[Effect of 5-phosphoribosyl-1-pyrophosphate on the L-glutamate dehydrogenase activity of the bovine liver].
Bovine liver glutamate dehydrogenase (GDH) is a very complex enzyme in its molecular structure and activity regulation. The present paper deals with the effect of PRPP on GDH activity. This phosphate sugar, playing a key role in purine metabolism, behaves as an effector in the L-glutamate oxidation, showing both an activating effect (at low L-glu concentration) and an inhibiting one (as far as 40%), increasing with L-glu and coenzyme (3-acetyl-pyridine adenine dinucleotide) concentration. The inhibition is quite evident at low PRPP concentration, thus suggesting a physiologic role in cellular regulation of GDH activity.
D000818:Animals; D002417:Cattle; D004305:Dose-Response Relationship, Drug; D005969:Glutamate Dehydrogenase / Q000378:metabolism*; D008099:Liver / Q000187:drug effects / Q000201:enzymology*; D009243:NAD / Q000378:metabolism; D010428:Pentosephosphates / Q000494:pharmacology*; D010754:Phosphoribosyl Pyrophosphate / Q000494:pharmacology*
D010428:Pentosephosphates; D009243:NAD; D010754:Phosphoribosyl Pyrophosphate; D005969:Glutamate Dehydrogenase
Effetto del 5-fosforibosil-1-pirofosfato sull'attivita' della L-glutammato deidrogenasi di fegato bovino.