Bacterial defluorination of 4-fluoroglutamic acid

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dc.contributor.author Donnelly, Clár
dc.contributor.author Murphy, Cormac D.
dc.date.accessioned 2012-09-04T15:44:28Z
dc.date.available 2012-09-04T15:44:28Z
dc.date.copyright 2007 Springer-Verlag en
dc.date.issued 2007
dc.identifier.citation Applied microbiology and biotechnology en
dc.identifier.uri http://hdl.handle.net/10197/3781
dc.description.abstract Fluorinated amino acids are used as enzyme inhibitors, mechanistic probes and in the production of pharmacologically active peptides. Because enantiomerically pure 4-fluoroglutamate is difficult to prepare, the selective degradation of the l-isomer is a potentially convenient method of obtaining d-4-fluoroglutamate from the racemate. In this paper, we describe our investigations on the degradation of 4-fluoroglutamate by bacteria. Fluoride ion was detected in resting-cell cultures of a number of bacteria that were incubated with racemic 4-fluoroglutamate. Analysis of the culture supernatants by chiral gas chromatography–mass spectrometry revealed that only the l-isomer was degraded. The degradation of 4-fluoroglutamate was also examined in cell-free extracts of Streptomyces cattleya and Proteus mirabilis, and it was observed that equimolar concentrations of fluoride ion and ammonia were generated. The activity was located in the soluble fraction of cell extracts, thus is not related to the l-2-amino-4-chloro-4-pentenoic acid dehydrochlorinase previously identified in membrane fractions of P. mirabilis. en
dc.description.sponsorship Other funder en
dc.language.iso en en
dc.publisher Springer en
dc.relation.requires CSCB Research Collection en
dc.rights The final publication is available at www.springerlink.com en
dc.subject Dehalogenation en
dc.subject Amino acid en
dc.subject Bacteria en
dc.subject.lcsh Amino acids en
dc.subject.lcsh Organofluorine compounds en
dc.subject.lcsh Bacteria en
dc.title Bacterial defluorination of 4-fluoroglutamic acid en
dc.type Journal Article en
dc.internal.availability Full text available en
dc.status Peer reviewed en
dc.identifier.volume 77 en
dc.identifier.issue 3 en
dc.identifier.startpage 699 en
dc.identifier.endpage 703 en
dc.identifier.doi 10.1007/s00253-007-1200-9
dc.neeo.contributor Donnelly|Clár|aut|
dc.neeo.contributor Murphy|Cormac D.|aut|
dc.description.othersponsorship Enterprise Ireland en


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