Acetylspermidine deacetylase
| acetylspermidine deacetylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.1.48 | ||||||||
| CAS no. | 67339-07-5 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, an acetylspermidine deacetylase (EC 3.5.1.48) is an enzyme that catalyzes the chemical reaction
- N8-acetylspermidine + H2O acetate + spermidine
Thus, the two substrates of this enzyme are N8-acetylspermidine and H2O, whereas its two products are acetate and spermidine.
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 N8-acetylspermidine amidohydrolase. Other names in common use include N8-monoacetylspermidine deacetylase, N8-acetylspermidine deacetylase, N-acetylspermidine deacetylase, N1-acetylspermidine amidohydrolase (incorrect), and 8-N-acetylspermidine amidohydrolase.
References
[edit]- Libby PR (1978). "Properties of an acetylspermidine deacetylase from rat liver". Arch. Biochem. Biophys. 188 (2): 360–3. doi:10.1016/S0003-9861(78)80020-4. PMID 28089.
- Blankenship J (1978). "Deacetylation of N8-acetylspermidine by subcellular fractions of rat tissue". Arch. Biochem. Biophys. 189 (1): 20–7. doi:10.1016/0003-9861(78)90109-1. PMID 708044.
- Marchant P, Manneh VA, Blankenship J (1986). "N1-acetylspermidine is not a substrate for N-acetylspermidine deacetylase". Biochim. Biophys. Acta. 881 (2): 297–9. doi:10.1016/0304-4165(86)90017-6. PMID 3955076.
