Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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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)

The ars operon of the resistance plasmid R773 was found to produce moderate levels of resistance to tellurite. A MIC of 64 micrograms of TeO3(2-) per ml was found for Escherichia coli cells harboring plasmids which contained all three of the structural genes (arsA, arsB, and arsC) of the anion-translocating ATPase. MICs specified by plasmids carrying only one or two structural elements or the cloning vector alone were 2 to 4 micrograms/ml. The rate of TeO3(2-) uptake was found to be on the order of 55% less for cultures containing the resistance plasmids.
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PMID:The arsenical ATPase efflux pump mediates tellurite resistance. 153 16

The possibility that chlorhexidine is a specific inhibitor of membrane bound bacterial adenosine triphosphatase (ATPase) was addressed. The in-vitro susceptibilities of several Providencia stuartii cell envelope enzymes, including ATPase, to chlorhexidine were compared. The following concentrations of chlorhexidine were required to cause 50% inhibition of enzyme activity in preparations from chlorhexidine-sensitive strains (MIC 50 mg chlorhexidine/l): ATPase (160 mg/l), succinic dehydrogenase (greater than 300 mg/l), penicillin binding protein 7 (300 mg/l) and beta-lactamase (45 mg/l). Fifty per cent inhibition of the ATPase from a chlorhexidine-resistant strain (MIC 1600 mg/l) was achieved at an in-vitro concentration of 225 mg chlorhexidine/l. Our observations do not support the suggestion that bacterial membrane-bound ATPases are specific targets for chlorhexidine.
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PMID:Inhibition of Providencia stuartii cell envelope enzymes by chlorhexidine. 295 30

[3H]gentamicin uptake and killing were studied in three strains of gentamicin-resistant Staphylococcus aureus possessing plasmid-encoded, gentamicin-modifying enzymes and in three isogenic, enzyme-free, gentamicin-susceptible derivatives. At low (less than or equal to 2.0 micrograms/ml) concentrations of gentamicin, uptake by resistant organisms was impaired compared with that of susceptible strains, and no killing was noted. In contrast, at higher (2.5 to 10.0 micrograms/ml) concentrations (which were below the MIC for the resistant strains), rapid gentamicin uptake similar to that seen in susceptible isolates was observed. Although growth inhibition at these concentrations was apparent, there was no loss of viability in resistant strains. Consistently, the membrane H+-ATPase inhibitor N,N'-dicyclohexyl carbodiimide caused resistant strains to take up low concentrations (1.0 microgram/ml) of gentamicin at rates comparable to those seen in susceptible organisms without causing an associated loss of viability. These studies show differences between gentamicin uptake in S. aureus and streptomycin uptake in Escherichia coli (Dickie et al., Antimicrob. Agents Chemother. 14:569-580, 1978) regarding the kinetics of uptake in resistant strains with plasmid-encoded aminoglycoside-modifying enzymes. Specifically, they suggest that for 2-deoxystreptamine compounds such as gentamicin, ribosomal binding followed by accelerated uptake and subsequent interference with cell growth may occur without invariably being associated with lethal effect.
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PMID:Gentamicin uptake in Staphylococcus aureus possessing plasmid-encoded, aminoglycoside-modifying enzymes. 651 46

