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Spermine synthase (EC 2.5.1.22, spermidine aminopropyltransferase, spermine synthetase) is an enzyme that converts spermidine into spermine.[1][2] This enzyme catalyses the following chemical reaction
- S-adenosylmethioninamine + spermidine S-methyl-5'-thioadenosine + spermine
| Spermine synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.5.1.22 | ||||||||
| CAS no. | 74812-43-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Spermine synthase is an enzyme involved in polyamine biosynthesis. It is present in all eukaryotes and plays a role in a variety of biological functions in plants[3] Its structure consists of two identical monomers of 41 kDa with three domains each, creating a homodimer formed via dimerization. The interactions between one of the three domains, the N-terminals of the monomers, is responsible for dimerization as that is where the active site is located; the central terminal consisting of four β- strands structurally forming a lid for the third domain, the C-terminal domain.[4]
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