Hydroxynitrile lyases: Functions and properties
Version of Record online: 28 APR 2006
Volume 98, Issue 4, pages 891–898, December 1996
How to Cite
Hickel, A., Hasslacher, M. and Griengl, H. (1996), Hydroxynitrile lyases: Functions and properties. Physiologia Plantarum, 98: 891–898. doi: 10.1111/j.1399-3054.1996.tb06700.x
- Issue online: 28 APR 2006
- Version of Record online: 28 APR 2006
- Received 19 June, 1996
- Biochemical properties;
- enzyme mechanism;
- hydroxynitrile lyase;
- industrial application
Plant hydroxynitrile lyases (Hnl) have attracted the attention of bioorganic scientists for more than 90 years. However, the most important increase in knowledge of this class of enzymes has only arisen in the recent decade. The industrial application of these enzymes as biocatalysts for the synthesis of enantiomerically pure α-cyanohydrins may be responsible for the growing interest in this area.
The Hnls are involved in the catabolic degradation of cyanogenic glycosides, releasing HCN which serves as defense agent against herbivores and microbial attack, or as a nitrogen source. Hydroxynitrile lyases from various plant families appear to represent a new example of enzymes that originated from the convergent evolution of different precursor proteins. The enzymes have been classified into non-FAD- and FAD-containing proteins. FAD-containing enzymes have been isolated exclusively from the Rosaceae, whereas the FAD-independent Hnls, which are more heterogenous in structure, have been characterized from various plant families (Poaceae, Euphorbiaceae, Linaceae, Olacaceae. Filitaceae). The aim of this review is to present a general survey of the natural function and localization of this class of enzymes and a comprehensive summary of the biochemical and genetic data of the isolated proteins.