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Purification and properties of fluoroacetate dehalogenase from Pseudomonas fluorescens DSM 8341

Donnelly, Clár, Murphy, Cormac D.·2009·Biotechnology Letters
DOI 10.1007/s10529-008-9849-4
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Abstract

The degradation of fluoroacetate by microorganisms has been established for some time, although only a handful of dehalogenases capable of hydrolyzing the stable C-F bond have been studied. Pseudomonas fluorescens DSM 8341 was originally isolated from soil and readily degrades fluoroacetate, thus it was thought that its dehalogenase might have some desirable properties. The enzyme was purified from cell-free extracts and characterised: it is a monomer of 32,500 Da, with a pH optimum of 8 and is stable between pH 4 and 10; its activity is stimulated by some metal ions (Mg(2+), Mn(2+) and Fe(3+)), but inhibited by others (Hg(2+), Ag(2+)). The enzyme is specific for fluoroacetate, and the K(m) for this substrate (0.68 mM) is the lowest determined for enzymes of this type that have been investigated to date.

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Research works printed but not linked: 16

  1. Goldman P (1965) Enzymatic cleavage of carbon-fluorine bond in fluoroacetate. J Biol Chem 240:3434–3438 · DOI · Paper page
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  7. Kurihara T, Yamauchi T, Ichiyama S, Takahata H, Esaki N (2003) Purification, characterization, and gene cloning of a novel fluoroacetate dehalogenase from Burkholderia sp FA1. J Mol Catal B 23:347–355 · DOI · Paper page
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  10. Liu JQ, Kurihara T, Miyagi M, Eskai N, Soda K (1998) Reaction mechanism of fluoroacetate dehalogenase from Moraxella sp. B. J Biol Chem 273:30897–30902 · DOI · Paper page
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Metadata

Authors
Donnelly, C., & Murphy, C. D.
Venue
Biotechnology Letters
Publisher
Springer Science and Business Media LLC
Published
2008-09-21
Volume
31
Issue
2
Pages
245-250
ISSN
  • 0141-5492
  • 1573-6776
DOI
10.1007/s10529-008-9849-4
Cited by
44
References
0
Language
en
Licence
www.springer.com/tdm (tdm)

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