The mechanism of fungitoxic action of an antifungal antibiotic benanomicin A was studied with intact cells and protoplasts of Saccharomyces cerevisiae as well as with its enzymic preparations. The results obtained are summarized as follows: (1) benanomicin A at relatively high concentrations (almost equal to MIC) was fungicidal and disrupted the cell permeability barrier, inducing leakage of intracellular K+ and ATP in growing cells, while the antibiotic had none of these effects in non-growing cells; (2) no biosynthesis of any of several major cellular constituents in yeast cells was inhibited markedly or selectively enough to explain its fungitoxic activity; (3) whereas benanomicin A induced lysis of metabolically active yeast protoplasts incubated in the presence of glucose, inactive yeast protoplasts incubated without glucose were refractory to the lytic action of the antibiotic; (4) osmotically shocked yeast cells became feasible to the cidal action of benanomicin A; (5) benanomicin A substantially inhibited uptake of 6-deoxy-glucose by yeast cells; (6) liposomes composed of phospholipids and cholesterol were not susceptible to benanomicin A; and (7) benanomicin A inhibited in vitro activity of H(+)-ATPase from yeast cell membranes to a greater extent than that for H(+)-ATPase from yeast mitochondria or H(+)-ATPase from yeast vacuolar membranes. Based on these and our previous data that benanomicin A preferentially binds to mannan or mannoproteins constituting the cell wall and cell membrane of yeasts, such binding of the antibiotic is suggested to deteriorate the normal structure and function of those cell membranes of yeasts which are in a growing or metabolically active state, ultimately leading to cell death.
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PMID:Mode of antifungal action of benanomicin A in Saccharomyces cerevisiae. 951 Sep 12

Effects of a newly synthesized antiulcer agent, YJA20379-4, on gastric proton pump (H+/K+-ATPase) activity, Helicobacter pylori (H. pylori) growth, gastric acid secretion, and gastro-duodenal lesions, were examined in comparison with those of omeprazole. YJA20379-4 markedly inhibited the H+/K+-ATPase activity in a concentration-dependent manner and the inhibitory effect was increased under a weak acidic condition; the IC50 values were 32 and 81 microM at pH 6.4 and 7.4, respectively. The inhibition was completely antagonized by 0.5 mM dithiothreitol (DTT). In addition, YJA20379-4 showed a significant anti-H. pylori activity determined by the agar dilution method. The value of minimum inhibitory concentration (MIC, 3.9-11.7 microg/ml) was at least 3 times more potent than that of omeprazole. In pylorus ligated rats, YJA20379-4 inhibited basal gastric acid secretion when administered by the intraduodenal route (ED50: 23.6 mg/kg). In experimental ulcer models, YJA20379-4 administered by the oral route dose-dependently prevented the development of gastro-duodenal lesions in rats. Moreover, repeated administration of YJA20379-4 promoted the healing of gastric ulcers induced by acetic acid. On the basis of the data obtained, it is suggested that YJA20379-4 has a wide spectrum of antiulcer activities, and its mode of antiulcer actions is dependent on the inhibition of H+/K+-ATPase activity and H. pylori growth and the enhancement of a mucosal defense. Thus, YJA20379-4 might prove to be a beneficial therapy for gastritis and peptic ulcer diseases.
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PMID:Effects of YJA20379-4 on gastric secretion, Helicobacter pylori growth and various gastric and duodenal lesions in rats. 963 98

CAN-296 is a complex carbohydrate (approximately 4300 Da) isolated from the cell wall of Mucor rouxii. It exhibits excellent in vitro fungicidal activity against a wide spectrum of pathogenic yeasts, including isolates resistant to azoles and polyenes. The rapid irreversible action of CAN-296 on intact fungal cells and protoplasts suggested a membrane-located target for its action. The proton translocating ATPase (H+-ATPase) of fungi is an essential enzyme required for the regulation of intracellular pH and nutrient transport. Inhibition of H+-ATPase leads to intracellular acidification and cell death. We therefore investigated the effect of CAN-296 on H+-ATPase-mediated proton pumping by intact cells of Candida and Saccharomyces species by measuring the glucose-induced acidification of external medium. CAN-296 inhibited proton pumping of Candida albicans, Candida glabrata, Candida krusei, Candida guilliermondii and Saccharomyces cerevisiae at low concentrations (0.078-1.25 mg/l). Other commonly used antifungal agents such as amphotericin B, itraconazole and fluconazole had no effect on H+-ATPase-mediated proton pumping. A clinical isolate of C. glabrata with reduced in vitro susceptibility (MIC = 10 mg/l) to CAN-296 also showed resistance to CAN-296 inhibition of proton pumping. Purified membrane fractions rich in H+-ATPase activity were not inhibited by CAN-296 suggesting that the effect on the H+-ATPase-mediated proton pumping in intact yeast cells is an indirect effect, perhaps mediated by local or global disruption of the plasma membrane. These results suggest that the inhibition of fungal H+-ATPase is at least partly responsible for the antifungal activity of CAN-296.
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PMID:Proton translocating ATPase mediated fungicidal activity of a novel complex carbohydrate: CAN-296. 1075 43

