Linked Life Data

15623532

Source:http://linkedlifedata.com/resource/pubmed/id/15623532

Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:15623532rdf:typepubmed:Citationlld:pubmed
pubmed-article:15623532lifeskim:mentionsumls-concept:C0009235lld:lifeskim
pubmed-article:15623532lifeskim:mentionsumls-concept:C0043481lld:lifeskim
pubmed-article:15623532lifeskim:mentionsumls-concept:C0057072lld:lifeskim
pubmed-article:15623532lifeskim:mentionsumls-concept:C0442805lld:lifeskim
pubmed-article:15623532lifeskim:mentionsumls-concept:C0597571lld:lifeskim
pubmed-article:15623532lifeskim:mentionsumls-concept:C0678594lld:lifeskim
pubmed-article:15623532lifeskim:mentionsumls-concept:C0037791lld:lifeskim
pubmed-article:15623532lifeskim:mentionsumls-concept:C0205197lld:lifeskim
pubmed-article:15623532lifeskim:mentionsumls-concept:C1875307lld:lifeskim
pubmed-article:15623532pubmed:issue11lld:pubmed
pubmed-article:15623532pubmed:dateCreated2005-3-14lld:pubmed
pubmed-article:15623532pubmed:abstractTextPichia stipitis NAD(+)-dependent xylitol dehydrogenase (XDH), a medium-chain dehydrogenase/reductase, is one of the key enzymes in ethanol fermentation from xylose. For the construction of an efficient biomass-ethanol conversion system, we focused on the two areas of XDH, 1) change of coenzyme specificity from NAD(+) to NADP(+) and 2) thermostabilization by introducing an additional zinc atom. Site-directed mutagenesis was used to examine the roles of Asp(207), Ile(208), Phe(209), and Asn(211) in the discrimination between NAD(+) and NADP(+). Single mutants (D207A, I208R, F209S, and N211R) improved 5 approximately 48-fold in catalytic efficiency (k(cat)/K(m)) with NADP(+) compared with the wild type but retained substantial activity with NAD(+). The double mutants (D207A/I208R and D207A/F209S) improved by 3 orders of magnitude in k(cat)/K(m) with NADP(+), but they still preferred NAD(+) to NADP(+). The triple mutant (D207A/I208R/F209S) and quadruple mutant (D207A/I208R/F209S/N211R) showed more than 4500-fold higher values in k(cat)/K(m) with NADP(+) than the wild-type enzyme, reaching values comparable with k(cat)/K(m) with NAD(+) of the wild-type enzyme. Because most NADP(+)-dependent XDH mutants constructed in this study decreased the thermostability compared with the wild-type enzyme, we attempted to improve the thermostability of XDH mutants by the introduction of an additional zinc atom. The introduction of three cysteine residues in wild-type XDH gave an additional zinc-binding site and improved the thermostability. The introduction of this mutation in D207A/I208R/F209S and D207A/I208R/F209S/N211R mutants increased the thermostability and further increased the catalytic activity with NADP(+).lld:pubmed
pubmed-article:15623532pubmed:languageenglld:pubmed
pubmed-article:15623532pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15623532pubmed:citationSubsetIMlld:pubmed
pubmed-article:15623532pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15623532pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15623532pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15623532pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15623532pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15623532pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15623532pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15623532pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15623532pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15623532pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15623532pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15623532pubmed:statusMEDLINElld:pubmed
pubmed-article:15623532pubmed:monthMarlld:pubmed
pubmed-article:15623532pubmed:issn0021-9258lld:pubmed
pubmed-article:15623532pubmed:authorpubmed-author:MakinoKeisuke...lld:pubmed
pubmed-article:15623532pubmed:authorpubmed-author:WatanabeSeiya...lld:pubmed
pubmed-article:15623532pubmed:authorpubmed-author:KodakiTsutomu...lld:pubmed
pubmed-article:15623532pubmed:issnTypePrintlld:pubmed
pubmed-article:15623532pubmed:day18lld:pubmed
pubmed-article:15623532pubmed:volume280lld:pubmed
pubmed-article:15623532pubmed:ownerNLMlld:pubmed
pubmed-article:15623532pubmed:authorsCompleteYlld:pubmed
pubmed-article:15623532pubmed:pagination10340-9lld:pubmed
pubmed-article:15623532pubmed:dateRevised2008-11-21lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:meshHeadingpubmed-meshheading:15623532...lld:pubmed
pubmed-article:15623532pubmed:year2005lld:pubmed
pubmed-article:15623532pubmed:articleTitleComplete reversal of coenzyme specificity of xylitol dehydrogenase and increase of thermostability by the introduction of structural zinc.lld:pubmed
pubmed-article:15623532pubmed:affiliationInstitute of Advanced Energy, Kyoto University, Gokasyo, Uji, Kyoto 611-0011, Japan.lld:pubmed
pubmed-article:15623532pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:15623532pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15623532lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15623532lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15623532lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15623532lld:pubmed