Plant Physiol.
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Purification and Characterization of a NADPH-Dependent Aldehyde Reductase from Mung Bean That Detoxifies Eutypine, a Toxin from Eutypa lata1

Ségolène Colrat, Alain Latché, Monique Guis, Jean-Claude Pech, Mondher Bouzayen, Jean Fallot, and Jean-Paul Roustan*

Ecole Nationale Supérieure Agronomique Unité, Associée, Institut National de la Recherche Agronomique, BP 107, 31326 Castanet-Tolosan cedex, France

Eutypine (4-hydroxy-3-[3-methyl-3-butene-1-ynyl] benzaldehyde) is a toxin produced by Eutypa lata, the causal agent of eutypa dieback in the grapevine (Vitis vinifera). Eutypine is enzymatically converted by numerous plant tissues into eutypinol (4-hydroxy-3-[3-methyl-3-butene-1-ynyl] benzyl alcohol), a metabolite that is nontoxic to grapevine. We report a four-step procedure for the purification to apparent electrophoretic homogeneity of a eutypine-reducing enzyme (ERE) from etiolated mung bean (Vigna radiata) hypocotyls. The purified protein is a monomer of 36 kD, uses NADPH as a cofactor, and exhibits a Km value of 6.3 µM for eutypine and a high affinity for 3- and 4-nitro-benzaldehyde. The enzyme failed to catalyze the reverse reaction using eutypinol as a substrate. ERE detoxifies eutypine efficiently over a pH range from 6.2 to 7.5. These data strongly suggest that ERE is an aldehyde reductase that could probably be classified into the aldo-keto reductase superfamily. We discuss the possible role of this enzyme in eutypine detoxification.

*   Corresponding author; e-mail roustan{at}flora.ensat.fr; fax 33-5-62-19-39-01.

Plant Physiol. (1999) 119: 621-626
Copyright Clearance Center:   0032-0889/99/119//06
© 1999 American Society of Plant Physiologists






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