Non-competitive inhibition of ornithine decarboxylase by a phosphopeptide and phosphoamino acids.
In Tetrahymena pyriformis the cytosolic ornithine decarboxylase (L-ornithine carboxy-lyase, EC 4.1.1.17) activity is considerably inhibited by the presence of polyamines in the growth medium, while the nuclear ornithine decarboxylase is only slightly affected. Experimental evidence suggests that the presence of putrescine and/or spermidine elicits the appearance of non-competitive inhibitors of ornithine decarboxylase. One of the inhibitors has a molecular weight of 25,000 and properties of antizyme. In addition, two other low molecular weight inhibitors are extracted, one which is a phosphoserine oligopeptide, and the other which is phosphotyrosine. All inhibit non-competitively the homologous and heterologous (Escherichia coli and rat liver) ornithine decarboxylases. Similarly, non-competitive inhibition was obtained when the commercially available phosphoamino acids were tested against the already mentioned ornithine decarboxylases.
D000596:Amino Acids / Q000494:pharmacology*; D000818:Animals; D002467:Cell Nucleus / Q000201:enzymology; D003600:Cytosol / Q000201:enzymology; D007700:Kinetics; D065108:Ornithine Decarboxylase Inhibitors; D010748:Phosphopeptides / Q000302:isolation & purification / Q000502:physiology*; D011073:Polyamines / Q000494:pharmacology*; D013769:Tetrahymena pyriformis / Q000201:enzymology*
D000596:Amino Acids; D065108:Ornithine Decarboxylase Inhibitors; D010748:Phosphopeptides; D011073:Polyamines