| pubmed-article:7032914 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7032914 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:7032914 | lifeskim:mentions | umls-concept:C0041249 | lld:lifeskim |
| pubmed-article:7032914 | lifeskim:mentions | umls-concept:C0041258 | lld:lifeskim |
| pubmed-article:7032914 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:7032914 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:7032914 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:7032914 | pubmed:dateCreated | 1982-3-22 | lld:pubmed |
| pubmed-article:7032914 | pubmed:abstractText | The kinetics of the binding of L-tryptophan to the alpha 2 holo beta 2 complex of tryptophan synthase from Escherichia coli have been measured by rapid-mixing techniques under conditions where tryptophan release is mainly rate-determining in tryptophan synthesis. The dependence of the three observable rate processes on the concentration of L-tryptophan suggests a mechanism in which a rapid binding step is followed by two isomerizations. The effect of the substrate analogue indolepropanol phosphate on the kinetics of binding and synthesis from L-serine and indole supports a branched mechanism with an unproductive enzyme-ligand complex being the major species. The productive enzyme-ligand complex absorbs light at 473 nm but not at 500 nm. These observations, and binding studies with D-tryptophan, suggest that at least two alterative modes of binding of L-tryptophan exist on the enzyme. The effects of protons, indole and indolepropanol phosphate on the three rate processes explain the dependence of kcat on the three non-competitive ligands. | lld:pubmed |
| pubmed-article:7032914 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7032914 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7032914 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7032914 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7032914 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7032914 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7032914 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7032914 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7032914 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:7032914 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:7032914 | pubmed:author | pubmed-author:KirschnerKK | lld:pubmed |
| pubmed-article:7032914 | pubmed:author | pubmed-author:NessTT | lld:pubmed |
| pubmed-article:7032914 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7032914 | pubmed:volume | 120 | lld:pubmed |
| pubmed-article:7032914 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7032914 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7032914 | pubmed:pagination | 379-87 | lld:pubmed |
| pubmed-article:7032914 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
| pubmed-article:7032914 | pubmed:meshHeading | pubmed-meshheading:7032914-... | lld:pubmed |
| pubmed-article:7032914 | pubmed:meshHeading | pubmed-meshheading:7032914-... | lld:pubmed |
| pubmed-article:7032914 | pubmed:meshHeading | pubmed-meshheading:7032914-... | lld:pubmed |
| pubmed-article:7032914 | pubmed:meshHeading | pubmed-meshheading:7032914-... | lld:pubmed |
| pubmed-article:7032914 | pubmed:meshHeading | pubmed-meshheading:7032914-... | lld:pubmed |
| pubmed-article:7032914 | pubmed:meshHeading | pubmed-meshheading:7032914-... | lld:pubmed |
| pubmed-article:7032914 | pubmed:meshHeading | pubmed-meshheading:7032914-... | lld:pubmed |
| pubmed-article:7032914 | pubmed:meshHeading | pubmed-meshheading:7032914-... | lld:pubmed |
| pubmed-article:7032914 | pubmed:meshHeading | pubmed-meshheading:7032914-... | lld:pubmed |
| pubmed-article:7032914 | pubmed:year | 1981 | lld:pubmed |
| pubmed-article:7032914 | pubmed:articleTitle | The mechanism of tryptophan binding to tryptophan synthase from Escherichia coli. | lld:pubmed |
| pubmed-article:7032914 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7032914 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:7032914 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7032914 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7032914 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7032914 | lld:pubmed |
