Mandelonitrile lyase

[5] HNLs are peculiar in that, within the same organism and even the same sample, there exist a variety of different isoforms of this enzyme.

It is understood that this is the case because the N-terminal fold is a region known to bind FAD as a needed cofactor.

Also curious is that FAD plays no observed role in active site oxidation-reduction reactions of this enzyme.

HNLs are known to be stereospecific, giving the action of this enzyme a major advantage in effectively creating precursors essential to the metabolic development of amino acids and a wide range of clinically relevant small molecules.

Figures 2 and 3 detail the typical synthetic and solved biochemical mechanisms for the formation of this key metabolic intermediate.

In addition, most of the synthetic methods for facilitating this set of reactions take place in organic solvent, whereas it has been shown that HNL activity is highest at a polar-nonpolar interface.

[18] The importance of these mandelonitrile synthons makes the HNL class of enzymes a major target for controlled catalysis that has been optimized through work at the interface of polar and non-polar solvent conditions.

Figure 1: Model of mandelonitrile lyase based on PDB entry 1JU2
Figure 2: The general organic chemistry synthetic pathway for mandelonitrile. [ 8 ]
Figure 3: Generalized scheme for the enzymatic cycle and action of HNL. R group indicates a benzene ring. [ 1 ] [ 9 ] [ 10 ] [ 11 ] [ 12 ]