TY - JOUR
T1 - Phosphate starvation-independent 2-aminoethylphosphonic acid biodegradation in a newly isolated strain of Pseudomonas putida, NG2
AU - Ternan, Nigel
AU - Quinn, JP
PY - 1998/8
Y1 - 1998/8
N2 - A strain of Pseudomonas putida that utilized the biogenic organophosphonate 2-aminoethylphosphonic acid as sole carbon and energy, nitrogen and phosphorus source contained 2-aminoethylphosphonic acid: pyruvate aminotransferase and phosphonoacetaldehyde hydrolase (phosphonatase) activities which were inducible by the presence of 2-aminoethylphosphonic acid in the culture medium, regardless of the phosphate status of the cells. Neither of these activities were induced in either phosphate-free or phosphate-replete medium in the absence of 2-aminoethylphosphonic acid. Alkaline phosphatase activity was induced in phosphate limited medium, however, indicating a phosphate-starvation inducible response. In Enterobacter aerogenes IFO 12010, 2-aminoethylphosphonate : pyruvate aminotransferase and phosphonatase activities were induced only when cells were both phosphate limited and supplied with 2-aminoethylphosphonic acid as sole phosphorus source for growth. Neither enzyme activity was induced in phosphate-replete medium, or in medium where both 2-aminoethylphosphonic acid and inorganic phosphate were supplied as sources of phosphorus. The results point to the presence of a substrate inducible 2-aminoethylphosphonic acid biodegradation pathway in the isolated strain of Pseudomonas putida. Uniquely, therefore, the pathway is not under pho regulon control in this strain.
AB - A strain of Pseudomonas putida that utilized the biogenic organophosphonate 2-aminoethylphosphonic acid as sole carbon and energy, nitrogen and phosphorus source contained 2-aminoethylphosphonic acid: pyruvate aminotransferase and phosphonoacetaldehyde hydrolase (phosphonatase) activities which were inducible by the presence of 2-aminoethylphosphonic acid in the culture medium, regardless of the phosphate status of the cells. Neither of these activities were induced in either phosphate-free or phosphate-replete medium in the absence of 2-aminoethylphosphonic acid. Alkaline phosphatase activity was induced in phosphate limited medium, however, indicating a phosphate-starvation inducible response. In Enterobacter aerogenes IFO 12010, 2-aminoethylphosphonate : pyruvate aminotransferase and phosphonatase activities were induced only when cells were both phosphate limited and supplied with 2-aminoethylphosphonic acid as sole phosphorus source for growth. Neither enzyme activity was induced in phosphate-replete medium, or in medium where both 2-aminoethylphosphonic acid and inorganic phosphate were supplied as sources of phosphorus. The results point to the presence of a substrate inducible 2-aminoethylphosphonic acid biodegradation pathway in the isolated strain of Pseudomonas putida. Uniquely, therefore, the pathway is not under pho regulon control in this strain.
M3 - Article
VL - 21
SP - 346
EP - 352
JO - Systematic and Applied Microbiology
JF - Systematic and Applied Microbiology
SN - 0723-2020
IS - 3
ER -