+ electron
acceptor
Spermidine dehydrogenase
| Spermidine dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.5.99.6 | ||||||||
| CAS no. | 9076-64-6 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Spermidine dehydrogenase (EC 1.5.99.6) is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme are spermidine, an electron acceptor, and water. Its products are 1,3-diaminopropane, 4-aminobutanal, and the correcponding reduced acceptor.[1][2][3]
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donor with other acceptors. The systematic name of this enzyme class is spermidine:acceptor oxidoreductase. This enzyme is also called spermidine:(acceptor) oxidoreductase. This enzyme participates in urea cycle and metabolism of amino groups and beta-alanine metabolism. It has 2 cofactors: flavin adenine dinucleotide, and heme.[1]
References
- 1 2 Enzyme 1.5.99.6 at KEGG Pathway Database.
- ↑ Tabor CW, Kellogg PD (1970). "Identification of flavin adenine dinucleotide and heme in a homogeneous spermidine dehydrogenase from Serratia marcescens". J. Biol. Chem. 245 (20): 5424–33. doi:10.1016/S0021-9258(18)62772-3. PMID 4918845.
- ↑ Tabor H; Tabor CW (1972). "Biosynthesis and metabolism of 1,4-diaminobutane, spermidine, spermine, and related amines. IIE2a Speridine dehydrogenase". Adv. Enzymol. Relat. Areas Mol. Biol. 36: 225–226.