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- W1999826972 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." @default.
- W1999826972 created "2016-06-24" @default.
- W1999826972 creator A5022168725 @default.
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- W1999826972 date "2009-10-01" @default.
- W1999826972 modified "2023-10-18" @default.
- W1999826972 title "Evolution of nitrilases in glucosinolate-containing plants" @default.
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- W1999826972 doi "https://doi.org/10.1016/j.phytochem.2009.07.028" @default.
- W1999826972 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19698961" @default.
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