Aliphatic nitrilase
From Wikipedia, the free encyclopedia
In enzymology, an aliphatic nitrilase (EC 3.5.5.7) is an enzyme that catalyzes the chemical reaction
- R-CN + 2 H2O R-COOH + NH3
Thus, the two substrates of this enzyme are R-CN and H2O, whereas its two products are 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. The systematic name of this enzyme class is aliphatic nitrile aminohydrolase. This enzyme participates in styrene degradation.
[edit] References
- IUBMB entry for 3.5.5.7
- BRENDA references for 3.5.5.7 (Recommended.)
- PubMed references for 3.5.5.7
- PubMed Central references for 3.5.5.7
- Google Scholar references for 3.5.5.7
- 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: 9000–7. PMID 1390687.
- Pace HC, Brenner C (2001). "The nitrilase superfamily: classification, structure and function". Genome. Biol. 2: REVIEWS0001. PMID 11380987.
[edit] External links
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- The CAS registry number for this enzyme class is 9024-90-2.