Covalently bound pyruvate in phosphopantothenoylcysteine decarboxylase from horse liver.
Horse liver phosphopantothenoylcysteine decarboxylase (EC 4.1.1.36) incorporates nonexchangeable tritium from borotritide with a decrease of the activity. Substrate prevents both tritium incorporation and the decrease in activity. Acid and base hydrolysis of the tritiated protein releases labeled lactate identified by high-voltage paper electrophoresis, paper chromatography and silicic acid chromatography. These results indicate the presence of pyruvate covalently bound through an ester linkage to phosphopantothenoylcysteine decarboxylase which is then another example of a mammalian enzyme in which pyruvate is involved in a catalytic activity.
D026921:Amino Acid Transport Systems, Neutral; D000818:Animals; D001665:Binding Sites; D002262:Carboxy-Lyases / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism*; D050487:Glycine Plasma Membrane Transport Proteins; D006736:Horses; D008099:Liver / Q000201:enzymology; D009097:Multienzyme Complexes; D010453:Peptide Synthases; D011773:Pyruvates / Q000378:metabolism*; D019289:Pyruvic Acid; D014316:Tritium / Q000378:metabolism
D026921:Amino Acid Transport Systems, Neutral; D002352:Carrier Proteins; D050487:Glycine Plasma Membrane Transport Proteins; D009097:Multienzyme Complexes; D011773:Pyruvates; D014316:Tritium; D019289:Pyruvic Acid; D002262:Carboxy-Lyases; C022373:Phosphopantothenoyl-cysteine decarboxylase; D010453:Peptide Synthases