| 5-aminopentanamidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.1.30 | ||||||||
| CAS no. | 9054-60-8 | ||||||||
| 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 5-aminopentanamidase (EC 3.5.1.30) is an enzyme that catalyzes the chemical reaction
- 5-aminopentanamide + H2O 5-aminopentanoate + NH3
5-aminopentanoate + NH3Thus, the two substrates of this enzyme are 5-aminopentanamide and H2O, whereas its two products are 5-aminopentanoate and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is 5-aminopentanamide amidohydrolase. Other names in common use include 5-aminovaleramidase, and 5-aminonorvaleramidase. This enzyme participates in lysine degradation.
References
- Reitz MS, Rodwell VW (1970). "Delta-aminovaleramidase of Pseudomonas putida". J. Biol. Chem. 245 (12): 3091–6. PMID 5432799.
- Takeda H, Yamamoto S, Kojima Y, Hayaishi O (1969). "Studies on monooxygenases. I. General properties of crystalline L-lysine monooxygenase". J. Biol. Chem. 244 (11): 2935–41. PMID 5772467.
| 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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