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A possible metabolic role for o-diphenoloxidase in Mycobacterium leprae

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Summary

Among mycobacteria,Mycobacterium leprae is unique in its ability to oxidize a variety of diphenols to quinones in vitro. What physiologic roleo-diphenoloxidase has in the organism remained unknown. Reducing substrates like NADPH, NADH and ascorbic acid reacted with the quinone formed from dopa (3,4-dihydroxyphenylalanine); the substrates were oxidized and the quinone was reduced back to diphenol in the process. Since the quinone undergoes reversible oxidation-reduction, diphenoloxidase might serve as an alternative respiratory mechanism inM. leprae for the utilization of other substrates, as has been reported in plants.

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Authors and Affiliations

  1. Biochemistry Research Department, National Hansen's Disease Center, 70721, Carville, Louisiana, USA

    K. Prabhakaran & E. B. Harris

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  1. K. Prabhakaran
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  2. E. B. Harris
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Prabhakaran, K., Harris, E.B. A possible metabolic role for o-diphenoloxidase in Mycobacterium leprae. Experientia 41, 1571–1572 (1985). https://doi.org/10.1007/BF01964812

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