Nitrilase

nitrilase 1
Crystallographic structure of Pyrococcus abyssi 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 is a polypeptide consisting of alpha helices and beta sheets. It is 262 residues in length and its structure was determined through x-ray diffraction. The structure of nitrilase shown has a resolution of 1.57 Å or 0.157 nm. Nitrilase is an enzyme and therefore requires a ligand in order for it to become active. Magnesium ion is the ligand that is a tightly bound to the enzyme to allow for this activation.^[2]

Nitrilases are naturally found in some foods, notably barley.

References

1. PDB: 3IVZ​; Raczynska, J. E.; Vorgias, C. E.; Antranikian, G.; Rypniewski, W. (2011). "Crystallographic analysis of a thermoactive nitrilase". Journal of Structural Biology 173 (2): 294–302. doi:10.1016/j.jsb.2010.11.017. PMID 21095228.
2. Protein Data Bank

External links

• nitrilase at the US National Library of Medicine Medical Subject Headings (MeSH)