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
| 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 | ||||||||
| |||||||||
- S-adenosylmethioninamine + spermidine S-methyl-5'-thioadenosine + spermine
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]
References
edit- ^ Hibasami H, Borchardt RT, Chen SY, Coward JK, Pegg AE (May 1980). "Studies of inhibition of rat spermidine synthase and spermine synthase". The Biochemical Journal. 187 (2): 419–28. doi:10.1042/bj1870419. PMC 1161808. PMID 7396856.
- ^ Pajula RL, Raina A, Eloranta T (November 1979). "Polyamine synthesis in mammalian tissues. Isolation and characterization of spermine synthase from bovine brain". European Journal of Biochemistry. 101 (2): 619–26. doi:10.1111/j.1432-1033.1979.tb19756.x. PMID 520313.
- ^ Imamura T, Fujita K, Tasaki K, Higuchi A, Takahashi H (August 2015). "Characterization of spermidine synthase and spermine synthase--The polyamine-synthetic enzymes that induce early flowering in Gentiana triflora". Biochemical and Biophysical Research Communications. 463 (4): 781–6. doi:10.1016/j.bbrc.2015.06.013. PMID 26056006.
- ^ Pegg AE, Michael AJ (January 2010). "Spermine synthase". Cellular and Molecular Life Sciences. 67 (1): 113–21. doi:10.1007/s00018-009-0165-5. PMC 2822986. PMID 19859664.
External links
edit
- Spermine+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- EC 2.5.1.22
- SMS
.svg){kind=small} | This biochemistry article is a stub. You can help Wikipedia by expanding it. |