title: Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells.
abstract: Various membrane ATPases have been tested for their sensitivity to bafilomycin A1, a macrolide antibiotic. F1F0 ATPases from bacteria and mitochondria are not affected by this antibiotic. In contrast, E1E2 ATPases--e.g., the K+-dependent (Kdp) ATPase from Escherichia coli, the Na+,K+-ATPase from ox brain, and the Ca2+-ATPase from sarcoplasmic reticulum--are moderately sensitive to this inhibitor. Finally, membrane ATPases from Neurospora vacuoles, chromaffin granules, and plant vacuoles are extremely sensitive. From this we conclude that bafilomycin A1 is a valuable tool for distinguishing among the three different types of ATPases and represents the first relatively specific potent inhibitor of vacuolar ATPases.
authors.affiliation: Department of Biology, University of California, Santa Cruz 95064.
authors.forename: E J
authors.initials: EJ
authors.lastname: Bowman
authors.forename: A
authors.initials: A
authors.lastname: Siebers
authors.forename: K
authors.initials: K
authors.lastname: Altendorf
mesh_terms: D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors*; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D004926:Escherichia coli / Q000201:enzymology; D007783:Lactones / Q000494:pharmacology; D018942:Macrolides; D008566:Membranes / Q000201:enzymology; D009491:Neurospora / Q000201:enzymology; D014617:Vacuoles / Q000201:enzymology
chemical_list: D000900:Anti-Bacterial Agents; D007783:Lactones; D018942:Macrolides; C040929:bafilomycin A1; C052501:bafilomycin B1; C052502:bafilomycin C1; C057627:bafilomycin D; D000251:Adenosine Triphosphatases