Aliphatic nitrilase
| aliphatic nitrilase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.5.5.7 | ||||||||
| CAS number | 9024-90-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
| |||||||||
In enzymology, an aliphatic nitrilase also known as aliphatic nitrile aminohydrolase (EC 3.5.5.7) is an enzyme that catalyzes the hydrolysis of nitriles to carboxylic acids:
- R-CN + 2 H2O R-COOH + NH3
Thus, the two substrates of this enzyme are an aliphatic nitrile (R-CN) and H2O, whereas its two products are a carboxylic acid (R-COOH) and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in nitriles. This enzyme participates in styrene degradation.
References
* Kobayashi M, Yanaka N, Nagasawa T, Yamada H (1992). "Primary structure of an aliphatic nitrile-degrading enzyme, aliphatic nitrilase, from Rhodococcus rhodochrous K22 and expression of its gene and identification of its active site residue". Biochemistry. 31 (37): 9000–7. doi:10.1021/bi00152a042. PMID 1390687.
- Pace HC, Brenner C (2001). "The nitrilase superfamily: classification, structure and function". Genome. Biol. 2 (1): REVIEWS0001. PMC 150437
. PMID 11380987.
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