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Evolution of nitrilases in glucosinolate-containing plants
Authors:Tim Janowitz  Inga Trompetter  Markus Piotrowski
Institution:Department of Plant Physiology, Ruhr-Universität Bochum, Universitätsstraße 150, 44801 Bochum, Germany
Abstract:Nitrilases, enzymes that catalyze the hydrolysis of organic cyanides, are ubiquitous in the plant kingdom. The typical plant nitrilase is a nitrilase 4 homolog which is involved in the cyanide detoxification pathway. In this pathway, nitrilase 4 converts β-cyanoalanine, the intermediate product of cyanide detoxification, into asparagine, aspartic acid and ammonia. In the Brassicaceae, a new family of nitrilases has evolved, the nitrilase 1 homologs. These enzymes are not able to use β-cyanoalanine as a substrate. Instead, they display rather broad substrate specificities and are able to hydrolyze nitriles that result from the decomposition of glucosinolates, the typical secondary metabolites of the Brassicaceae. Here we summarize and discuss data indicating that nitrilase 1 homologs have evolved to function in glucosinolate catabolism.
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