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DeutschCyanoalanine nitrilase
| cyanoalanine nitrilase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.5.4 | ||||||||
| CAS no. | 85638-44-4 | ||||||||
| 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 / QuickGO | ||||||||
| |||||||||
In enzymology, a cyanoalanine nitrilase (EC 3.5.5.4) is an enzyme that catalyzes the chemical reaction
- 3-cyano-L-alanine + 2 H2O L-aspartate + NH3
Thus, the two substrates of this enzyme are 3-cyano-L-alanine and H2O, whereas its two products are L-aspartate 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 3-cyano-L-alanine aminohydrolase. This enzyme is also called beta-cyanoalanine nitrilase. This enzyme participates in cyanoamino acid metabolism.
References
[edit]- Yanase H, Sakai T, Tonomuro K (1983). "Purification, crystallization and some properties of beta-cyano-L-alanine-degrading enzyme in Pseudomonas sp. 13". Agric. Biol. Chem. 47 (3): 473–482. doi:10.1271/bbb1961.47.473.
