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Phytochemistry. 2009 Oct-Nov;70(15-16):1680-6. doi: 10.1016/j.phytochem.2009.07.028. Epub 2009 Aug 19.

Evolution of nitrilases in glucosinolate-containing plants.

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1
Department of Plant Physiology, Ruhr-Universit├Ąt Bochum, 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 beta-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 beta-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.

PMID:
19698961
DOI:
10.1016/j.phytochem.2009.07.028
[Indexed for MEDLINE]
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