Is the Paracoccus halodenitrificans ATPase a chimeric enzyme?
Membranes from Paracoccus halodenitrificans contain an ATPase that is most active in the absence of NaCl. The most unusual characteristic of the enzyme is its pattern of sensitivity to various inhibitors. Azide and rhodamine 6G, inhibitors of F1F0-ATPases, inhibit ATP hydrolysis as do bafilomycin A1, concanamycin A (folimycin), N-ethylmaleimide, and p-chloromercuriphenylsulfonate which are inhibitors of vacuolar ATPases. This indiscriminate sensitivity suggests that this ATPase may be a hybrid and that caution should be exercised when using inhibition as a diagnostic for distinguishing between F1F0-ATPases and vacuolar ATPases.
Hochstein
L I
LI
Exobiology Branch, Ames Research Center, Moffett Field, CA 94035, USA.
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors* / Q000378:metabolism; D000900:Anti-Bacterial Agents / Q000494:pharmacology; D001386:Azides / Q000494:pharmacology; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D005033:Ethylmaleimide / Q000494:pharmacology; D018942:Macrolides; D008566:Membranes / Q000187:drug effects / Q000201:enzymology; D009566:Nitrates / Q000494:pharmacology; D010230:Paracoccus / Q000201:enzymology*; D011189:Potassium Chloride / Q000494:pharmacology; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors* / Q000378:metabolism; D012235:Rhodamines / Q000494:pharmacology; D012965:Sodium Chloride / Q000494:pharmacology*; D025262:Vacuolar Proton-Translocating ATPases
D000900:Anti-Bacterial Agents; D001386:Azides; D004791:Enzyme Inhibitors; D018942:Macrolides; D009566:Nitrates; D012235:Rhodamines; C026188:rhodamine 6G; D012965:Sodium Chloride; D004024:Dicyclohexylcarbodiimide; D011189:Potassium Chloride; C036978:concanamycin A; C040929:bafilomycin A1; C031618:sodium nitrate; D000251:Adenosine Triphosphatases; D025262:Vacuolar Proton-Translocating ATPases; D006180:Proton-Translocating ATPases; D005033:Ethylmaleimide