7.1.2.1 2,3-Butanedione - 1001 7.1.2.1 2-(3-pyridinyl)-1,2-benzisoselenazol-3(2H)-one an ebselen analogue 83761 7.1.2.1 2-methylbenzisoselenazol-3(2H)-one - 226751 7.1.2.1 2-n-propylbenzisoselenazol-3(2H)-one - 226754 7.1.2.1 2-phenyl-1,2-benzisoselenazol-3(2H)-one i.e. ebselen, inhibition of enzyme results in inhibition of medium acidification. Fungicidal effect is at least in part due to interference with both the proton-translocating function and the ATPase activity of plasma membrane H+-ATPase 6966 7.1.2.1 2-phenyl-1,2-benzisoselenazol-3(2H)-one i.e. ebselen 6966 7.1.2.1 2-phenyl-1,2-benzisoselenazol-3(2H)-one i.e. ebselen, a synthetic selenium-containing compound with antimicrobial activity. It acts fungicidally against Candida albicans at 0.030 mM, effect of ebselen on the growth of the strain, overview 6966 7.1.2.1 2-phenyl-1,2-benzisoselenazol-3(2H)-one i.e. ebselen, a synthetic selenium-containing compound with antimicrobial activity, effect of ebselen on the growth of the strain, overview; i.e. ebselen, a synthetic selenium-containing compound with antimicrobial activity, effect of ebselen on the growth of the strain, overview. The antifungal action of ebselen is related, at least in part, to its ability to interact with L-cysteine, high affinity of selenium for sulfhydryl groups 6966 7.1.2.1 2-phenyl-1,2-benzisoselenazol-3(2H)-one 1-oxide an ebselen analogue 83762 7.1.2.1 2-phenyl-7-azabenzisoselenazol-3(2H)-one - 226756 7.1.2.1 2-phenylbenzisothiazol-3(2H)-one - 226757 7.1.2.1 adenosine 5'-(beta,gamma-imido)-triphosphate 5 mM, 60% inhibition 51504 7.1.2.1 adenosine 5'-monophosphate decreases the interaction between the phosphorylated Vha2 and the 14-3-3 protein, followed by a reduction of the H+-ATPase activity and citrate exudation under Al stress conditions 2942 7.1.2.1 ADP 5 mM, 60% inhibition, Kd value 0.8 mM 13 7.1.2.1 Al3+ inhibition of H+-ATPase activity, Mg2+ partly prevents 264 7.1.2.1 Al3+ the proton transport activity of the enzyme is inhibited by 50% in the presence of 100 mM Al3+ at pH 6.5 and 10% at pH 7.5 264 7.1.2.1 aluminium the activity of plasma membrane H+-ATPase is affected by aluminium at the transcription, translation, and post-translation levels 25170 7.1.2.1 aluminum fluoride - 163516 7.1.2.1 ATP competitive inhibitor, the enzyme activity decreases in the presence of Mg2+-free ATP. ATP inhibition also occurs at pH 7.5. Upon increasing Mg2+ concentration from 5 mM to 15 mM, the decrease in ATPase activity at high ATP concentration is prevented 4 7.1.2.1 bafilomycin - 32152 7.1.2.1 bafilomycin A1 - 6127 7.1.2.1 benzisoselenazol-3(2H)-one - 227207 7.1.2.1 beryllium fluoride - 13740 7.1.2.1 Ca2+ completely inactive when Mg2+ is substituted by Ca2+, strongly inhibited by Ca2+ in presence of Mg2+ 15 7.1.2.1 Ca2+ extracellular, inhibits the enzym ein osteoclast membranes, Ca2+ behaves as a negative feedback signal for osteoclast function 15 7.1.2.1 Cd2+ complete loss of ATP hydrolysis and proton transport. Exposure does not enhance the lipid peroxidation in plasma membrane, but causes an increase in the saturation of plasma membrane fatty acids and a decrease of the fatty acid chain length 52 7.1.2.1 concanamycin A - 9528 7.1.2.1 Cu2+ - 19 7.1.2.1 Cu2+ complete loss of ATP hydrolysis and proton transport. Exposure does not enhance the lipid peroxidation in plasma membrane, but causes an increase in the saturation of plasma membrane fatty acids and a decrease of the fatty acid chain length 19 7.1.2.1 Cu2+ short-term (10 min) exposure to copper (0.05 mM) completely inhibits the activity of the enzyme 19 7.1.2.1 destruxin B specific and reversible inhibition, complete inhibition at concentrations above 0.02 mM 11075 7.1.2.1 Dicyclohexylcarbodiimide - 2554 7.1.2.1 Dicyclohexylcarbodiimide no protection by MgATP2- 2554 7.1.2.1 diethylstilbestrol - 1679 7.1.2.1 Dio-9 - 20897 7.1.2.1 distilbestrol - 16662 7.1.2.1 Disulfiram - 986 7.1.2.1 ebselen i.e. 2-phenylbenzisoselenazol-3(2H)-one 2514 7.1.2.1 fluconazole - 1579 7.1.2.1 fluoroaluminates Mg2+ is an essential cofactor for inhibition, biphasic inhibitory process at pH 7.5 with a preference for AlF4- species 106070 7.1.2.1 folimycin - 227964 7.1.2.1 fusicoccin - 17657 7.1.2.1 Hemileia vastatrix treatment with soluble fraction of urediospores induces specific inhibition of of the resistant variety's Colombia H+-ATPase and proton pump activities, while the inhibition of the Caturra variety's proton-pump acitivy is only 16.5% 144079 7.1.2.1 iejimalide A a macrolide that is cytostatic or cytotoxic against