pubmed-article:14702302 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:14702302 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
pubmed-article:14702302 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
pubmed-article:14702302 | lifeskim:mentions | umls-concept:C0031453 | lld:lifeskim |
pubmed-article:14702302 | lifeskim:mentions | umls-concept:C0596902 | lld:lifeskim |
pubmed-article:14702302 | lifeskim:mentions | umls-concept:C0814810 | lld:lifeskim |
pubmed-article:14702302 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:14702302 | pubmed:dateCreated | 2004-1-2 | lld:pubmed |
pubmed-article:14702302 | pubmed:abstractText | 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 (DeltaaroP DeltapheP Deltamtr Deltatna DeltatyrP). 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 micro M, 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. | lld:pubmed |
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pubmed-article:14702302 | pubmed:language | eng | lld:pubmed |
pubmed-article:14702302 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14702302 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:14702302 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:14702302 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:14702302 | pubmed:month | Jan | lld:pubmed |
pubmed-article:14702302 | pubmed:issn | 0021-9193 | lld:pubmed |
pubmed-article:14702302 | pubmed:author | pubmed-author:SuzukiHideyuk... | lld:pubmed |
pubmed-article:14702302 | pubmed:author | pubmed-author:KumagaiHidehi... | lld:pubmed |
pubmed-article:14702302 | pubmed:author | pubmed-author:KatayamaTakan... | lld:pubmed |
pubmed-article:14702302 | pubmed:author | pubmed-author:KoyanagiTakas... | lld:pubmed |
pubmed-article:14702302 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:14702302 | pubmed:volume | 186 | lld:pubmed |
pubmed-article:14702302 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:14702302 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:14702302 | pubmed:pagination | 343-50 | lld:pubmed |
pubmed-article:14702302 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
pubmed-article:14702302 | pubmed:meshHeading | pubmed-meshheading:14702302... | lld:pubmed |
pubmed-article:14702302 | pubmed:meshHeading | pubmed-meshheading:14702302... | lld:pubmed |
pubmed-article:14702302 | pubmed:meshHeading | pubmed-meshheading:14702302... | lld:pubmed |
pubmed-article:14702302 | pubmed:meshHeading | pubmed-meshheading:14702302... | lld:pubmed |
pubmed-article:14702302 | pubmed:meshHeading | pubmed-meshheading:14702302... | lld:pubmed |
pubmed-article:14702302 | pubmed:meshHeading | pubmed-meshheading:14702302... | lld:pubmed |
pubmed-article:14702302 | pubmed:meshHeading | pubmed-meshheading:14702302... | lld:pubmed |
pubmed-article:14702302 | pubmed:meshHeading | pubmed-meshheading:14702302... | lld:pubmed |
pubmed-article:14702302 | pubmed:meshHeading | pubmed-meshheading:14702302... | lld:pubmed |
pubmed-article:14702302 | pubmed:meshHeading | pubmed-meshheading:14702302... | lld:pubmed |
pubmed-article:14702302 | pubmed:meshHeading | pubmed-meshheading:14702302... | lld:pubmed |
pubmed-article:14702302 | pubmed:year | 2004 | lld:pubmed |
pubmed-article:14702302 | pubmed:articleTitle | Identification of the LIV-I/LS system as the third phenylalanine transporter in Escherichia coli K-12. | lld:pubmed |
pubmed-article:14702302 | pubmed:affiliation | Division of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Kyoto, Japan. | lld:pubmed |
pubmed-article:14702302 | pubmed:publicationType | Journal Article | lld:pubmed |