Detection of a bromoperoxidase in Streptomyces phaeochromogenes.
A bromoperoxidase could be detected after fractionation in the chloramphenicol producing actinomycete, Streptomyces phaeochromogenes. This enzyme is capable of catalyzing the bromination of the antifungal antibiotic pyrrolnitrin [3-chloro-4-(2-nitro-3-chlorophenyl)pyrrole] in the 2-position of the pyrrole ring. The enzyme had a pH optimum of 5.0. This procaryotic bromoperoxidase requires the presence of H2O2 and can also brominate monochlorodimedone, but cannot catalyze chlorination. This enzyme is the first haloperoxidase described from procaryotic sources.
D006863:Hydrogen-Ion Concentration; D010544:Peroxidases / Q000378:metabolism*; D011764:Pyrrolnitrin / Q000378:metabolism; D013302:Streptomyces / Q000201:enzymology*
D010544:Peroxidases; C026195:bromide peroxidase; D011764:Pyrrolnitrin