Purification and some characteristics of a non-haem bromoperoxidase from Streptomyces aureofaciens.
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.
D000596:Amino Acids / Q000032:analysis; D001965:Bromides / Q000494:pharmacology; D002384:Catalysis; D002712:Chlorides / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D010544:Peroxidases / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000494:pharmacology; D013304:Streptomyces aureofaciens / Q000201:enzymology*
D000596:Amino Acids; D001965:Bromides; D002712:Chlorides; D010544:Peroxidases; C026195:bromide peroxidase