FEMS Microbiology Letters · 2004 · 11 citations · 14 references
Life SciencesMolecular BiologyPlant BiologyEnzymologyMicrobial GeneticsPlant Molecular BiologyAmino Acid Biosynthesis InhibitionBacterial Gene RegulationCell Wall BiosynthesisGene Regulation In MicrobesPathway RegulationPlant EnzymesBacterial Cell Wall BiosynthesisEnzyme BiosynthesisEscherichia ColiEscherichia Coli Expression SystemsLysine BiosynthesisLysine MetabolismMicrobial Amino Acid BiosynthesisPlant Amino Acid Biosynthesis
Dihydropicolinate synthase (DHDPS; E.C. 4.2.1.52) catalyses the first committed step of lysine biosynthesis in plants and bacteria. Plant DHDPS enzymes, which are responsible solely for lysine biosynthesis, are strongly inhibited by lysine (I0.5= 10 μM), whereas the bacterial enzymes which are less responsive or insensitive to lysine inhibition have the additional function of meso-diaminopimelate biosynthesis which is required for cell wall formation. Previous studies have suggested that expression of the Escherichia coli dapA gene, encoding DHDPS, is unregulated. We show here that this is not the case and that expression of LacZ from the dapA promoter (PdapA) increases in response to diaminopimelic acid limitation in E. coli K-12.
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