Effects of inhibitors on mitochondrial adenosine triphosphatase of Crithidia fasciculata: an unusual pattern of specificities.
The mitochondrial adenosine triphosphatase of the kinetoplastid protozoon, Crithidia fasciculata, is inhibited by oligomycin, venturicidin, triethyltin sulphate, N,N'-dicyclohexylcarbodiimide, leucinostatin, Dio-9 and quercetin, but not spegazzinine or by compounds which interact with the beta-subunit of mitochondrial F1-ATPase (efrapeptin, aurovertin, citreoviridin or 4-chloro-7-nitrobenzofurazan). These results suggest that the F1 portion of the crithidial enzyme has an unusual type of beta-subunit. Further evidence for the atypical nature of this enzyme is provided by the observation that F1-inhibitor proteins from Acanthamoeba castellanii or bovine heart mitochondria do not inhibit the C. fasciculata enzyme activity.
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors*; D000818:Animals; D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D003421:Crithidia / Q000201:enzymology*; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology; D008928:Mitochondria / Q000201:enzymology*; D009840:Oligomycins / Q000494:pharmacology; D009930:Organic Chemicals; D010455:Peptides / Q000494:pharmacology; D011506:Proteins / Q000494:pharmacology; D006180:Proton-Translocating ATPases; D011794:Quercetin / Q000494:pharmacology; D014267:Triethyltin Compounds / Q000494:pharmacology; D014475:Uncoupling Agents / Q000494:pharmacology; D014698:Venturicidins / Q000494:pharmacology; D000097795:ATPase Inhibitory Protein
D000251:Adenosine Triphosphatases; D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D004024:Dicyclohexylcarbodiimide; D009840:Oligomycins; D009930:Organic Chemicals; D010455:Peptides; D011506:Proteins; D006180:Proton-Translocating ATPases; D011794:Quercetin; D014267:Triethyltin Compounds; D014475:Uncoupling Agents; D014698:Venturicidins; D000097795:ATPase Inhibitory Protein; C100056:DIO 9; C031209:Triethyltin sulfate; C008268:leucinostatin A