Exogenous orthophosphate regulation of the phosphohydrolase activities of Pseudomonas aeruginosa and Pseudomonas maltophilia
Treshchanina, N.A.; Nesmeianova, M.A.; Zhdan-Pushkina, S.M.
Mikrobiologiia 50(6): 996-1001
1981
ISSN/ISBN: 0026-3656 PMID: 6276704 Document Number: 174710
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.