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A mutant pyruvate dehydrogenase E1 subunit allows survival of Escherichia coli strains defective in 1‐deoxy‐ d ‐xylulose 5‐phosphate synthase
Author(s) -
Sauret-Güeto Susanna,
Urós Eva María,
Ibáñez Ester,
Boronat Albert,
Rodríguez-Concepción Manuel
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.12.092
Subject(s) - escherichia coli , mutant , atp synthase , pyruvate dehydrogenase complex , biochemistry , protein subunit , enzyme , chemistry , dehydrogenase , gene , biology , microbiology and biotechnology
The 2‐ C ‐methyl‐ d ‐erythritol 4‐phosphate pathway has been proposed as a promising target to develop new antimicrobial agents. However, spontaneous mutations in Escherichia coli were observed to rescue the otherwise lethal loss of the first two enzymes of the pathway, 1‐deoxy‐ d ‐xylulose 5‐phosphate (DXP) synthase (DXS) and DXP reductoisomerase (DXR), with a relatively high frequency. A mutation in the gene encoding the E1 subunit of the pyruvate dehydrogenase complex was shown to be sufficient to rescue the lack of DXS but not DXR in vivo, suggesting that the mutant enzyme likely allows the synthesis of DXP or an alternative substrate for DXR.