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Detection of a bromoperoxidase in Streptomyces phaeochromogenes
Author(s) -
van Pée Karl-Heinz,
Lingens Franz
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)81005-4
Subject(s) - pyrrole , chemistry , enzyme , streptomyces , streptomyces aureofaciens , halogenation , chloramphenicol , biochemistry , stereochemistry , antibiotics , bacteria , organic chemistry , biology , genetics
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 H 2 O 2 and can also brominate monochlorodimedone, but cannot catalyze chlorination. This enzyme is the first haloperoxidase described from procaryotic sources.