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Query: EC:3.6.1.3 (ATPase)
 65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Our current work on a vacuolar membrane proton ATPase in the yeast Saccharomyces cerevisiae has revealed that it is a third type of H+-translocating ATPase in the organism. A three-subunit ATPase, which has been purified to near homogeneity from vacuolar membrane vesicles, shares with the native, membrane-bound enzyme common enzymological properties of substrate specificities and inhibitor sensitivities and are clearly distinct from two established types of proton ATPase, the mitochondrial F0F1-type ATP synthase and the plasma membrane E1E2-type H+-ATPase. The vacuolar membrane H+-ATPase is composed of three major subunits, subunit a (Mr = 67 kDa), b (57 kDa), and c (20 kDa). Subunit a is the catalytic site and subunit c functions as a channel for proton translocation in the enzyme complex. The function of subunit b has not yet been identified. The functional molecular masses of the H+-ATPase under two kinetic conditions have been determined to be 0.9-1.1 x 10(5) daltons for single-cycle hydrolysis of ATP and 4.1-5.3 x 10(5) daltons for multicycle hydrolysis of ATP, respectively. N,N'-Dicyclohexyl-carbodiimide2 does not inhibit the former reaction but strongly inhibits the latter reaction. The kinetics of single-cycle hydrolysis of ATP indicates the formation of an enzyme-ATP complex and subsequent hydrolysis of the bound ATP to ADP and Pi at a 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole-sensitive catalytic site. Cloning of structural genes for the three subunits of the H+-ATPase (VMA1, VMA2, and VMA3) and their nucleotide sequence determination have been accomplished, which provide greater advantages for molecular biological studies on the structure-function relationship and biogenesis of the enzyme complex. Bioenergetic aspects of the vacuole as a main, acidic compartment ensuring ionic homeostasis in the cytosol have been described.
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PMID:Structure and function of the yeast vacuolar membrane proton ATPase. 253 38

Carrot (Daucus carota L.) cells grown in suspension culture oxidized exogeneous NADH. The NADH oxidation was able to stimulate K+ (86Rb+) transport into cells, but it did not affect sucrose transport. N,N'-Dicyclohexyl-carbodiimide, diethylstilbestrol, and oligomycin, which only partially inhibited NADH oxidation, almost completely collapsed the K+ (86Rb+) transport. Vanadate, which is less effective as an ion transport inhibitor, was less effective in inhibiting the NADH-driven transport of K+ (86Rb+). p-Fluormethoxycarbonylcyanide phenylhydrazone inhibits the K+ transport over 90% including that induced by NADH. The results are interpreted as evidence that a plasma membrane redox system in root cells is closely associated with the ATPase which can drive K+ transport. Because of the inhibitor effects, it appears that membrane components common to the redox system and ATPase function in the transport of K+.
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PMID:A link between transport and plasma membrane redox system(s) in carrot cells. 624 53

Properties of membrane-bound and soluble bicarbonate-dependent ATPase from rat erythrocytes were studied. In presence of Mg2+ and Mn2+ bicarbonate activated ATPase in membranes, Zn2+, Ba2+, Ni2+, Ca2+ and Co2+ were ineffective. Ca2+ did not stimulate also the soluble HCO3-- - ATPase. Dicyclohexyl carbodiimide inhibited the membrane-bound ATPase and did not affect the soluble enzyme.
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PMID:[Properties of anion-sensitive erythrocyte ATPase]. 644 13