| ricinine nitrilase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.5.2 | ||||||||
| CAS no. | 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 / QuickGO | ||||||||
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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
3-carboxy-4-methoxy-N-methyl-2-pyridone + NH3Thus, 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. doi:10.1186/gb-2001-2-1-reviews0001. PMC 150437. PMID 11380987.
| Hydrolases: carbon-nitrogen non-peptide (EC 3.5) | |
|---|---|
| 3.5.1: Linear amides / Amidohydrolases | |
| 3.5.2: Cyclic amides/ Amidohydrolases | |
| 3.5.3: Linear amidines/ Ureohydrolases | |
| 3.5.4: Cyclic amidines/ Aminohydrolases | |
| 3.5.5: Nitriles/ Aminohydrolases | |
| 3.5.99: Other | |
| Enzymes | |
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| Activity | |
| Regulation | |
| Classification | |
| Kinetics | |
| Types |
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