Dehalogenases in Soil Bacteria

Hardman, David J.; Slater, J. Howard

doi:10.1099/00221287-123-1-117

Cited by 49 publications

(61 citation statements)

References 8 publications

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“…Activity stain PAGE, utilizing Ag+ to precipitate free halide ions in regions of dehalogenase activities, has been employed to identify electrophoretically distinguishable 2-haloacid halidohydrolases (Slater et al, 1979;Hardman & Slater, 1981 ;Allison et al, 1983). The same technique was used by Scholtz et al (1988) to visualize one of the dehalogenase activities in Arthrobacter sp.…”

Section: Discussionmentioning

confidence: 99%

“…Dehalogenase activity was visualized after native PAGE by an activity reaction in the gel (cf. Hardman & Slater, 1981). Haloalkane substrates were incorporated into the gel as an emulsion by sonication of 10-200 pl haloalkane with 40 ml acrylamide solution immediately before casting the gel.…”

Section: Methodsmentioning

confidence: 99%

“…3 ; Goldman, 1965). Microorganisms possessing these enzymes are readily isolated from most soils and many have been shown to produce more than one halidohydrolase with activity towards mono-and disubstituted 2-haloacids (Hardman & Slater, 1981;Allison et al, 1983).…”

Section: Introductionmentioning

confidence: 99%

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Isolation and characterization of a haloalkane halidohydrolase from Rhodococcus erythropolis Y2

Sallis

Armfield²,

Bull

et al. 1990

Journal of General Microbiology

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Rhodococcus erythropolis strain Y2, isolated from soil by enrichment culture using 1-chlorobutane, was able to utilize a range of halogenated aliphatic compounds as sole sources of carbon and energy. The ability to utilize 1-chlorobutane was conferred by a single halidohydrolase-type haloalkane dehalogenase. The presence of the single enzyme in cell-free extracts was demonstrated by activity stain polyacrylamide gel electrophoresis. The purified enzyme was a monomeric protein with a relative molecular mass of 34 kDa and demonstrated activity against a broad range of haloalkanes, haloalcohols and haloethers. The highest activity was found towards a, o disubstituted chloro-and bromo-C2-C6 alkanes and 4-chlorobutanol. The K,,, value of the enzyme for 1-chlorobutane was 0.26 mM. A comparison of the R. erythropolis Y2 haloalkane halidohydrolase with other haloalkane dehalogenases is discussed on the basis of biochemical properties and N-terminal amino acid sequence data.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Isolation and characterization of a haloalkane halidohydrolase from Rhodococcus erythropolis Y2

Sallis

Armfield²,

Bull

et al. 1990

Journal of General Microbiology

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“…Dehalogenase activity was measured in cell-free extracts as previously described (Weightman & Slater, 1980;Hardman & Slater, 1981). One unit of dehalogenase activity was defined as the amount of enzyme catalysing the conversion of 1 ymol MCA min-' (mg protein)-'.…”

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confidence: 99%

Stereospecificity of 2-Monochloropropionate Dehalogenation by the Two Dehalogenases of Pseudomonas putida PP3: Evidence for Two Different Dehalogenation Mechanisms

Weightman¹,

Al²,

Jh³

1982

Microbiology

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Pseudomonas putida PP3 grew on DL-2-monochloropropionate (2MC PA) with a release of chloride ions consistent with the dechlorination of both isomers. The organism grew on either D-or L-2MCPA. Dehalogenase activity in cell-free extracts showed that both D-and L -~M C PA were dehalogenated. Pseudomonas putida PP3 contains two dehalogenases, and studies with the separated enzymes revealed that the fraction I enzyme used both D-and L-2MCPA, the rate of dechlorination of L-2MCPA being 80% of the rate of D-2MCPA dechlorination. The product of the reaction, lactate, retained the same optical configuration as the substrate provided. The fraction I1 dehalogenase also dechlorinated D-and L-2MCPA, with the same difference in rates as for the fraction I dehalogenase, but the lactates produced were of the opposite configuration to their precursors. The two dehalogenases showed further differences with respect to inhibition by two sulphydryl-blocking agents, N-ethylmaleimide and p-chloromercuribenzoate. Fraction I dehalogenase was considerably more sensitive to these two reagents compared with the fraction I1 dehalogenase. Dithiothreitol partially protected the fraction I dehalogenase from N-ethylmaleimide inhibition. The results are discussed in terms of the possible evolutionary relationships of the two dehalogenases.

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“…Leisinger 1963;Goldman 1965), and a considerable understanding of the halidohydrolases involved has been attained (Hardman and Slater 1981;Motosugi and Soda 1983;Miiller and Lingens 1986;Tsang et al 1988). Anaerobic degradation of haloacetates has not been observed, even though monochloroacetate halidohydrolases might be expected to function anaerobically.…”

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Monochloro- and dichloroacetic acids as carbon and energy sources for a stable, methanogenic mixed culture

Egli¹,

Thüer

Suter³

et al. 1989

Arch. Microbiol.

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Abstract.A stable methanogenic mixed culture was enriched from an industrial environment to utilize chloroacetate as sole carbon and energy source for growth. It immobilized spontaneously on activated charcoal and grew reproducibly on this carrier in a fluidized bed reactor when supplied with an anaerobic mineral salts medium. Substrate disappearance was complete. Methane, CO2 and chloride ions were conclusively identified as the metabolic products and quantified. The growth yield from chloroacetate was about I g of protein/mol of carbon. The calculated degradation rate in the fluidized bed reactor was 0.2 to 0.8 mmol/1-h. The first metabolic intermediate from [2-13C]monochloroacetat e in portions of biofilm-coated carrier was shown by 13C_NM R to be glycolate, from which 13C02 and 13CH4 were formed. Glycolate was formed in an oxygen-insensitive hydrolysis, but its conversion to C02 and CH4 was strictly anaerobic and sensitive to inhibition by bromoethanesulfonate. Degradation of [1-14C]-and [2-14C]_chloroacetat e each yielded the same amount of [14C]-methane. We thus presume glycolate to be cleaved to CO2 and Ha, which were the substrates for methanogenesis. Dehalogenation was limited to chloro-, bromo-, iodo-and dichloroacetate. These four compounds and glycolate were utilized as the sole carbon and energy sources by the methanogenic mixed culture.

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Dehalogenases in Soil Bacteria

Cited by 49 publications

References 8 publications

Isolation and characterization of a haloalkane halidohydrolase from Rhodococcus erythropolis Y2

Isolation and characterization of a haloalkane halidohydrolase from Rhodococcus erythropolis Y2

Stereospecificity of 2-Monochloropropionate Dehalogenation by the Two Dehalogenases of Pseudomonas putida PP3: Evidence for Two Different Dehalogenation Mechanisms

Monochloro- and dichloroacetic acids as carbon and energy sources for a stable, methanogenic mixed culture

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