Pyruvate kinase: a carnitine-regulated site of ATP production in Trypanosoma brucei brucei.
Pyruvate kinase activity in Trypanosoma brucei brucei is stimulated in the presence of L-carnitine and is inhibited by acetyl CoA, ATP or the ATP-Mg2+ complex. Increased pyruvate kinase activity is associated with stimulation of ATP synthesis in the presence of L-carnitine. There is evidence that carnitine stimulates pyruvate kinase activity indirectly by removing the inhibitory modulator acetyl CoA as a result of the carnitine acetyl transferase (CAT) also present in the trypanosomes.
D000105:Acetyl Coenzyme A / Q000494:pharmacology; D000255:Adenosine Triphosphate / Q000096:biosynthesis; D000818:Animals; D002331:Carnitine / Q000494:pharmacology; D002332:Carnitine O-Acetyltransferase / Q000032:analysis; D006019:Glycolysis; D008274:Magnesium / Q000494:pharmacology; D011770:Pyruvate Kinase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D013268:Stimulation, Chemical; D014346:Trypanosoma brucei brucei / Q000201:enzymology*
D000105:Acetyl Coenzyme A; D000255:Adenosine Triphosphate; D002332:Carnitine O-Acetyltransferase; D011770:Pyruvate Kinase; D008274:Magnesium; D002331:Carnitine