Journal article

Dual diaminopimelate biosynthesis pathways in Bacteroides fragilis and Clostridium thermocellum

Andre O Hudson, Ayelet Klartag, Charles Gilvarg, Renwick CJ Dobson, Felipe Garbelini Marques, Thomas Leustek

Biochimica et Biophysica Acta-Proteins and Proteomics | ELSEVIER | Published : 2011


Bacteroides fragilis and Clostridium thermocellum were recently found to synthesize diaminopimelate (DAP) by way of LL-DAP aminotransferase. Both species also contain an ortholog of meso-diaminopimelate dehydrogenase (Ddh), suggesting that they may have redundant pathways for DAP biosynthesis. The B. fragilis Ddh ortholog shows low homology with other examples of Ddh and this species belongs to a phylum, the Bacteriodetes, not previously known to contain this enzyme. By contrast, the C. thermocellum ortholog is well conserved with known examples of Ddh. Using in vitro and in vivo assays both the B. fragilis and C. thermocellum enzymes were found to be authentic examples of Ddh, displaying ki..

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Awarded by USA National Science Foundation

Funding Acknowledgements

This work was funded by USA National Science Foundation grant IPB0449542 to T.L. and C.G.; and a scholarship to P.G.M. from the FIPSE/CAPES program of the Brazilian Ministry of Education (P.G.M.). We are grateful to Dr. Sheila Patrick for contributing genomic DNA and Dr. Charles Jeffrey Smith for helpful discussions on Bacteroides fragilis gene expression data.