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http://hdl.handle.net/10261/47209
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Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Campo DC | Valor | Lengua/Idioma |
---|---|---|
dc.contributor.author | Gutiérrez, Mariana | - |
dc.contributor.author | Parella, Teodor | - |
dc.contributor.author | Joglar Tamargo, Jesús | - |
dc.contributor.author | Bujons, Jordi | - |
dc.contributor.author | Clapés Saborit, Pere | - |
dc.date.accessioned | 2012-03-20T10:36:04Z | - |
dc.date.available | 2012-03-20T10:36:04Z | - |
dc.date.issued | 2011 | - |
dc.identifier.citation | Chemical Communications | es_ES |
dc.identifier.issn | 1359-7345 | - |
dc.identifier.uri | http://hdl.handle.net/10261/47209 | - |
dc.description.abstract | Structure-guided re-design of the acceptor binding site of D-fructose-6-phosphate aldolase from E. coli leads to the construction of FSA A129S/A165G double mutant with an activity between 5- to >900-fold higher than that of wild-type towards N-Cbz-aminoaldehyde derivatives. | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | Royal Society of Chemistry (UK) | es_ES |
dc.rights | closedAccess | es_ES |
dc.title | Structure-guided redesign of D-fructose-6-phosphate aldolase from E. coli: remarkable activity and selectivity towards acceptor substrates by two-point mutation | es_ES |
dc.type | artículo | es_ES |
dc.identifier.doi | 10.1039/C1CC11069A | - |
dc.description.peerreviewed | Peer reviewed | es_ES |
dc.relation.publisherversion | http://dx.doi.org/10.1039/C1CC11069A | es_ES |
dc.identifier.e-issn | 1364-548X | - |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.fulltext | No Fulltext | - |
item.cerifentitytype | Publications | - |
item.openairetype | artículo | - |
item.languageiso639-1 | en | - |
item.grantfulltext | none | - |
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