Ricinine nitrilase
| ricinine nitrilase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.5.5.2 | ||||||||
| CAS number | 9075-40-5 | ||||||||
| 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, a ricinine nitrilase (EC 3.5.5.2) is an enzyme that catalyzes the chemical reaction
- ricinine + 2 H2O 3-carboxy-4-methoxy-N-methyl-2-pyridone + NH3
Thus, the two substrates of this enzyme are ricinine and H2O, whereas its two products are 3-carboxy-4-methoxy-N-methyl-2-pyridone 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 ricinine aminohydrolase. This enzyme participates in nitrogen metabolism.
References
- ROBINSON WG, HOOK RH (1964). "RICININE NITRILASE. I. REACTION PRODUCT AND SUBSTRATE SPECIFICITY". J. Biol. Chem. 239: 4257–62. PMID 14247679.
- HOOK RH, ROBINSON WG (1964). "RICININE NITRILASE. II. PURIFICATION AND PROPERTIES". J. Biol. Chem. 239: 4263–7. PMID 14247680.
- Pace HC, Brenner C (2001). "The nitrilase superfamily: classification, structure and function". Genome. Biol. 2 (1): REVIEWS0001. PMC 150437
. PMID 11380987.
This article is issued from Wikipedia - version of the 8/10/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.