We investigated the in vitro susceptibility of clinical isolates of Cryptococcus neoformans to the novel conjugated styryl ketone NC1175 by broth microdilution. The MIC(90) and the MFC of NC1175 for C. neoformans were 1 and 2 mg/L, respectively. NC1175 at low concentrations (1-4 mg/L) completely inhibited the glucose-induced acidification of the external medium caused by the extrusion of intracellular protons mediated by the plasma membrane located H(+)-ATPase. These data suggest that NC1175 is a fungicidal agent for C. neoformans and its possible cellular target(s) include the H(+)-ATPase.
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PMID:Inhibition of H(+)-ATPase-mediated proton pumping in Cryptococcus neoformans by a novel conjugated styryl ketone. 1126 29

The inhibitory effect of isoflavones isolated from the flowers and rhizomes of Pueraria thunbergiana (Leguminosae) on the growth of Helicobacter pylori (HP) was investigated. Isoflavone glycosides did not inhibit the growth of HP. However, their aglycones, irisolidone, tectorigenin and genistein, inhibited HP growth. Among them, irisolidone had the most potent inhibitory activity against HP and its MIC was 12.5-25 micrograms/ml. Genistein only weakly inhibited the urease of HP and H+/K(+)-ATPase of rat stomach: its IC50 were 0.43 and 0.89 mg/ml, respectively.
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PMID:In vitro anti-Helicobacter pylori activity of irisolidone isolated from the flowers and rhizomes of Pueraria thunbergiana. 1130 66

Bicozamycin (BCM) which inhibits protein synthesis by inhibiting Rho-dependent transcription termination factor ATPase activity is used for treatment of animal infections. BCM had moderate activity of MIC 16-32 micrograms/ml against enterohemorrhagic Verotoxin (VT)-producing Escherichia coli (EHEC) O157:H7 and inhibited production of VT1 and VT2. The activity of BCM against EHEC was slightly higher in anaerobic conditions, and was more evident in vivo. BCM decreased CFUs of EHEC in caecum more effectively than fosfomycin, cefixime and norfloxacin in a mouse infection model. Moreover, BCM did not increase the amount of either VT1 or VT2 in caecum in mice. In contrast, norfloxacin increased mortality of mice infected with EHEC by inducing VT production. The results suggest that BCM is useful for the treatment of EHEC infection and eradication of EHEC. Dairy live stock, especially young animals, have been implicated as a principal reservoir of EHEC. Eradication of EHEC from live stock will become an important problem in the near future. The narrow spectrum antibiotic BCM is expected to be a safe and effective antibiotic to eradicate EHEC from live stock.
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PMID:[Activity of bicozamycin against Escherichia coli O157:H7 producing Vero toxin]. 1143 31

This study investigated the effect that some polyacetylenes and protopanaxatriol, which were isolated from heated ginseng (family Araliaceae), have on inhibiting Helicobacter pylori (HP) growth. Among the compounds tested, panaxytriol was quite effective in inhibiting HP growth with an MIC of 50 microg/ml. Ginsenoside Rh1 and protopanaxatriol weakly inhibited H+/K+-ATPase from a rat stomach.
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PMID:In vitro anti-Helicobacter pylori activity of panaxytriol isolated from ginseng. 1153 60


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