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)

A gentamicin-resistant mutant of Pseudomonas aeruginosa PAO503 was selected after ethyl methane sulfonate mutagenesis. The strain, P. aeruginosa PAO2401 had increased resistance to all aminoglycosides tested but exhibited no change for other antibiotics. The mutation designated aglA (aminoglycoside resistance) was 50% cotransducible with the 8-min ilvB,C marker on the P. aeruginosa chromosome. It showed a marked reduction in cytochrome c(552) and nitrate reductase (Nar) and a change in terminal oxidase activity. Cytochrome c(552) is a component of the P. aeruginosa Nar. No changes in succinate and reduced nicotinamide adenine dinucleotide dehydrogenases, ubiquinone content, Mg(2+)/Ca(2+) membrane adenosine triphosphatase, and energy coupling of electron transport to adenosine 5'-triphosphate synthesis were detected. Transport of gentamicin and dihydrostreptomycin was impaired in PAO2401, but transport of proline, arginine, glutamine, glucose or the polyamine spermidine was not reduced. Ribosomes of PAO2401, and PAO503 bound dihydrostreptomycin equally well, and cell extracts did not inactivate gentamicin or dihydrostreptomycin. Strain PAO2401 is resistant to gentamicin and dihydrostreptomycin because of impaired transport of these compounds. The transport studies indicate a selective coupling of dihydrostreptomycin and gentamicin transport with terminal electron transport. This conclusion was supported by results from another mutant (PAO417-T2) with increased Nar activity, enhanced dihydrostreptomycin and gentamicin transport and a reduction in resistance to these drugs. These results are discussed in relation to a refined model for aminoglycoside transport and briefly relative to plasmid-mediated aminoglycoside resistance.
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PMID:Aminoglycoside-resistant mutation of Pseudomonas aeruginosa defective in cytochrome c552 and nitrate reductase. 624 53

Low-temperature-induced biochemical changes in bud and root band zone of the sugar cane set suppress sprouting, which is responsible for drastic yield decline in ratoon crops. This study was undertaken to modulate these low-temperature-induced biochemical changes using potassium, zinc, and Ethrel to enhance the sprouting of buds at 5 and 10 degrees C. Potassium, zinc, and Ethrel led to 80, 50, and 40% improvement in bud sprouting at 5 degrees C, respectively. An increase in reducing sugars and a decrease in sucrose contents were recorded with treatment of potassium, zinc, and Ethrel. Acid invertase, adenosine triphosphatase, indoleacetic acid oxidase, and nitrate reductase in vivo activities were also enhanced. However, treatments led to a significant decline in indoleacetic acid, total phenols, and superoxide dismutase activity, which rendered the in situ toxicity buildup in sets at low temperatures.
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PMID:Modulation of low-temperature-induced biochemical changes in bud and root band zones of sugar cane sets by potassium, zinc, and Ethrel for improving sprouting. 1903 60