1995
DOI: 10.1128/jb.177.9.2265-2269.1995
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Synthesis of fluoroacetate from fluoride, glycerol, and beta-hydroxypyruvate by Streptomyces cattleya

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Cited by 31 publications
(18 citation statements)
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“…In 1995 Tamura and co-workers demonstrated that [2-13 C] glycerol was incorporated into the carboxyl group of fluoroacetate by resting cell suspensions of S. cattleya (31). This observation lends support to the idea that the glycolytic pathway may provide the carbon substrate for the fluorination enzyme as glycerol is routed into glycolysis via the glycolytic intermediate dihydroxyacetone phosphate.…”
Section: Incorporation Of Glycerolsupporting
confidence: 52%
“…In 1995 Tamura and co-workers demonstrated that [2-13 C] glycerol was incorporated into the carboxyl group of fluoroacetate by resting cell suspensions of S. cattleya (31). This observation lends support to the idea that the glycolytic pathway may provide the carbon substrate for the fluorination enzyme as glycerol is routed into glycolysis via the glycolytic intermediate dihydroxyacetone phosphate.…”
Section: Incorporation Of Glycerolsupporting
confidence: 52%
“…The biosynthetic pathway to the fluorometabolites in S. cattleya was initially investigated by feeding radioisotope‐labelled putative precursors of the fluorination reaction to resting cell cultures and measuring the specific radioactivity in fluoroacetate (Reid et al. 1995; Tamura et al. 1995), but the results of these experiments were conflicting, making it difficult to draw conclusions.…”
Section: 4 Fluorinasementioning
confidence: 99%
“…8) as secondary metabolites by Sanada et al (1986) provided a more convenient system to study the biochemistry and enzymology of C-F bond formation. The biosynthetic pathway to the fluorometabolites in S. cattleya was initially investigated by feeding radioisotope-labelled putative precursors of the fluorination reaction to resting cell cultures and measuring the specific radioactivity in fluoroacetate (Reid et al 1995;Tamura et al 1995), but the results of these experiments were conflicting, making it difficult to draw conclusions. A greater understanding of the biosynthetic origin of the fluorometabolites was achieved with feeding experiments using stable isotope labelled precursors (Hamilton et al 1998).…”
Section: Fluorinasementioning
confidence: 99%
“…However, we found that the wild-type enzyme is not affected by toluene when suspended in a reaction mixture at a ratio of 10% (v/v). The reaction mixture containing 10 mol of Tris sulfate (pH 9.5), 0.75 mol of sodium hydroxide, the wild-type or the H272N mutant enzyme (1 mg each), and 10 l of toluene solution containing [1][2][3][4][5][6][7][8][9][10][11][12][13][14] C]chloroacetic acid in a final volume of 100 l was incubated at 30°C for 2 h. The reaction mixture was dialyzed against 50 mM potassium phosphate (pH 7.5) for 14 h and then applied to a C 18 reverse phase HPLC column. The elution was carried out with 0.05% trifluoroacetic acid for 5 min, followed by a linear gradient of 0 -80% acetonitrile in 0.05% trifluoroacetic acid as described above.…”
Section: Labeling Of H272n Mutant Enzyme With [ 14 C]chloroacetate-comentioning
confidence: 99%