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. 1988 Dec 1;256(2):681–684. doi: 10.1042/bj2560681

Chemical and enzymic oxidation by tyrosinase of 3,4-dihydroxymandelate.

J Cabanes 1, A Sanchez-Ferrer 1, R Bru 1, F García-Carmona 1
PMCID: PMC1135465  PMID: 3146978

Abstract

Tyrosinase usually catalyses the conversion of monophenols into o-diphenols and the oxidation of diphenols to the corresponding o-quinones. Sugumaran [(1986) Biochemistry 25, 4489-4492] has previously proposed an unusual oxidative decarboxylation of 3,4-dihydroxymandelate catalysed by tyrosinase. Our determination of the intermediates involved in the reaction demonstrated that 3,4-dihydroxybenzaldehyde is not the first intermediate appearing in the medium during the enzymic reaction. Re-examination of this new activity of tyrosinase has demonstrated that the product of the enzyme action is the o-quinone, which, owing to its instability, evolves to the final product, 3,4-dihydroxybenzaldehyde, by a chemical reaction of oxidative decarboxylation.

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Selected References

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