Phosphonate Catabolism by Campylobacter spp.

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Title Phosphonate Catabolism by Campylobacter spp.
Author Mendz, George L.; Megraud, Francis; Korolik, Victoria
Journal Name Archives of Microbiology
Year Published 2005
Place of publication Germany
Publisher Springer-Verlag
Abstract The catabolism of phosphonates (Phn) by Campylobacter spp. was investigated employing nuclear magnetic resonance spectroscopy and cell culture techniques. The bacteria were capable of cleaving the Phn bonds of different compounds, including -aminomethylphosphonate, phosphonoacetate and phenylphosphonate (PhePhn). The kinetic parameters of these activities were determined in vivo in intact cells and in situ in whole-cell lysates. Cleavage of Phn-bearing compounds was associated with the cell-wall and cytosolic fractions. Results from substrate competition experiments suggested that at least two enzyme activities appeared to be involved in the cleavage of carbon–phosphate (C–P) bonds. In silico analyses indicated that no genes orthologous to those encoding C–P bond-cleaving enzymes in other bacteria were present in the Campylobacter jejuni genome. In most bacteria studied, Phn catabolism is induced under conditions of phosphate limitation; however, in Campylobacter spp. these activities were expressed in cells grown in media rich in phosphate. In chemically defined media, PhePhn supported bacterial growth and proliferation at concentrations above 100 M in the absence of phosphate. Thus, Phn utilisation may be a survival mechanism of Campylobacter spp. in milieux lacking sufficient phosphate. The expression of these enzyme activities in media abundant in phosphate suggested also that they may have other physiological roles.
Peer Reviewed Yes
Published Yes
Alternative URI http://dx.doi.org/10.1007/s00203-004-0752-7
Volume 183
Page from 113
Page to 120
ISSN 0302-8933
Date Accessioned 2006-02-06
Date Available 2010-08-20T06:25:10Z
Language en_AU
Research Centre Institute for Glycomics
Faculty Institute for Glycomics
Subject PRE2009-Bacteriology
URI http://hdl.handle.net/10072/4182
Publication Type Journal Articles (Refereed Article)
Publication Type Code c1

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