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- W28925361 abstract "Among mycobacteria, Mycobacterium leprae is unique in its ability to oxidize a variety of diphenols to quinones in vitro. What physiologic role o-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 in M. leprae for the utilization of other substrates, as has been reported in plants." @default.
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- W28925361 date "1985-12-01" @default.
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- W28925361 title "A possible metabolic role foro-diphenoloxidase inMycobacterium leprae" @default.
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- W28925361 doi "https://doi.org/10.1007/bf01964812" @default.
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