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dc.contributor.authorFischer, Markusde
dc.contributor.authorPleiss, Jürgende
dc.date.accessioned2006-06-02de
dc.date.accessioned2016-03-31T07:46:45Z-
dc.date.available2006-06-02de
dc.date.available2016-03-31T07:46:45Z-
dc.date.issued2003de
dc.identifier.other26255027Xde
dc.identifier.urihttp://nbn-resolving.de/urn:nbn:de:bsz:93-opus-26789de
dc.identifier.urihttp://elib.uni-stuttgart.de/handle/11682/851-
dc.identifier.urihttp://dx.doi.org/10.18419/opus-834-
dc.description.abstractThe Lipase Engineering Database (http://www.led.uni-stuttgart.de) integrates information on sequence, structure, and function of lipases, esterases, and related proteins. Sequence data on 806 protein entries are assigned to 38 homologous families, which are grouped into 16 superfamilies with no global sequence similarity between each other. For each family, multisequence alignments are provided with functionally relevant residues annotated. Pre-calculated phylogenetic trees allow navigation inside superfamilies. Experimental structures of 45 proteins are superposed and consistently annotated. The Lipase Engineering Database has been applied to systematically analyze sequence-structure-function relationships of this vast and diverse enzyme class. It is a useful tool to identify functionally relevant residues apart from the active site residues, and to design mutants with desired substrate specificity.en
dc.language.isoende
dc.rightsinfo:eu-repo/semantics/openAccessde
dc.subject.classificationBioinformatik , Molekulare Bioinformatik , Proteindesign , Alignment <Biochemie>de
dc.subject.ddc540de
dc.subject.otherintegrated database , sequence-structure-function relationship , relational database , sequence alignment , phylogenetic analysisen
dc.titleThe Lipase Engineering Database – a navigation and analysis tool for protein familiesen
dc.typepreprintde
dc.date.updated2015-12-11de
ubs.fakultaetFakultät Chemiede
ubs.institutInstitut für Technische Biochemiede
ubs.opusid2678de
ubs.publikation.sourceNucleic acids research 31 (2003), S. 319-321. URL http://dx.doi.org/10.1093/nar/gkg015de
ubs.publikation.typPreprintde
Enthalten in den Sammlungen:03 Fakultät Chemie

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