Biotransformation of ionones by engineered cytochrome P450 BM-3

Urlacher, Vlada B.; Makhsumkhanov, Akhmadjan; Schmid, Rolf D.

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DC Element	Wert	Sprache
dc.contributor.author	Urlacher, Vlada B.	de
dc.contributor.author	Makhsumkhanov, Akhmadjan	de
dc.contributor.author	Schmid, Rolf D.	de
dc.date.accessioned	2006-06-01	de
dc.date.accessioned	2016-03-31T07:46:43Z	-
dc.date.available	2006-06-01	de
dc.date.available	2016-03-31T07:46:43Z	-
dc.date.issued	2005	de
dc.identifier.other	263638626	de
dc.identifier.uri	http://nbn-resolving.de/urn:nbn:de:bsz:93-opus-26603	de
dc.identifier.uri	http://elib.uni-stuttgart.de/handle/11682/837	-
dc.identifier.uri	http://dx.doi.org/10.18419/opus-820	-
dc.description.abstract	Wild type cytochrome P450 monooxygenase from Bacillus megaterium (P450 BM-3) has low activity for the hydroxylation of beta-ionone (>1 min-1). Substitution of phenylalanine by valine at position 87 increased the beta-ionone hydroxylation activity up to 100-fold (115 min-1). For further activity improvement methods of site-directed and random mutagenesis were applied. The R47L Y51F F87V mutant, designed by site-directed mutagenesis and the A74E F87V P386S mutant, obtained after two rounds of error-prone PCR, exhibit an increase in activity up to 300-fold compared to the wild type enzyme. All mutants converted -ionone regioselectively to 4-hydroxy-beta-ionone.	en
dc.language.iso	en	de
dc.rights	info:eu-repo/semantics/openAccess	de
dc.subject.classification	Cytochrom P-450 , Monooxygenasen , Biokatalyse , Biokonversion , Biotransformation , Hydroxylierung , Mutagenese , Genbibliothek	de
dc.subject.ddc	540	de
dc.subject.other	P450 BM-3 , beta-ionone , regioselectivity , mutagenesis , gene library	en
dc.title	Biotransformation of ionones by engineered cytochrome P450 BM-3	en
dc.type	preprint	de
dc.date.updated	2015-12-10	de
ubs.fakultaet	Fakultät Chemie	de
ubs.institut	Institut für Technische Biochemie	de
ubs.opusid	2660	de
ubs.publikation.source	Applied microbiology & biotechnology 70 (2006), S. 53-59. URL http://dx.doi.org./10.1007/s00253-005-0028-4	de
ubs.publikation.typ	Preprint	de
Enthalten in den Sammlungen:	03 Fakultät Chemie

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