Phytochemistry p. 567 - 569 (1997)
Update date:2022-09-26
Topics:
Mueller, Lukas A.
Hinz, Ursula
Zryd, Jean-Pierre
DOPA-dioxygenase from Amanita muscaria is known to catalyse the conversion of 3-(3,4-dihydroxyphenyl)alanine (DOPA) to betalamic acid in the key reaction of betalain biosynthesis. In this work, we re-examined the reactivity of DOPA-dioxygenase using a cDNA clone encoding active DOPA- dioxygenase the kinetic parameters of which were comparable to those of the native enzyme. Using L-DOPA as a substrate, the enzyme catalysed the formation of two products. In addition to betalamic acid, the enzyme also catalysed the formation of muscaflavin, a compound that occurs naturally in A. muscaria and in mushrooms of the Hygrocybe family but not in the betalain- containing plants of the order Caryophyllales. Muscaflavin arises by a 2,3- extradiol cleavage of DOPA, whereas betalamic acid is the product of a 4,5- cleavage. Our results indicate that the recombinant enzyme has both 2,3- and 4,5-dioxygenase activity, and do not support the prevailing view that the two compounds are produced by two distinct enzymes.
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