Mandelonitrile lyase

In enzymology, a mandelonitrile lyase is an enzyme that catalyzes the chemical reaction


 * mandelonitrile $$\rightleftharpoons$$ cyanide + benzaldehyde

Hence, this enzyme has one substrate, mandelonitrile, and two products, cyanide and benzaldehyde.

This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is mandelonitrile benzaldehyde-lyase (cyanide-forming). Other names in common use include hydroxynitrile lyase, (R)-oxynitrilase, oxynitrilase, D-oxynitrilase, D-alpha-hydroxynitrile lyase, and mandelonitrile benzaldehyde-lyase. This enzyme participates in cyanoamino acid metabolism. It has 2 cofactors: flavin, and Flavoprotein.

Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code.