Evolution of nitrilases in glucosinolate-containing plants
| Autor: | Markus Piotrowski, Inga Trompetter, Tim Janowitz |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Cyanide
Glucosinolates Arabidopsis Plant Science Horticulture Biochemistry Nitrilase Evolution Molecular chemistry.chemical_compound Aminohydrolases Aspartic acid Nitriles Arabidopsis thaliana Asparagine Glycosides Molecular Biology chemistry.chemical_classification biology Molecular Structure Brassicaceae General Medicine biology.organism_classification Enzyme chemistry Glucosinolate |
| Zdroj: | Phytochemistry. 70(15-16) |
| ISSN: | 1873-3700 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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