[Exogenous orthophosphate regulation of the phosphohydrolase activities of Pseudomonas aeruginosa and Pseudomonas maltophilia].
The activity of several phosphohydrolases, viz. alkaline phosphatase (EC 3.1.3.1), acid phosphatase (EC 3.1.3.2), ATPase (EC 3.6.1.3), tripolyphosphatase (EC 3.6.1.2) and polyphosphatase (EC 3.6.1.11), was studied in Pseudomonas aeruginosa VKM B-889 and Pseudomonas maltophilia VKM B-591. In the absence of orthophosphate in the medium when alkaline phosphatase was derepressed, its activity in P. aeruginosa rose in parallel with that of acid phosphatase, tripolyphosphatase and polyphosphatase. The maximal activity of alkaline phosphatase was detected in the cultural broth while that of the remaining enzymes was found in the soluble fraction of the cells. In P. maltophilia, the activity of phosphohydrolases was not regulated with orthophosphate; even when the cells were grown in its presence, the activity was much higher than that of acid phosphatase, ATPase and tripolyphosphatase of the derepressed cells of P. aeruginosa. In P. maltophilia, the maximal activity of the enzymes, just as that of alkaline phosphatase, was detected in the fraction of cellular membranes.
D003470:Culture Media / Q000378:metabolism; D010710:Phosphates / Q000494:pharmacology*; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D011549:Pseudomonas / Q000187:drug effects* / Q000201:enzymology; D011550:Pseudomonas aeruginosa / Q000187:drug effects* / Q000201:enzymology
D003470:Culture Media; D010710:Phosphates; D010744:Phosphoric Monoester Hydrolases
Reguliatsiia ékzogennym ortofosfatom fosforgidrolaznykh aktivnosteĭ u Pseudomonas aeruginosa i Pseudomonas maltophilia.