Bacterial defluorination of 4-fluoroglutamic acid

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Title: Bacterial defluorination of 4-fluoroglutamic acid
Authors: Donnelly, Clár
Murphy, Cormac D.
Permanent link: http://hdl.handle.net/10197/3781
Date: 2007
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.
Funding Details: Other funder
Type of material: Journal Article
Publisher: Springer
Copyright (published version): 2007 Springer-Verlag
Keywords: Dehalogenation;Amino acid;Bacteria
Subject LCSH: Amino acids
Organofluorine compounds
Bacteria
DOI: 10.1007/s00253-007-1200-9
Language: en
Status of Item: Peer reviewed
Appears in Collections:Biomolecular and Biomedical Science Research Collection
CSCB Research Collection

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