A possible metabolic role for o-diphenoloxidase in Mycobacterium leprae.
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.
D000818:Animals; D001135:Armadillos / Q000382:microbiology; D001426:Bacterial Proteins / Q000378:metabolism / Q000502:physiology*; D001487:Basidiomycota / Q000201:enzymology; D004156:Catechol Oxidase / Q000378:metabolism / Q000502:physiology*; D004295:Dihydroxyphenylalanine / Q000378:metabolism; D006801:Humans; D008543:Melanins / Q000096:biosynthesis; D008545:Melanoma / Q000201:enzymology; D014442:Monophenol Monooxygenase / Q000378:metabolism; D009166:Mycobacterium leprae / Q000302:isolation & purification / Q000378:metabolism*; D009243:NAD / Q000378:metabolism; D009249:NADP / Q000378:metabolism; D010084:Oxidation-Reduction; D010636:Phenols / Q000378:metabolism; D011809:Quinones / Q000096:biosynthesis; D013379:Substrate Specificity
D001426:Bacterial Proteins; D008543:Melanins; D010636:Phenols; D011809:Quinones; D009243:NAD; D009249:NADP; D004295:Dihydroxyphenylalanine; D004156:Catechol Oxidase; D014442:Monophenol Monooxygenase