TY - JOUR
T1 - Utilization of 2-aminoethylarsonic acid in Pseudomonas aeruginosa
AU - Lacoste, A. M.
AU - Dumora, C.
AU - Ali, B. R.S.
AU - Neuzil, E.
AU - Dixon, H. B.F.
PY - 1992
Y1 - 1992
N2 - This paper describes the metabolism, transport and growth inhibition effects of 2-aminoethylarsonic acid (AEA) and 3-aminopropylarsonic acid (APrA). The former compound supported growth of Pseudomonas aeruginosa, as sole nitrogen source. The two arsonates inhibited the growth of this bacterium when 2-aminoethylphosphonic acid (AEP) but not alanine or NH4Cl, was supplied as the only other nitrogen source. The analogy between AEA and the natural compound AEP led us to examine the in vitro and in vivo interaction of AEA with the enzymes of AEP metabolism. The uptake system for AEP (K(m) 6 μM) was found to be competitively inhibited by AEA and APrA (K; 18 μM for each). AEP-aminotransferase was found to act on AEA with a K(m) of 4 mM (3.85 mM for AEP). Alanine and 2-arsonoacetaldehyde were generated concomitantly, in a stoichiometric reaction. In vivo, AEA was catabolized by the AEP-aminotransferase since it was able to first induce this enzyme, then to be an efficient substrate. The lower growth observed may have been due to the slowness with which the permease and the aminotransferase were induced, and hence to a poor supply of alanine by transamination.
AB - This paper describes the metabolism, transport and growth inhibition effects of 2-aminoethylarsonic acid (AEA) and 3-aminopropylarsonic acid (APrA). The former compound supported growth of Pseudomonas aeruginosa, as sole nitrogen source. The two arsonates inhibited the growth of this bacterium when 2-aminoethylphosphonic acid (AEP) but not alanine or NH4Cl, was supplied as the only other nitrogen source. The analogy between AEA and the natural compound AEP led us to examine the in vitro and in vivo interaction of AEA with the enzymes of AEP metabolism. The uptake system for AEP (K(m) 6 μM) was found to be competitively inhibited by AEA and APrA (K; 18 μM for each). AEP-aminotransferase was found to act on AEA with a K(m) of 4 mM (3.85 mM for AEP). Alanine and 2-arsonoacetaldehyde were generated concomitantly, in a stoichiometric reaction. In vivo, AEA was catabolized by the AEP-aminotransferase since it was able to first induce this enzyme, then to be an efficient substrate. The lower growth observed may have been due to the slowness with which the permease and the aminotransferase were induced, and hence to a poor supply of alanine by transamination.
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U2 - 10.1099/00221287-138-6-1283
DO - 10.1099/00221287-138-6-1283
M3 - Article
C2 - 1527499
AN - SCOPUS:0026763797
SN - 0022-1287
VL - 138
SP - 1283
EP - 1287
JO - Journal of General Microbiology
JF - Journal of General Microbiology
IS - 6
ER -