Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P20020 (adenosine triphosphatase)
 3,299 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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

Staphylococus aureus, ATCC 6538P, was fractionated into protoplast membranes, mesosomal vesicles, periplasm, and cytoplasm. These fractions and the culture fluid were then assayed for various degradative enzyme activities. They were not restricted to a single fraction nor dispersed homogeneously, but were distributed predominantly (on the basis of specific activity) as follows: nuclease in the culture fluid; alkaline phosphatase, 5'-nucleotidase, and acid phosphatase in the periplasm; adenosine triphosphatase in the protoplast membrane; and protease (low levels) in mesosomal vesicles. No significant esterase nor cell wall hydrolytic activity was found in any fraction. S. aureus 80/81 was studied for penicillinase activity after induction with benzyl penicillin; this enzyme was localized in the mesosomal vesicles. Electron microscopy did not reveal any ultrastructural changes associated with secretion of the extracellular fraction. Overall, these studies demonstrate that degradative enzymes are located in several surface compartments and that, therefore, the mesosome does not function as a prototype lysosome in S. aureus.
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PMID:Cellular location of degradative enzymes in Staphylococcus aureus. 437 33