folic Acid / Q000494:pharmacology; D005565:Formiminoglutamic Acid / Q000378:metabolism; D005971:Glutamates / Q000378:metabolism; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D011485:Protein Binding; D013552:Swine; D013763:Tetrahydrofolates / Q000378:metabolism; D014166:Transferases / Q000378:metabolism*
D005971:Glutamates; D013763:Tetrahydrofolates; D005565:Formiminoglutamic Acid; D005492:Folic Acid; D014166:Transferases; D000642:Ammonia-Lyases