Nitrilase

nitrilase 1
Identifiers
Symbol	NIT1
Entrez	4817
HUGO	7828
OMIM	604618
PDB	3IVZ
RefSeq	NM_005600
UniProt	Q86X76
Other data
Locus	Chr. 1 pter-qter

Nitrilase enzymes (nitrile aminohydrolase; EC 3.5.5.1) catalyse the hydrolysis of nitriles to carboxylic acids and ammonia, without the formation of "free" amide intermediates. Nitrilases are involved in natural product biosynthesis and post translational modifications in plants, animals, fungi and certain prokaryotes. Nitrilases can also be used as catalysts in preparative organic chemistry. Among others, nitrilases have been used for the resolution of racemic mixtures. Nitrilase should not be confused with nitrile hydratase (nitrile hydro-lyase; EC 4.2.1.84) which hydrolyses nitriles to amides. Nitrile hydratases are almost invariably co-expressed with an amidase, which converts the amide to the carboxylic acid. Consequently, it can sometimes be difficult to distinguish nitrilase activity from nitrile hydratase plus amidase activity.

Nitrilase was first discovered in the early 1960s for its ability to catalyze the hydration of a nitrile to a carboxylic acid. Although it was known at the time that nitrilase could operate with wide substrate specificity in producing the corresponding acid, later studies reported the first NHase (nitrile hydratase) activity exhibited by nitrilase. That is, amide compounds could also be formed via nitrile hydrolysis. Further research has revealed several conditions that promote amide formation, which are outlined below.

Below is a list of steps involved in transforming a generic nitrile compound with nitrilase:

Most nitrilases are made up of a single polypeptide ranging from 32-45 kDa, and its structure is an ⍺-β-β-⍺ fold. The favored form of the enzyme is a large aggregate consisting of 6-26 subunits. Nitrilase exploits the lys-cys-glu catalytic triad which is essential for its active site function and enhancing its performance.

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