The tonoplast proton-translocating ATPase of higher plants as a third class of proton-pumps.
Taken together, all the data reported recently in the literature suggest that tonoplast ATPase belongs to a new class of proton pumps. To date, the most studied system is the proton-pumping ATPase from the tonoplast of Hevea latex. Its main characteristics are presented. It resembles the mitochondrial ATPase in its specificity, its substrate affinity, and its sensitivity to different inhibitors. However, for some aspects, it resembles the plasma membrane system in its response to other inhibitors tested (quercetin for example). It differs from both ATPases in its sensitivity to nitrate as well as by its molecular structure, i.e. a complex exhibiting a least 4 or 5 polypeptides. These results favor the existence of a third class of proton pumps, intermediate between the F1F0-class and the E1E2-class.
D000255:Adenosine Triphosphate / Q000031:analogs & derivatives / Q000494:pharmacology; D001693:Biological Transport, Active; D002462:Cell Membrane / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D007476:Ionophores / Q000494:pharmacology; D008928:Mitochondria / Q000201:enzymology; D010944:Plants / Q000201:enzymology*; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors / Q000145:classification / Q000378:metabolism*; D011794:Quercetin / Q000494:pharmacology; D013379:Substrate Specificity; D014639:Vanadium / Q000494:pharmacology
D007476:Ionophores; D014639:Vanadium; D000255:Adenosine Triphosphate; D011794:Quercetin; D006180:Proton-Translocating ATPases