Destruxin B, a specific and readily reversible inhibitor of vacuolar-type H(+)-translocating ATPase.
Destruxin B, a peptide antibiotic, inhibits vacuolar-type ATPase (V-ATPase) specifically and dose-dependently among ATPases examined. Acidification of intracellular organelles is also blocked by destruxin B at comparable concentrations when assessed by accumulation of acridine orange. The inhibitory activity of destruxin B is weaker than that of bafilomycin A1 and folimycin, well known macrolide inhibitors of V-ATPase, when compared at the same molar concentration. Unlike the macrolide antibiotics, however, the inhibitory activity of destruxin B is readily reversible. This novel feature of destruxin B should make it a useful probe in the analysis of V-ATPase function in cell physiology.
Muroi
M
M
Animal and Cellular Systems Laboratory, Physical and Chemical Research Institute (RIKEN), Saitama, Japan.
Shiragami
N
N
Takatsuki
A
A
D000818:Animals; D000900:Anti-Bacterial Agents / Q000494:pharmacology; D002540:Cerebral Cortex / Q000201:enzymology; D047630:Depsipeptides; D004305:Dose-Response Relationship, Drug; D007425:Intracellular Membranes / Q000201:enzymology; D007700:Kinetics; D018942:Macrolides; D008928:Mitochondria / Q000201:enzymology; D009183:Mycotoxins / Q000494:pharmacology*; D010456:Peptides, Cyclic / Q000494:pharmacology*; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors*; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D000254:Sodium-Potassium-Exchanging ATPase / Q000037:antagonists & inhibitors; D013552:Swine; D014617:Vacuoles / Q000201:enzymology*
D000900:Anti-Bacterial Agents; D047630:Depsipeptides; D018942:Macrolides; D009183:Mycotoxins; D010456:Peptides, Cyclic; C040424:destruxin B; C040929:bafilomycin A1; D006180:Proton-Translocating ATPases; D000254:Sodium-Potassium-Exchanging ATPase