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Biochem Biophys Res Commun. 1993 Dec 15;197(2):619-24.

Isolation of a new tautomerase monitored by the conversion of D-dopachrome to 5,6-dihydroxyindole.

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Department of Pharmacology, University of Lund, Sweden.


Two membrane bound enzymes which tautomerize L-dopachrome and are specific for the L-isomer of dopachrome have been defined in melanin forming cells. Another enzyme that tautomerizes D-dopachrome with concomitant decarboxylation to give 5,6-dihydroxyindole (DHI) was found in the cytoplasm of human melanoma cells, human liver and in all of the organs studied in rat. The decolorization of D-dopachrome with the formation of DHI was used in monitoring the isolation of a tautomerase from liver of male rats and therefore the enzyme is provisionally called D-dopachrome tautomerase. The molecular weight of D-dopachrome tautomerase monomer was approximately 12 kD and its N-terminal amino acid sequence was P-F-V-E-L-E-T-N-L-P-A-. The Km for D-dopachrome was 1.5 mM and Vmax 0.5 mmol per min and mg protein.

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