| pubmed-article:3547407 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3547407 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:3547407 | lifeskim:mentions | umls-concept:C0038592 | lld:lifeskim |
| pubmed-article:3547407 | lifeskim:mentions | umls-concept:C0033629 | lld:lifeskim |
| pubmed-article:3547407 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:3547407 | pubmed:dateCreated | 1987-4-6 | lld:pubmed |
| pubmed-article:3547407 | pubmed:abstractText | Protein engineering of electrostatic interactions between charged substrates and complementary charged amino acids, at two different sites in the substrate binding cleft of the protease subtilisin BPN', increases kcat/Km toward complementary charged substrates (up to 1900 times) and decreases kcat/Km toward similarly charged substrates. From kinetic analysis of 16 mutants of subtilisin and the wild type, the average free energies for enzyme-substrate ion-pair interactions at the two different sites are calculated to be -1.8 +/- 0.5 and -2.3 +/- 0.6 kcal/mol (1 cal = 4.18 J) [at 25 degrees C in 0.1 M Tris X HCl (pH 8.6)]. The combined electrostatic effects are roughly additive. These studies demonstrate the feasibility for rational design of charged ligand binding sites in proteins by tailoring of electrostatic interactions. | lld:pubmed |
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| pubmed-article:3547407 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3547407 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3547407 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:3547407 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3547407 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:3547407 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:3547407 | pubmed:author | pubmed-author:WellsJ AJA | lld:pubmed |
| pubmed-article:3547407 | pubmed:author | pubmed-author:BotsR SRS | lld:pubmed |
| pubmed-article:3547407 | pubmed:author | pubmed-author:GraycarT PTP | lld:pubmed |
| pubmed-article:3547407 | pubmed:author | pubmed-author:PowersD BDB | lld:pubmed |
| pubmed-article:3547407 | pubmed:author | pubmed-author:EstellD ADA | lld:pubmed |
| pubmed-article:3547407 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3547407 | pubmed:volume | 84 | lld:pubmed |
| pubmed-article:3547407 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3547407 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3547407 | pubmed:pagination | 1219-23 | lld:pubmed |
| pubmed-article:3547407 | pubmed:dateRevised | 2010-9-10 | lld:pubmed |
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| pubmed-article:3547407 | pubmed:year | 1987 | lld:pubmed |
| pubmed-article:3547407 | pubmed:articleTitle | Designing substrate specificity by protein engineering of electrostatic interactions. | lld:pubmed |
| pubmed-article:3547407 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3547407 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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