| pubmed-article:20851958 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20851958 | lifeskim:mentions | umls-concept:C1001404 | lld:lifeskim |
| pubmed-article:20851958 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:20851958 | lifeskim:mentions | umls-concept:C0009221 | lld:lifeskim |
| pubmed-article:20851958 | lifeskim:mentions | umls-concept:C0233820 | lld:lifeskim |
| pubmed-article:20851958 | lifeskim:mentions | umls-concept:C0439851 | lld:lifeskim |
| pubmed-article:20851958 | lifeskim:mentions | umls-concept:C1324819 | lld:lifeskim |
| pubmed-article:20851958 | lifeskim:mentions | umls-concept:C1552596 | lld:lifeskim |
| pubmed-article:20851958 | lifeskim:mentions | umls-concept:C0457083 | lld:lifeskim |
| pubmed-article:20851958 | lifeskim:mentions | umls-concept:C1947931 | lld:lifeskim |
| pubmed-article:20851958 | pubmed:issue | 22 | lld:pubmed |
| pubmed-article:20851958 | pubmed:dateCreated | 2010-11-8 | lld:pubmed |
| pubmed-article:20851958 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20851958 | pubmed:abstractText | Schwanniomyces occidentalis ?-fructofuranosidase (Ffase) releases ?-fructose from the nonreducing ends of ?-fructans and synthesizes 6-kestose and 1-kestose, both considered prebiotic fructooligosaccharides. Analyzing the amino acid sequence of this protein revealed that it includes a serine instead of a leucine at position 196, caused by a nonuniversal decoding of the unique mRNA leucine codon CUG. Substitution of leucine for Ser196 dramatically lowers the apparent catalytic efficiency (k(cat)/K(m)) of the enzyme (approximately 1,000-fold), but surprisingly, its transferase activity is enhanced by almost 3-fold, as is the enzymes' specificity for 6-kestose synthesis. The influence of 6 Ffase residues on enzyme activity was analyzed on both the Leu196/Ser196 backgrounds (Trp47, Asn49, Asn52, Ser111, Lys181, and Pro232). Only N52S and P232V mutations improved the transferase activity of the wild-type enzyme (about 1.6-fold). Modeling the transfructosylation products into the active site, in combination with an analysis of the kinetics and transfructosylation reactions, defined a new region responsible for the transferase specificity of the enzyme. | lld:pubmed |
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| pubmed-article:20851958 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20851958 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20851958 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20851958 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20851958 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:20851958 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20851958 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20851958 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:20851958 | pubmed:issn | 1098-5336 | lld:pubmed |
| pubmed-article:20851958 | pubmed:author | pubmed-author:Sanz-Aparicio... | lld:pubmed |
| pubmed-article:20851958 | pubmed:author | pubmed-author:Fernández-Lob... | lld:pubmed |
| pubmed-article:20851958 | pubmed:author | pubmed-author:PortilloFranc... | lld:pubmed |
| pubmed-article:20851958 | pubmed:author | pubmed-author:Alvaro-Benito... | lld:pubmed |
| pubmed-article:20851958 | pubmed:author | pubmed-author:de... | lld:pubmed |
| pubmed-article:20851958 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20851958 | pubmed:volume | 76 | lld:pubmed |
| pubmed-article:20851958 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20851958 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20851958 | pubmed:pagination | 7491-9 | lld:pubmed |
| pubmed-article:20851958 | pubmed:dateRevised | 2011-7-28 | lld:pubmed |
| pubmed-article:20851958 | pubmed:meshHeading | pubmed-meshheading:20851958... | lld:pubmed |
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| pubmed-article:20851958 | pubmed:meshHeading | pubmed-meshheading:20851958... | lld:pubmed |
| pubmed-article:20851958 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20851958 | pubmed:articleTitle | New insights into the fructosyltransferase activity of Schwanniomyces occidentalis ß-fructofuranosidase, emerging from nonconventional codon usage and directed mutation. | lld:pubmed |
| pubmed-article:20851958 | pubmed:affiliation | Centro de Biología Molecular Severo Ochoa, Departamento de Biología Molecular (UAM-CSIC), Universidad Autónoma Madrid, Cantoblanco, 28049 Madrid, Spain. | lld:pubmed |
| pubmed-article:20851958 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20851958 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
