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- W2130074511 abstract "ABSTRACT In Escherichia coli , the active transport of phenylalanine is considered to be performed by two different systems, AroP and PheP. However, a low level of accumulation of phenylalanine was observed in an aromatic amino acid transporter-deficient E. coli strain (Δ aroP Δ pheP Δ mtr Δ tna Δ tyrP ). The uptake of phenylalanine by this strain was significantly inhibited in the presence of branched-chain amino acids. Genetic analysis and transport studies revealed that the LIV-I/LS system, which is a branched-chain amino acid transporter consisting of two periplasmic binding proteins, the LIV-binding protein (LIV-I system) and LS-binding protein (LS system), and membrane components, LivHMGF, is involved in phenylalanine accumulation in E. coli cells. The K m values for phenylalanine in the LIV-I and LS systems were determined to be 19 and 30 μM, respectively. Competitive inhibition of phenylalanine uptake by isoleucine, leucine, and valine was observed for the LIV-I system and, surprisingly, also for the LS system, which has been assumed to be leucine specific on the basis of the results of binding studies with the purified LS-binding protein. We found that the LS system is capable of transporting isoleucine and valine with affinity comparable to that for leucine and that the LIV-I system is able to transport tyrosine with affinity lower than that seen with other substrates. The physiological importance of the LIV-I/LS system for phenylalanine accumulation was revealed in the growth of phenylalanine-auxotrophic E. coli strains under various conditions." @default.
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- W2130074511 date "2004-01-15" @default.
- W2130074511 modified "2023-10-10" @default.
- W2130074511 title "Identification of the LIV-I/LS System as the Third Phenylalanine Transporter in <i>Escherichia coli</i> K-12" @default.
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- W2130074511 doi "https://doi.org/10.1128/jb.186.2.343-350.2004" @default.
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