| pubmed-article:8202475 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8202475 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:8202475 | lifeskim:mentions | umls-concept:C0001480 | lld:lifeskim |
| pubmed-article:8202475 | lifeskim:mentions | umls-concept:C0162449 | lld:lifeskim |
| pubmed-article:8202475 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:8202475 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:8202475 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:8202475 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:8202475 | pubmed:dateCreated | 1994-7-6 | lld:pubmed |
| pubmed-article:8202475 | pubmed:abstractText | During the reaction catalyzed by the phosphofructokinase (EC 2.7.1.11) from Escherichia coli, the phosphoryl group transferred from ATP interacts with Thr-125 [Shirakihara, Y. & Evans, P. R. (1988) J. Mol. Biol. 204, 973-994]. The replacement of Thr-125 by serine changes the saturation by fructose 6-phosphate from cooperative to hyperbolic and abolishes the allosteric inhibition by phosphoenolpyruvate. The same changes, a saturation by fructose 6-phosphate that is no longer cooperative and an activity that is no longer inhibited by phosphoenolpyruvate, are observed with wild-type phosphofructokinase when adenosine 5'-[gamma-thio]triphosphate is used instead of ATP as the phosphoryl donor. These two perturbations of the ATP-Thr-125 interaction lead to the suppression of both the allosteric inhibition by phosphoenolpyruvate and the cooperativity of fructose-6-phosphate saturation, as if replacing the neutral oxygen of ATP by sulfur or removing the methyl group of Thr-125 had "locked" phosphofructokinase in its active conformation. The geometry of this ATP-Thr-125 interaction and/or the presence of the methyl group on the beta-carbon of Thr-125 are crucial for the regulatory properties of phosphofructokinase. This interaction could be a hydrogen bond between the neutral oxygen of the gamma-phosphate of ATP and the hydroxyl group of Thr-125. | lld:pubmed |
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| pubmed-article:8202475 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8202475 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8202475 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8202475 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8202475 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8202475 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:8202475 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:8202475 | pubmed:author | pubmed-author:GarelJ RJR | lld:pubmed |
| pubmed-article:8202475 | pubmed:author | pubmed-author:Le BrasGG | lld:pubmed |
| pubmed-article:8202475 | pubmed:author | pubmed-author:AuzanCC | lld:pubmed |
| pubmed-article:8202475 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8202475 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:8202475 | pubmed:volume | 91 | lld:pubmed |
| pubmed-article:8202475 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8202475 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8202475 | pubmed:pagination | 5242-6 | lld:pubmed |
| pubmed-article:8202475 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:8202475 | pubmed:meshHeading | pubmed-meshheading:8202475-... | lld:pubmed |
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| pubmed-article:8202475 | pubmed:meshHeading | pubmed-meshheading:8202475-... | lld:pubmed |
| pubmed-article:8202475 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8202475 | pubmed:articleTitle | The cooperativity and allosteric inhibition of Escherichia coli phosphofructokinase depend on the interaction between threonine-125 and ATP. | lld:pubmed |
| pubmed-article:8202475 | pubmed:affiliation | Laboratoire d'Enzymologie, Centre National de la Recherche Scientifique, Gif-sur-Yvette, France. | lld:pubmed |
| pubmed-article:8202475 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8202475 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:948412 | entrezgene:pubmed | pubmed-article:8202475 | lld:entrezgene |
