| pubmed-article:186263 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:186263 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:186263 | lifeskim:mentions | umls-concept:C0004007 | lld:lifeskim |
| pubmed-article:186263 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:186263 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
| pubmed-article:186263 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:186263 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:186263 | pubmed:dateCreated | 1977-1-28 | lld:pubmed |
| pubmed-article:186263 | pubmed:abstractText | The nature of the feedback inhibition of the bifunctional enzyme, aspartokinase I-homoserine dehydrogenase I of Escherichia coli was studied using 13C nuclear magnetic resonance (NMR). Since aspartokinase is activated by Mn(II), the interaction of the inhibitor L-threonine (specifically enriched to 90% 13C in the carboxyl carbon) with the metal-enzyme complex was studied. Spin-lattice (T1) and spin-spin (T2) relaxation times were determined by the partially relaxed Fourier transform method and line-width measurements respectively at 20 MHz. The pronounced broadening of the DL-threonine carboxyl peak in the presence of the Mn(II)-enzyme complex indicates that an L-threonine binding site is close to the metal binding site of the kinase active site. The non-identity of (T1)*M and (T2)*M indicates that conditions of fast exchange prevail. The (T1)*M/(T2)*M ratio was used to estimate a correlation time of 2.0 ns for the dipolar interaction at 25 degrees C. An estimate for the distance between Mn(II) and the threonine carboxyl carbon of 4.4 A (0.44 nm) was obtained. This 13C NMR study has thus located one of the two classes of threonine regulatory sites which exist per subunit; the threonine site identified here is at the aspartokinase active site, adjacent to the catalytic metal site. | lld:pubmed |
| pubmed-article:186263 | pubmed:language | eng | lld:pubmed |
| pubmed-article:186263 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:186263 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:186263 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:186263 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:186263 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:186263 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:186263 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:186263 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:186263 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:186263 | pubmed:author | pubmed-author:TakahashiMM | lld:pubmed |
| pubmed-article:186263 | pubmed:author | pubmed-author:WrightKK | lld:pubmed |
| pubmed-article:186263 | pubmed:author | pubmed-author:DamleSS | lld:pubmed |
| pubmed-article:186263 | pubmed:author | pubmed-author:TilakAA | lld:pubmed |
| pubmed-article:186263 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:186263 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:186263 | pubmed:volume | 69 | lld:pubmed |
| pubmed-article:186263 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:186263 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:186263 | pubmed:pagination | 249-55 | lld:pubmed |
| pubmed-article:186263 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
| pubmed-article:186263 | pubmed:meshHeading | pubmed-meshheading:186263-T... | lld:pubmed |
| pubmed-article:186263 | pubmed:meshHeading | pubmed-meshheading:186263-M... | lld:pubmed |
| pubmed-article:186263 | pubmed:meshHeading | pubmed-meshheading:186263-T... | lld:pubmed |
| pubmed-article:186263 | pubmed:meshHeading | pubmed-meshheading:186263-M... | lld:pubmed |
| pubmed-article:186263 | pubmed:meshHeading | pubmed-meshheading:186263-K... | lld:pubmed |
| pubmed-article:186263 | pubmed:meshHeading | pubmed-meshheading:186263-E... | lld:pubmed |
| pubmed-article:186263 | pubmed:meshHeading | pubmed-meshheading:186263-P... | lld:pubmed |
| pubmed-article:186263 | pubmed:meshHeading | pubmed-meshheading:186263-F... | lld:pubmed |
| pubmed-article:186263 | pubmed:meshHeading | pubmed-meshheading:186263-P... | lld:pubmed |
| pubmed-article:186263 | pubmed:meshHeading | pubmed-meshheading:186263-F... | lld:pubmed |
| pubmed-article:186263 | pubmed:meshHeading | pubmed-meshheading:186263-P... | lld:pubmed |
| pubmed-article:186263 | pubmed:meshHeading | pubmed-meshheading:186263-M... | lld:pubmed |
| pubmed-article:186263 | pubmed:meshHeading | pubmed-meshheading:186263-B... | lld:pubmed |
| pubmed-article:186263 | pubmed:meshHeading | pubmed-meshheading:186263-A... | lld:pubmed |
| pubmed-article:186263 | pubmed:year | 1976 | lld:pubmed |
| pubmed-article:186263 | pubmed:articleTitle | Nuclear-magnetic-relaxation studies of the interaction of inhibitor with the threonine-sensitive aspartokinase of Escherichia coli. | lld:pubmed |
| pubmed-article:186263 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:186263 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| entrez-gene:945803 | entrezgene:pubmed | pubmed-article:186263 | lld:entrezgene |
