| pubmed-article:776615 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:776615 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:776615 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:776615 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:776615 | lifeskim:mentions | umls-concept:C0041258 | lld:lifeskim |
| pubmed-article:776615 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:776615 | lifeskim:mentions | umls-concept:C0021236 | lld:lifeskim |
| pubmed-article:776615 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:776615 | pubmed:dateCreated | 1976-8-23 | lld:pubmed |
| pubmed-article:776615 | pubmed:abstractText | The binding of indole and indolepropanol phosphate, an analogue of the substrate indoleglycerol phosphate, to the individual alpha and beta2-subunits and to the alpha2beta2-complex of tryptophan synthase was studied by equilibrium dialysis. The use of [14C]indole and indolepropanol [32P]phosphate permitted simultaneous binding studies to be carried out. Competition between indole and indolepropanol phosphate in binding to a particular site was taken as evidence for that site being part of the active site of the alpha-subunit. The binding of indole to the active site of the alpha-subunit is weak (Kd = 18mM). A second distinct site binds indole more strongly (Kd = 1.5 mM) and interacts with the active site indirectly. It is therefore designated an effector site. Furthermore, the binding of indole and/or indolepropanol phosphate appears to stabilize different conformations of the alpha-subunit. The beta2-subunit binds indole only weakly (Kd = 12 mM) to many (n = 10) sites per polypeptide chain. The alpha2beta2-complex retains one or two sites per alphabeta-equivalent of relatively high affinity (Kd = 1.2 mM). The active sites of the component alpha and beta-subunits probably belong to the second class of many (n = 40) sites of low (Kd = 30 mM) affinity for indole. These findings support conclusions from the literature that both bi-substrate reactions involving indole catalyzed by tryptophan synthase and its subunits must follow strictly ordered addition mechanisms with the respective other substrate adding first. | lld:pubmed |
| pubmed-article:776615 | pubmed:language | eng | lld:pubmed |
| pubmed-article:776615 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:776615 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:776615 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:776615 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:776615 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:776615 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:776615 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:776615 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:776615 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:776615 | pubmed:author | pubmed-author:KirschnerKK | lld:pubmed |
| pubmed-article:776615 | pubmed:author | pubmed-author:WeischetW OWO | lld:pubmed |
| pubmed-article:776615 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:776615 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:776615 | pubmed:volume | 64 | lld:pubmed |
| pubmed-article:776615 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:776615 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:776615 | pubmed:pagination | 313-20 | lld:pubmed |
| pubmed-article:776615 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
| pubmed-article:776615 | pubmed:meshHeading | pubmed-meshheading:776615-M... | lld:pubmed |
| pubmed-article:776615 | pubmed:meshHeading | pubmed-meshheading:776615-I... | lld:pubmed |
| pubmed-article:776615 | pubmed:meshHeading | pubmed-meshheading:776615-K... | lld:pubmed |
| pubmed-article:776615 | pubmed:meshHeading | pubmed-meshheading:776615-E... | lld:pubmed |
| pubmed-article:776615 | pubmed:meshHeading | pubmed-meshheading:776615-P... | lld:pubmed |
| pubmed-article:776615 | pubmed:meshHeading | pubmed-meshheading:776615-M... | lld:pubmed |
| pubmed-article:776615 | pubmed:meshHeading | pubmed-meshheading:776615-B... | lld:pubmed |
| pubmed-article:776615 | pubmed:meshHeading | pubmed-meshheading:776615-L... | lld:pubmed |
| pubmed-article:776615 | pubmed:meshHeading | pubmed-meshheading:776615-T... | lld:pubmed |
| pubmed-article:776615 | pubmed:year | 1976 | lld:pubmed |
| pubmed-article:776615 | pubmed:articleTitle | The binding of indole to the alpha-subunit and beta2-subunit and to the alpha2beta2-complex of tryptophan synthase from Escherichia coli. Identification of a second indole-binding site on the alpha-subunit. | lld:pubmed |
| pubmed-article:776615 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:776615 | lld:pubmed |
