We found a match
Your institution may have rights to this item. Sign in to continue.
- Title
Catabolism and Detoxification of 1-Aminoalkylphosphonic Acids: N-Acetylation by the phnO Gene Product.
- Authors
Hove-Jensen, Bjarne; McSorley, Fern R.; Zechel, David L.
- Abstract
In Escherichia coli uptake and catabolism of organophosphonates are governed by the phnCDEFGHIJKLMNOP operon. The phnO cistron is shown to encode aminoalkylphosphonate N-acetyltransferase, which utilizes acetylcoenzyme A as acetyl donor and aminomethylphosphonate, (S)- and (R)-1-aminoethylphosphonate, 2-aminoethyl- and 3-aminopropylpho- sphonate as acetyl acceptors. Aminomethylphosphonate, (S)-1-aminoethylphosphonate, 2-aminoethyl- and 3-aminopro- pylphosphonate are used as phosphate source by E. coli phn+ strains. 2-Aminoethyl- or 3-aminopropylphosphonate but not aminomethylphosphonate or (S)-1-aminoethylphosphonate is used as phosphate source by phnO strains. Neither phn+ nor phnO strains can use (R)-1-aminoethylphosphonate as phosphate source. Utilization of aminomethylphosphonate or (S)-1- aminoethylphosphonate requires the expression of phnO. In the absence of phnO-expression (S)-1-aminoethylphosphonate is bacteriocidal and rescue of phnO strains requires the simultaneous addition of D-alanine and phosphate. An intermediate of the carbon-phosphorus lyase pathway, 5'-phospho-α-D-ribosyl 1'-(2-N-acetamidoethylphosphonate), a substrate for carbon-phosphorus lyase, was found to accumulate in cultures of a phnP mutant strain. The data show that the physiological role of N-acetylation by phnO-specified aminoalkylphosphonate N-acetyltransferase is to detoxify (S)-1- aminoethylphosphonate, an analog of D-alanine, and to prepare (S)-1-aminoethylphosphonate and aminomethylpho- sphonate for utilization of the phosphorus-containing moiety.
- Subjects
ESCHERICHIA coli; METABOLISM; PHOSPHONATES; ACETYLTRANSFERASES; ACETYLCOENZYME A; PHOSPHATES
- Publication
PLoS ONE, 2012, Vol 7, Issue 10, p1
- ISSN
1932-6203
- Publication type
Article
- DOI
10.1371/journal.pone.0046416