| pubmed-article:21719707 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21719707 | lifeskim:mentions | umls-concept:C1016143 | lld:lifeskim |
| pubmed-article:21719707 | lifeskim:mentions | umls-concept:C0023828 | lld:lifeskim |
| pubmed-article:21719707 | lifeskim:mentions | umls-concept:C0001898 | lld:lifeskim |
| pubmed-article:21719707 | lifeskim:mentions | umls-concept:C0052088 | lld:lifeskim |
| pubmed-article:21719707 | lifeskim:mentions | umls-concept:C0038592 | lld:lifeskim |
| pubmed-article:21719707 | lifeskim:mentions | umls-concept:C0085845 | lld:lifeskim |
| pubmed-article:21719707 | lifeskim:mentions | umls-concept:C2257889 | lld:lifeskim |
| pubmed-article:21719707 | pubmed:issue | 33 | lld:pubmed |
| pubmed-article:21719707 | pubmed:dateCreated | 2011-8-15 | lld:pubmed |
| pubmed-article:21719707 | pubmed:abstractText | The aspartate:alanine antiporter (AspT) of the lactic acid bacterium Tetragenococcus halophilus is a member of the aspartate:alanine exchanger (AAEx) transporter family. T. halophilus AspT catalyzes the electrogenic exchange of L-aspartate(1-) with L-alanine(0). Although physiological functions of AspT were well studied, L-aspartate(1-):L-alanine(0) antiport mechanisms are still unsolved. Here we report that the binding sites of L-aspartate and L-alanine are independently present in AspT by means of the kinetic studies. We purified His(6)-tagged T. halophilus AspT and characterized its kinetic properties when reconstituted in liposomes (K(m) = 0.35 ± 0.03 mm for L-aspartate, K(m) = 0.098 ± 0 mm for D-aspartate, K(m) = 26 ± 2 mm for L-alanine, K(m) = 3.3 ± 0.2 mm for D-alanine). Competitive inhibition by various amino acids of L-aspartate or L-alanine in self-exchange reactions revealed that L-cysteine selectively inhibited L-aspartate self-exchange but only weakly inhibited L-alanine self-exchange. Additionally, L-serine selectively inhibited L-alanine self-exchange but barely inhibited L-aspartate self-exchange. The aspartate analogs L-cysteine sulfinic acid, L-cysteic acid, and D-cysteic acid competitively and strongly inhibited L-aspartate self-exchange compared with L-alanine self-exchange. Taken together, these kinetic data suggest that the putative binding sites of L-aspartate and L-alanine are independently located in the substrate translocation pathway of AspT. | lld:pubmed |
| pubmed-article:21719707 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21719707 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21719707 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21719707 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21719707 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21719707 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21719707 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21719707 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21719707 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21719707 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:21719707 | pubmed:issn | 1083-351X | lld:pubmed |
| pubmed-article:21719707 | pubmed:author | pubmed-author:EnomotoMasaru... | lld:pubmed |
| pubmed-article:21719707 | pubmed:author | pubmed-author:KuwaharaShige... | lld:pubmed |
| pubmed-article:21719707 | pubmed:author | pubmed-author:AbeKeietsuK | lld:pubmed |
| pubmed-article:21719707 | pubmed:author | pubmed-author:NanataniKeiK | lld:pubmed |
| pubmed-article:21719707 | pubmed:author | pubmed-author:SasaharaAyako... | lld:pubmed |
| pubmed-article:21719707 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21719707 | pubmed:day | 19 | lld:pubmed |
| pubmed-article:21719707 | pubmed:volume | 286 | lld:pubmed |
| pubmed-article:21719707 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21719707 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21719707 | pubmed:pagination | 29044-52 | lld:pubmed |
| pubmed-article:21719707 | pubmed:dateRevised | 2011-10-19 | lld:pubmed |
| pubmed-article:21719707 | pubmed:meshHeading | pubmed-meshheading:21719707... | lld:pubmed |
| pubmed-article:21719707 | pubmed:meshHeading | pubmed-meshheading:21719707... | lld:pubmed |
| pubmed-article:21719707 | pubmed:meshHeading | pubmed-meshheading:21719707... | lld:pubmed |
| pubmed-article:21719707 | pubmed:meshHeading | pubmed-meshheading:21719707... | lld:pubmed |
| pubmed-article:21719707 | pubmed:meshHeading | pubmed-meshheading:21719707... | lld:pubmed |
| pubmed-article:21719707 | pubmed:meshHeading | pubmed-meshheading:21719707... | lld:pubmed |
| pubmed-article:21719707 | pubmed:meshHeading | pubmed-meshheading:21719707... | lld:pubmed |
| pubmed-article:21719707 | pubmed:meshHeading | pubmed-meshheading:21719707... | lld:pubmed |
| pubmed-article:21719707 | pubmed:meshHeading | pubmed-meshheading:21719707... | lld:pubmed |
| pubmed-article:21719707 | pubmed:meshHeading | pubmed-meshheading:21719707... | lld:pubmed |
| pubmed-article:21719707 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21719707 | pubmed:articleTitle | Substrate specificity of the aspartate:alanine antiporter (AspT) of Tetragenococcus halophilus in reconstituted liposomes. | lld:pubmed |
| pubmed-article:21719707 | pubmed:affiliation | Department of Microbial Biotechnology, Laboratory of Applied Microbiology, Graduate School of Agricultural Science, Tohoku University, Sendai 981-8555, Japan. | lld:pubmed |
| pubmed-article:21719707 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21719707 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
