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dc.contributor.authorUrlacher, Vlada B.de
dc.contributor.authorSchmid, Rolf D.de
dc.date.accessioned2006-06-01de
dc.date.accessioned2016-03-31T07:46:42Z-
dc.date.available2006-06-01de
dc.date.available2016-03-31T07:46:42Z-
dc.date.issued2002de
dc.identifier.other26254329Xde
dc.identifier.urihttp://nbn-resolving.de/urn:nbn:de:bsz:93-opus-26573de
dc.identifier.urihttp://elib.uni-stuttgart.de/handle/11682/834-
dc.identifier.urihttp://dx.doi.org/10.18419/opus-817-
dc.description.abstractRecent studies on microbial cytochrome P450 enzymes cover several new areas. Advances have been made in structure-function analysis. New non-enzymatic/electrochemical systems for the replacement of NAD(P)H have been developed. The properties of some enzymes have been re-engineered by site-directed mutagenesis or by methods of directed evolution. New P450s have been functionally expressed and characterized. A combination of these approaches is believed to facilitate the use of isolated P450 monooxygenases in biocatalysis.en
dc.language.isoende
dc.rightsinfo:eu-repo/semantics/openAccessde
dc.subject.classificationCytochrom P-450 , Monooxygenasen , Biokatalyse , Biokonversion , Biotransformation , Proteindesignde
dc.subject.ddc540de
dc.titleBiotransformations using prokaryotic P450 monooxygenasesen
dc.typepreprintde
dc.date.updated2015-12-10de
ubs.fakultaetFakultät Chemiede
ubs.institutInstitut für Technische Biochemiede
ubs.opusid2657de
ubs.publikation.sourceCurrent opinion in biotechnology 13 (2002), S. 557-564. URL http://dx.doi.org/10.1016/S0958-1669(02)00357-9de
ubs.publikation.typPreprintde
Enthalten in den Sammlungen:03 Fakultät Chemie

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