a wide range of cancer cells at low nanomolar concentrations, inhibits vacuolar H+-ATPase in the context of epithelial tumor cells leading to a lysosome-initiated cell death process, overview 83757 7.1.2.1 iejimalide B a macrolide that is cytostatic or cytotoxic against a wide range of cancer cells at low nanomolar concentrations, inhibits vacuolar H+-ATPase in the context of epithelial tumor cells leading to a lysosome-initiated cell death process, overview 83758 7.1.2.1 K+ K+ is an intrinsic uncoupler of the proton pump. Binding of K+ to the cytoplasmic phosphorylation domain can induce dephosphorylation of the phosphorylated E1P reaction cycle intermediate by a mechanism involving residue E184 in the conserved TGEs motif 39 7.1.2.1 K-252a a potent inhibitor of protein kinase 17792 7.1.2.1 K2SO4 in plants grown with 10 mM K2SO4 plus 100 mM NaCl supply, activity decreases competitively with Na+, after 21 d of salinity, with different effects on Km and Vmax 2560 7.1.2.1 KF - 2410 7.1.2.1 lansoprazole - 4413 7.1.2.1 miconazole - 1206 7.1.2.1 molybdate 86% residual activity at 1 mM 509 7.1.2.1 molybdate 87% residual activity at 1 mM 509 7.1.2.1 additional information proton pump interactor (PPI1) is unable to suppress the auto-inhibitory action of the enzyme C-terminus, but further enhances the activity of the enzyme whose C-terminus has been displaced by low pH or by fusicoccin-induced binding of 14-3-3 proteins 2 7.1.2.1 additional information not inhibitory: SCH28080 2 7.1.2.1 additional information not inhibitory: Ni2+ 2 7.1.2.1 additional information inhibitor screening, overview 2 7.1.2.1 additional information both inhibitors, iejimalides A and B, sequentially neutralize the pH of lysosomes, induce S-phase cell-cycle arrest, and trigger apoptosis in MCF-7 cells, overview 2 7.1.2.1 additional information ebselen is at least 10fold more potent as antifungal compound compared the azoles fluconazole, itraconazole, and ketoconatzole, and as amphotericin B 2 7.1.2.1 additional information not inhibited by nitrate, azide, and molybdate 2 7.1.2.1 additional information not inhibited by azide and nitrate 2 7.1.2.1 additional information phenylglyoxal does not inhibit enzyme activity; phenylglyoxal does not inhibit enzyme activity; phenylglyoxal does not inhibit enzyme activity 2 7.1.2.1 N-(Ethoxycarbonyl)-2-ethoxy-1,2-dihydroquinoline no protection by MgADP-, protection by MgATP2- or Mg-vanadate 20392 7.1.2.1 N-ethylmaleimide 2 mM, 26% inhibition 49 7.1.2.1 N-ethylmaleimide - 49 7.1.2.1 Na2MO4 weak 106819 7.1.2.1 Na3VO4 0.1 mM 4546 7.1.2.1 NaF - 235 7.1.2.1 NEM pseudo-first order kinetics, inhibition is prevented either by MgADP- and MgATP2- 89 7.1.2.1 nitrate - 308 7.1.2.1 Omeprazole - 2976 7.1.2.1 orthovanadate - 1328 7.1.2.1 oxidized glutathione - 1794 7.1.2.1 p-hydroxymercuribenzoate - 98 7.1.2.1 Phenylglyoxal pseudo-first order kinetics, inhibition is prevented either by MgADP- and MgATP2- 301 7.1.2.1 SidK a protein of Legionella pneumophila, an intracellular pathogen, specifically targets host v-ATPase. SidK interacts via an N-terminal portion with VatA, a key component of the proton pump leading to the inhibition of ATP hydrolysis and proton translocation. SidK inhibits vacuole acidification and impairs the ability of the cells to digest non-pathogenic Escherichia coli 83756 7.1.2.1 sodium orthovanadate specific inhibitor 3399 7.1.2.1 sodium orthovanadate - 3399 7.1.2.1 Triton X-100 strong inhibition 61 7.1.2.1 Trypsin 85% inhibition of the enzyme in plasma membrane vesicles in absence of MgATP2-, no inhibition in presence of MgATP2- 393 7.1.2.1 vanadate Na3VO4, non-competitive 233 7.1.2.1 vanadate - 233 7.1.2.1 vanadate inhibition of enzyme, treatment additionally leads to severe suppression of phosphorus uptake by roots in low-phosphorus nutrient solution 233 7.1.2.1 vanadate about 7% residual activity at 0.3 mM 233 7.1.2.1 vanadate 8% residual activity at 0.1 mM 233 7.1.2.1 vanadate significant inhibition at 0.1 mM; significant inhibition at 0.1 mM; significant inhibition at 0.1 mM 233 7.1.2.1 vanadate for enzymes isolated from root, kinetic models of vanadate inhibition indicate simultaneous binding of Mg-ATP and vanadate to the same enzyme state. For shoot enzymes, application of the competitive inhibitor Mg-free ATP attenuates vanadate inhibition, consistent with a model in which either Mg-free ATP or Mg-ATP is bound to the enzyme when vanadate binds 233 7.1.2.1 Zn2+ short-term (10 min) exposure to zinc (0.25 mM) completely inhibits the activity of the enzyme 14