Please use this identifier to cite or link to this item: http://dx.doi.org/10.18419/opus-8016
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dc.contributor.authorPieper, Dietmar H.de
dc.contributor.authorStadler-Fritzsche, Karinde
dc.contributor.authorKnackmuss, Hans-Joachimde
dc.contributor.authorEngesser, Karl-Heinrichde
dc.contributor.authorBruce, Neil C.de
dc.contributor.authorCain, Ronald B.de
dc.date.accessioned2012-08-22de
dc.date.accessioned2016-03-31T11:44:55Z-
dc.date.available2012-08-22de
dc.date.available2016-03-31T11:44:55Z-
dc.date.issued1990de
dc.identifier.other371054478de
dc.identifier.urihttp://nbn-resolving.de/urn:nbn:de:bsz:93-opus-76458de
dc.identifier.urihttp://elib.uni-stuttgart.de/handle/11682/8033-
dc.identifier.urihttp://dx.doi.org/10.18419/opus-8016-
dc.description.abstract4-Carboxymethyl-4-methylbut-2-en-4-olide (4-methyl-2-enelactone) isomerase, transforming 4-methyl-2-enelactone to 3-methyl-2-enelactone, was purified from a derivative strain of Pseudomonas sp. B13, named B13 FR1, carrying the plasmid pFRC2OP. This plasmid contained the isomerase gene cloned from Alcaligenes eutrophus JMP 134, which uses 4-methyl-2-enelactone as a carbon source. The enzyme consists of a single peptide chain of Mr 40,000 as judged by SDS/PAGE. In addition to 4-methyl-2-enelactone, the putative reaction intermediate, 1-methyl-3,7-dioxo-2,6-dioxy-bicyclo[3.3.0]octane (1-methylbislactone), was a substrate for the enzyme, but kinetic data presented did not favour its role as a reaction intermediate. Isomeric methyl-substituted 4-carboxymethylbut-2-en-4-olides were neither substrates nor inhibitors. Possible reaction mechanisms are discussed.en
dc.language.isoende
dc.rightsinfo:eu-repo/semantics/openAccessde
dc.subject.classificationAlcaligenes eutrophus , Brenzcatechinde
dc.subject.ddc570de
dc.titlePurification and characterization of 4-methylmuconolactone methylisomerase, a novel enzyme of the modified 3-oxoadipate pathway in the gram-negative bacterium Alcaligenes eutrophus JMP 134en
dc.typearticlede
ubs.fakultaetFakultätsübergreifend / Sonstige Einrichtungde
ubs.fakultaetFakultät Energie-, Verfahrens- und Biotechnikde
ubs.institutSonstige Einrichtungde
ubs.institutInstitut für Mikrobiologiede
ubs.opusid7645de
ubs.publikation.sourceBiochemical journal 271 (1990), S. 529-534. URL http://www.biochemj.org/bj/271/0529/2710529.pdfde
ubs.publikation.typZeitschriftenartikelde
Appears in Collections:15 Fakultätsübergreifend / Sonstige Einrichtung

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