| pubmed-article:10199659 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10199659 | lifeskim:mentions | umls-concept:C0014279 | lld:lifeskim |
| pubmed-article:10199659 | lifeskim:mentions | umls-concept:C0020291 | lld:lifeskim |
| pubmed-article:10199659 | lifeskim:mentions | umls-concept:C0014898 | lld:lifeskim |
| pubmed-article:10199659 | lifeskim:mentions | umls-concept:C0443286 | lld:lifeskim |
| pubmed-article:10199659 | lifeskim:mentions | umls-concept:C0205681 | lld:lifeskim |
| pubmed-article:10199659 | lifeskim:mentions | umls-concept:C0813987 | lld:lifeskim |
| pubmed-article:10199659 | lifeskim:mentions | umls-concept:C1707689 | lld:lifeskim |
| pubmed-article:10199659 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:10199659 | pubmed:dateCreated | 1999-6-1 | lld:pubmed |
| pubmed-article:10199659 | pubmed:abstractText | Four-helix bundle proteins have been designed that catalyze the hydrolysis and transesterification reactions of p-nitrophenyl esters by a cooperative nucleophilic and general acid mechanism. The catalysts consist of two 42-residue peptides that fold into helix-loop-helix motifs and dimerise. They have previously been shown to recognize anionic and hydrophobic substrates and to follow saturation kinetics. The catalytic entity is a HisH(+)-His pair in a helical segment spaced i, i+4, which can be supplemented by arginines and lysines in the adjacent helix. The binding residues have now been optimized for the catalysis of mono-p-nitrophenyl fumarate hydrolysis and found to vary with the location of the site. The catalytic efficiency of the HisH(+)-His site in helix II in positions 30 and 34 is enhanced by the introduction of arginine and or lysine residues in positions 11 and 15, but not in 8 and 11 or in 15 and 19. The most efficient catalyst using this site, JNIIR11K15, catalyses the reaction with a second-order rate constant of 0.134 M(-1) s(-1) in aqueous solution at pH 5.1 and 290 K. The second-order rate constant is larger than those of the corresponding sites with 'longer' and 'shorter' binding residues. Similar experiments have shown that the efficiency and selectivity of catalysts based on a HisH(+)-11-His-15 site in helix I are enhanced the most by the introduction of Lys-30 and Arg-34. | lld:pubmed |
| pubmed-article:10199659 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10199659 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10199659 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10199659 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10199659 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10199659 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10199659 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10199659 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10199659 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10199659 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10199659 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10199659 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10199659 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10199659 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10199659 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:10199659 | pubmed:issn | 0968-0896 | lld:pubmed |
| pubmed-article:10199659 | pubmed:author | pubmed-author:NilssonJJ | lld:pubmed |
| pubmed-article:10199659 | pubmed:author | pubmed-author:NilssonHH | lld:pubmed |
| pubmed-article:10199659 | pubmed:author | pubmed-author:BaltzerLL | lld:pubmed |
| pubmed-article:10199659 | pubmed:author | pubmed-author:BrooK SKS | lld:pubmed |
| pubmed-article:10199659 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10199659 | pubmed:volume | 7 | lld:pubmed |
| pubmed-article:10199659 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10199659 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10199659 | pubmed:pagination | 83-91 | lld:pubmed |
| pubmed-article:10199659 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:10199659 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10199659 | pubmed:articleTitle | Designed four-helix bundle catalysts--the engineering of reactive sites for hydrolysis and transesterification reactions of p-nitrophenyl esters. | lld:pubmed |
| pubmed-article:10199659 | pubmed:affiliation | Department of Chemistry, Göteborg University, Sweden. lars.baltzer@oc.chalmers.se | lld:pubmed |
| pubmed-article:10199659 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10199659 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10199659 | lld:pubmed |
