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Rv0989c encodes a novel ( E )‐geranyl diphosphate synthase facilitating decaprenyl diphosphate biosynthesis in Mycobacterium tuberculosis
Author(s) -
Mann Francis M.,
Thomas Jill A.,
Peters Reuben J.
Publication year - 2011
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.2011.01.007
Subject(s) - biosynthesis , farnesyl diphosphate synthase , atp synthase , biochemistry , enzyme , mycobacterium tuberculosis , bacteria , cell wall , biology , microbiology and biotechnology , chemistry , tuberculosis , medicine , genetics , pathology
Mycobacterium tuberculosis (Mtb) has a highly complex cell wall, which is required for both bacterial survival and infection. Cell wall biosynthesis is dependent on decaprenyl diphosphate as a glyco‐carrier, which is hence an essential metabolite in this pathogen. Previous biochemical studies indicated ( E )‐geranyl diphosphate (GPP) is required for the synthesis of decaprenyl diphosphate. Here we demonstrate that Rv0989c encodes the “missing” GPP synthase, representing the first such enzyme to be characterized from bacteria, and which presumably is involved in decaprenyl diphosphate biosynthesis in Mtb. Our investigation also has revealed previously unrecognized substrate plasticity of the farnesyl diphosphate synthases from Mtb , resolving previous discrepancies between biochemical and genetic studies of cell wall biosynthesis.