TY - JOUR
T1 - Genetic and biochemical characterization of a pathway for the degradation of 2-aminoethylphosphonate in Sinorhizobium meliloti 1021
AU - Borisova, Svetlana A.
AU - Christman, Harry D.
AU - Mourey Metcalf, M. E.
AU - Zulkepli, Nurul A.
AU - Zhang, Jun Kai
AU - Van Der Donk, Wilfred A.
AU - Metcalf, William W.
PY - 2011/6/24
Y1 - 2011/6/24
N2 - A variety of microorganisms have the ability to use phosphonic acids as sole sources of phosphorus. Here, a novel pathway for degradation of 2-aminoethylphosphonate in the bacterium Sinorhizobium meliloti 1021 is proposed based on the analysis of the genome sequence. Gene deletion experiments confirmed the involvement of the locus containingphnW, phnA, and phnY genes in the conversion of 2-aminoethylphosphonate to inorganic phosphate. Biochemical studies of the recombinant PhnY and PhnA proteins verified their roles as phosphonoacetaldehyde dehydrogenase and phosphonoacetate hydrolase, respectively. This pathway is likely not limited to S. meliloti as suggested by the presence of homologous gene clusters in other bacterial genomes.
AB - A variety of microorganisms have the ability to use phosphonic acids as sole sources of phosphorus. Here, a novel pathway for degradation of 2-aminoethylphosphonate in the bacterium Sinorhizobium meliloti 1021 is proposed based on the analysis of the genome sequence. Gene deletion experiments confirmed the involvement of the locus containingphnW, phnA, and phnY genes in the conversion of 2-aminoethylphosphonate to inorganic phosphate. Biochemical studies of the recombinant PhnY and PhnA proteins verified their roles as phosphonoacetaldehyde dehydrogenase and phosphonoacetate hydrolase, respectively. This pathway is likely not limited to S. meliloti as suggested by the presence of homologous gene clusters in other bacterial genomes.
UR - https://www.scopus.com/pages/publications/79959360686
UR - https://www.scopus.com/inward/citedby.url?scp=79959360686&partnerID=8YFLogxK
U2 - 10.1074/jbc.M111.237735
DO - 10.1074/jbc.M111.237735
M3 - Article
C2 - 21543322
AN - SCOPUS:79959360686
SN - 0021-9258
VL - 286
SP - 22283
EP - 22290
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 25
ER -