Nitrilase

[1] Nitrilases are involved in natural product biosynthesis and post translational modifications in plants, animals, fungi and certain prokaryotes.

[6] In order to dimerize, the C-terminals of each subunit extend out from the core and interact with each other, and this is largely made possible by the salt bridges formed between arginine and glutamate residues.

[6] Although the exact binding mechanism to the nitrile substrate still remains unknown, by drawing comparisons between the sequence and structure with other nitrilases, the catalytic triad was determined to consist of Glu 42, Lys 113, and Cys 146.

[8][10] Nitrilases have critical roles in plant-microbe interactions for defense, detoxification, nitrogen utilization, and plant hormone synthesis.

NIT1, 2, and 3 of the A. thaliana species are examples of the first group of plant nitrilases (arylacetonitrilases) which hydrolyze the nitriles produced during the synthesis or degradation of cyanogenic glycosides and glucosinolates.

[11][14] Other bacterial applications of nitrilases produced by plant-associated microorganisms include the degradation of plant nitriles for a carbon and nitrogen source.

The conversion of a general nitrile to either an amide or carboxylic acid is facilitated by nitrilase. [ 5 ] [ 1 ]
The active site of a thermoactive nitrilase from Pyrococcus abyssi, detailing the Lys-Cys-Glu catalytic triad responsible for cleaving C-N bonds. Unfortunately, attempts to crystallize the enzyme with either fumaro- or malononitrile have been ineffective so the binding motif remains unknown. [ 6 ]