Substrate response in acid phosphatase activity of Pseudomonas pseudomallei and Pseudomonas cepacia, with special reference to tyrosine phosphatase.
The substrate response in acid phosphatase activity of Pseudomonas pseudomallei and Pseudomonas cepacia was examined with different phosphate esters including hexose phosphates and phosphoaminoacids in a whole cell assay system. The enzymatic activity against each substrate was evaluated in terms of percent activity to that against para-nitrophenyl phosphate set as 100. A remarkable finding was that the phosphatase reaction was the highest with phosphotyrosine or phosphoserine as substrate showing 180% activity. This tyrosine phosphatase activity was resistant to heating at 60 C for 20 min and inhibited greatly by 0.1% ZnCl2. Pseudomonas cepacia showed the same pattern of substrate response and the same characteristics of tyrosine phosphatase activity.
Kanai
K
K
National Institute of Health, Department of Medical Sciences, Nonthaburi, Thailand.
Kondo
E
E
D000135:Acid Phosphatase / Q000378:metabolism; D016956:Burkholderia cepacia / Q000201:enzymology*; D016957:Burkholderia pseudomallei / Q000201:enzymology*; D002712:Chlorides / Q000494:pharmacology; D006358:Hot Temperature / Q000009:adverse effects; D006801:Humans; D017027:Protein Tyrosine Phosphatases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D013379:Substrate Specificity; D015032:Zinc / Q000494:pharmacology; D017967:Zinc Compounds
D002712:Chlorides; D017967:Zinc Compounds; C016837:zinc chloride; D000135:Acid Phosphatase; D017027:Protein Tyrosine Phosphatases; D015032:Zinc