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dc.contributor.authorWillner, Itamarde
dc.contributor.authorLion-Dagan, Mazzide
dc.contributor.authorRubin, Shaide
dc.contributor.authorWonner, Johannde
dc.contributor.authorEffenberger, Franzde
dc.contributor.authorBäuerle, Peterde
dc.date.accessioned2009-09-14de
dc.date.accessioned2016-03-31T07:47:50Z-
dc.date.available2009-09-14de
dc.date.available2016-03-31T07:47:50Z-
dc.date.issued1994de
dc.identifier.other316493511de
dc.identifier.urihttp://nbn-resolving.de/urn:nbn:de:bsz:93-opus-46419de
dc.identifier.urihttp://elib.uni-stuttgart.de/handle/11682/1199-
dc.identifier.urihttp://dx.doi.org/10.18419/opus-1182-
dc.description.abstractα-Chymotrypsin exhibits photoswitchable activities in an organic solvent after covalent modification of the protein backbone with thiophenefulgide active ester (2). The thiophenefulgide-modified α-chymotrypsin exhibits reversible photoisomerizable properties between states (3)-E and (3)-C. The modified α-chymotrypsin, where nine lysine residues are substituted by thiophenefulgide units, retains 60% of the activity of the native enzyme. The activities of thiophenefulgide-modified α-chymotrypsin toward esterification of N-acetyl-L-phenylalanine (4) by ethanol in cyclohexane are controlled by the configuration of the attached photoisomerizable component and by prior bioimprinting of the protein backbone with the reaction substrate (4). The esterification of (4) in cyclohexane using bioimprinted (3)-C is two-fold faster than in the presence of (3)-E. In the presence of a nonbioimprinted enzyme, esterification of (4) by (3)-C is five-fold faster than with (3)-E. The activity of bioimprinted (3)-E toward esterification of (4) is 4.5-fold higher than that of nonbioimprinted (3)-E. Switchable cyclic esterification of (4) is accomplished by sequential photoisomerization of the thiophenefulgide-modified α-chymotrypsin between states (3)-C and (3)-E.en
dc.language.isoende
dc.rightsinfo:eu-repo/semantics/openAccessde
dc.subject.classificationPhotoregulation , Proteine , Biokatalysatorde
dc.subject.ddc540de
dc.titlePhotoregulation of α-chymotrypsin activity in organic media : effects of bioimprintingen
dc.typearticlede
ubs.fakultaetFakultät Chemiede
ubs.fakultaetFakultätsübergreifend / Sonstige Einrichtungde
ubs.institutInstitut für Organische Chemiede
ubs.institutSonstige Einrichtungde
ubs.opusid4641de
ubs.publikation.sourcePhotochemistry and Photobiology 59 (1994), S. 491-496de
ubs.publikation.typZeitschriftenartikelde
Enthalten in den Sammlungen:03 Fakultät Chemie

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