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Characterization of a tyrosinase from Amanita muscaria involved in betalain biosynthesis

Characterization of a tyrosinase from Amanita muscaria involved in betalain biosynthesis

Phytochemistry 42(6): 1511-1515

A tyrosinase was characterized from the betalain-containing pileus of the mushroom Amanita muscaria. The enzyme was located exclusively in the coloured parts of the mushroom and hydroxylated tyrosine to 3-(3,4-dihydroxyphenyl)-alanine (DOPA), suggesting that it is involved in betalain biosynthesis. The tyrosinase was not specific for tyrosine, and in addition to the monophenolase activity, the enzyme also oxidized diphenols to o-quinones (diphenolase activity). The native enzyme appeared to be a heterodimer of two subunits with M-rs of 27000 and 30000, which is unusual for tyrosinases. Typical tyrosinase inhibitors such as tropolone, 2-mercaptobenzothiazole and benzoic acid strongly inhibited the enzyme.

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Accession: 002775440

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DOI: 10.1016/0031-9422(96)00171-9

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