Purification and Molecular and Catalytic Properties of Bromoperoxidase from Streptomyces phaeochromogenes

Journal of general microbiology 09/1985; 131(8):1911-6. DOI: 10.1099/00221287-131-8-1911
Source: PubMed


A bromoperoxidase has been isolated and purified from the chloramphenicol-producing actinomycete Streptomyces phaeochromogenes. The purified enzyme was homogeneous as determined by polyacrylamide gel electrophoresis. The prosthetic group of the bromoperoxidase was ferriprotoporphyrin IX. Based on gel filtration results the molecular weight of the enzyme was 147 000 +/- 3000. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis showed a single band having the mobility of a 72 500 molecular weight species. Therefore, in solution at neutral pH, the bromoperoxidase behaved as a dimer. The isoelectric point was 4.0. The spectral properties of the native and reduced enzyme are reported. The homogeneous enzyme also had peroxidase and catalase activity.

  • [Show abstract] [Hide abstract]
    ABSTRACT: A novel bromoperoxidase was isolated from the marine red alga Ceramium rubrum (Ceramiaceae, Rhodophyta); for the enzymic activity of this peroxidase the transition metal vanadium proved to be essential. The presence of vanadium in the enzyme preparation was established by atomic absorption spectrophotometry. Like the vanadium-containing bromoperoxidases from brown algae, this enzyme was not inhibited by cyanide or azide. This is the first report of the occurrence of a vanadium-containing bromoperoxidase in a red seaweed.
    No preview · Article · Apr 1987 · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
  • [Show abstract] [Hide abstract]
    ABSTRACT: 1.1. Extracts of a 25,000 g sediment of Murex trunculus hypobranchial gland homogenate contain an enzyme which brominates monochlorodimedon in the presence of bromide and H2O2.2.2. Dependence of activity on H2O2 concentration exhibits a sharp optimum which increases from 20 μM at pH 7.4 to 400 μM at pH Dependence on Br− concentration follows a simple saturation curve with Km values of 7 mM at pH 7.4 and 30 mM at pH The pH optima depend on H2O2 concentration, ranging from pH 6.6 at 10 μM to pH 4.8 at 200 μM.5.5. The enzyme is totally inactive with Cl− and F−, although both these ions inhibit bromination.
    No preview · Article · Dec 1987 · Comparative biochemistry and physiology. B, Comparative biochemistry
  • [Show abstract] [Hide abstract]
    ABSTRACT: A bromoperoxidase was isolated from the chlortetracycline-producing actinomycete, Streptomyces aureofaciens. This enzyme catalysed bromination and iodination, but surprisingly did not catalyse chlorination. The enzyme had an acidic pH optimum (pH 4.3) and the isoelectric point was 3.5. The Km for bromide was 20 mM and the Km for H2O2 was as high as 8 mM. The bromoperoxidase did not contain haem, since it was not inhibited by azide or cyanide. Excess bromide or chloride had no effect on its brominating activity; however, fluoride strongly inhibited the bromoperoxidase (Ki = 20 microM). On the basis of gel electrophoresis in the absence and presence of sodium dodecyl sulphate, the molecular mass of the enzyme was 65 kDa and it consisted of two subunits of 32 kDa each. The bromoperoxidase was remarkably thermostable.
    No preview · Article · Mar 1988 · Biochimica et Biophysica Acta
Show more