Choline derivatives increase two different acid phosphatases in Rhizobium meliloti and Pseudomonas aeruginosa (original) (raw)

1990, Archives of Microbiology

In Pseudomonas aeruginosa and Rhizobium meliloti several choline derivatives, utilized as the sole c a r b o n and nitrogen source, increase acid phosphatase activity. The enzyme activity of both bacteria could be released into the surrounding medium by E D T Alysozyme treatment. The R. meliloti acid phosphatase activity o f crude periplasmic extracts measured with p-nitrophenylphosphate was not inhibited by the presence o f 5 m M choline, betaine, t r i m e t h y l a m m o n i u m or phosphorylcholine. The activity could not be detected using phosphorylethanolamine or phosphorylcholine as substrates. A m o n g several phosphoesters tested only pyridoxal-5'-phosphate was hydrolyzed at a considerable rate. In 7.5% polyacrylamide slab gel electrophoresis (non-denaturing conditions) o f crude extracts obtained from bacteria grown in the presence o f serine, glutamate, aspartate or dimethylglycine a phosphatase activity with identical mobility could be detected when alphanaphthylphosphate or pyridoxal-5'-phosphate were used as substrates. In conclusion, although the coline metabolites are capable o f increasing acid phosphatase activities in R. meliloti and in P. aeruginosa, there are two different enzymes involved, apparently in different metabolisms.

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