SUMMARY: A new bromoperoxidase-catalase was purified from the chloramphenicol-producing actinomy-cete ISP 5230. The homogeneous enzyme showed brominating activity, catalase activity and a very low peroxidase activity. The spectral properties and pH dependence of the catalase activity showed similarities to conventional catalases. In contrast to other haem-bromoperoxidases, the bromoperoxidase-catalase was stable when treated with an ethanol/ chloroform mixture. Gel filtration gave an estimated of 127000-136000. SDS-PAGE showed a single band corresponding in mobility to a species with an of 61000. The pI was estimated to be 4·5. The bromoperoxidase-catalase was not present in active form in a mutant of ISP 5230, blocked in the chlorination step of chloramphenicol biosynthesis. However, an inactive species of the enzyme was detected in crude extracts of the mutant by using antibodies. From these results it is concluded that this bromoperoxidase participates in the chlorination step during chloramphenicol biosynthesis.


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