[H+-ATPase and H+-pyrophosphatase in yeast vacuolar membrane].
Saccharomyces carlsbergenis vacuoles possess an ATPase activity differing from those of the well-known H(+)-ATPase of plasma membranes and mitochondria as well as from those of other phosphohydrolases. Yeast vacuolar ATPase represents an electrogenic H(+)-translocase. H(+)-ATPase was incorporated into a liposomal membrane in a functionally active form. Tonoplast ATPase did not form a phosphorylated intermediate. Purified vacuolar ATPase contained three major polypeptides with M(r) of 72, 62 and 16 kDa. S. carlsbergensis vacuoles also contained a pyrophosphatase (PPase) whose properties differed significantly from those of other vacuolar phosphohydrolases. Vacuolar membrane-bound PPase is a proton pump; its molecular mass is about 120 kDa. The enzyme molecule consists of three subunits, each of M(r) = 41 kDa. Soluble PPase from vacuolar sap has a molecular mass of about 82 kDa and consists of three subunits of M(r) = 28 kDa.
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D007425:Intracellular Membranes / Q000201:enzymology; D008081:Liposomes; D010766:Phosphorylation; D017494:Proton Pumps; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D011755:Pyrophosphatases / Q000378:metabolism*; D012440:Saccharomyces / Q000201:enzymology*; D014617:Vacuoles / Q000201:enzymology*
D008081:Liposomes; D017494:Proton Pumps; D011755:Pyrophosphatases; D006180:Proton-Translocating ATPases
H+-ATPase i H+-pirofosfataza vakuoliarnoĭ membrany drozhzheĭ.