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

Previous studies have shown that mutations in the unc gene of Escherichia coli K12 cause defects in energy transduction as well as a membrane-bound (Mg2+, Ca2+)-adenosine triphosphatase. We studied the effect of this mutation on the "downhill" efflux of methyl-beta-D-galactopyranoside, a suboli K12 did not show significant differences in substrate influx of efflux, a differential effect of an uncoupler, 2,4-dinitrophenol was demonstrated. In contrast to the unc+, dinitrophenol failed to inhibit significantly the rate coefficient of efflux in the unc- strain. Analysis of spontaneous unc+ revertants of the unc- mutant provided additional evidence that a functional unc gene is necessary for dinitrophenol inhibition of efflux. Other uncouplers tested in the unc+ strain showed different effects on efflux. While arsenate, azide and carbonyl cyanide p-trifluoromethoxyphenulhydrazone caused little or no effect, 2,4-dibromophenol and pentachlorophenol increased efflux by a considerable factor.
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PMID:Effect of uncoupler on "downhill" substrate efflux of Escherichia coli is dependent on (Mg2+, Ca2+). Adenosine triphosphatase. 13 4