Journal article
L,L-diaminopimelate aminotransferase from chlamydomonas reinhardtii: A target for algaecide development
RCJ Dobson, I Girón, AO Hudson
Plos One | PUBLIC LIBRARY SCIENCE | Published : 2011
Abstract
In some bacterial species and photosynthetic cohorts, including algae, the enzyme L,L-diaminopimelate aminotransferase (DapL) (E.C. 2.6.1.83) is involved in the anabolism of the essential amino acid L-lysine. DapL catalyzes the conversion of tetrahydrodipicolinate (THDPA) to L,L-diaminopimelate (L,L-DAP), in one step bypassing the DapD, DapC and DapE enzymatic reactions present in the acyl DAP pathways. Here we present an in vivo and in vitro characterization of the DapL ortholog from the alga Chlamydomonas reinhardtii (Cr-DapL). The in vivo analysis illustrated that the enzyme is able to functionally complement the E. coli dap auxotrophs and was essential for plant development in Arabidopsi..
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Awarded by Office of Science of the U.S. Department of Energy
Funding Acknowledgements
R.C.J.D. acknowledges the C.R. Roper Bequest for fellowship support. The work conducted by the U.S. Department of Energy Joint Genome Institute is supported by the Office of Science of the U.S. Department of Energy under Contract No. DE-AC02-05CH11231. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.