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dc.contributor.authorBarth, Sandrade
dc.contributor.authorFischer, Markusde
dc.contributor.authorSchmid, Rolf D.de
dc.contributor.authorPleiss, Jürgende
dc.date.accessioned2006-06-01de
dc.date.accessioned2016-03-31T07:46:44Z-
dc.date.available2006-06-01de
dc.date.available2016-03-31T07:46:44Z-
dc.date.issued2004de
dc.identifier.other262545233de
dc.identifier.urihttp://nbn-resolving.de/urn:nbn:de:bsz:93-opus-26690de
dc.identifier.urihttp://elib.uni-stuttgart.de/handle/11682/845-
dc.identifier.urihttp://dx.doi.org/10.18419/opus-828-
dc.description.abstractThe epoxide hydrolases and haloalkane dehalogenase database (EH/HD) integrates sequence and structure of a highly diverse protein family including mainly the Asp-hydrolases of EHs and HDs but also proteins like the Ser-hydrolases non-heme peroxidases, prolyl iminopetidases or 2-hydroxymuconic semialdehyde hydrolases. These proteins have a highly conserved structure, but display a remarkable diversity in sequence and function. 305 protein entries were assigned to 14 homologous families, forming two superfamilies. Annotated multisequence alignments and phylogenetic trees are provided for each homologous family and superfamily. Experimentally derived structures of 19 proteins are superposed and consistently annotated. Sequence and structure of all 305 proteins were systematically analysed. Thus, deeper insight is gained into the role of a highly conserved sequence motifs and structural elements. The EH/HD database is available at http://www.led.uni-stuttgart.de.en
dc.language.isoende
dc.rightsinfo:eu-repo/semantics/openAccessde
dc.subject.classificationBioinformatik , Molekulare Bioinformatik , Proteindesign , Alignment <Biochemie> , Hydrolasen , Dehalogenasende
dc.subject.ddc540de
dc.subject.otherSequence-structure-function relationship , sequence alignment , protein structure , phylogenetic analysis , GXGXS-motifen
dc.titleThe database of epoxide hydrolases and haloalkane dehalogenases: one structure, many functionsen
dc.typepreprintde
dc.date.updated2015-12-10de
ubs.fakultaetFakultät Chemiede
ubs.institutInstitut für Technische Biochemiede
ubs.opusid2669de
ubs.publikation.sourceBioinformatics 20 (2004), S. 2845-2847. URL http://dx.doi.org./10.1093/bioinformatics/bth284de
ubs.publikation.typPreprintde
Enthalten in den Sammlungen:03 Fakultät Chemie

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